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Q8IQ70 | MSRNRAAMVSAFRLFLRPATTTTHRSLALRLAPGTTFALHLRPCHELQQHRSFASTAEDGETDKHKKPTTGEDIYVEYVNGMPHMTVRLPSRNELCQFALKPISHNVGDLLAMLRAEDRGIDRAAVINKHGVRIASSCTIESLLDDSFSIQINNRTLDVNPPKRDKVTLESMDKVGDVRKVIAQLYEAFNVGEYQLEKSNQLAKELETLRYELEPLEEKKLELSKKAARRTNFMTWMGLGLMSVQFGILARLTWWEYSWDIMEPVTYFVTYGTTMAMYAYYCVTKREYMMEDVKNREFSLSLYRNAKKVQFDVEHYNELKRKSAELEYNLRRINDPLNMQLPSHLVRTQENTPPTLTEEKAERKYT | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria . Constitutes a pore-forming and calcium-conducting subunit . Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways . Together with Itpr, has a role in oxidative stress-induced ER-mitochondria calcium transfer . During pupation, required for memory function in mushroom body neurons .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42478
Sequence Length: 366
Domain: Forms a well-packed pentamer with an overall cylindrical shape. The inner core of the pentamer is formed with the second transmembrane region and the second coiled-coil region: while the transmembrane regions pack into a five-helix bundle having a largely polar pore across the membrane, the coiled-coil outside the membrane forms a pentamer with a hydrophobic core. The inner core is wrapped by the first transmembrane region through contacts between the first and the second transmembrane regions. The second transmembrane is followed by the inner juxtamembrane region (IJMH) that orients at a wide angle relative to the second transmembrane. The two core domains are held together on the periphery by the outer juxtamembrane helix (OJMH).
Subcellular Location: Mitochondrion inner membrane
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Q8NE86 | MAAAAGRSLLLLLSSRGGGGGGAGGCGALTAGCFPGLGVSRHRQQQHHRTVHQRIASWQNLGAVYCSTVVPSDDVTVVYQNGLPVISVRLPSRRERCQFTLKPISDSVGVFLRQLQEEDRGIDRVAIYSPDGVRVAASTGIDLLLLDDFKLVINDLTYHVRPPKRDLLSHENAATLNDVKTLVQQLYTTLCIEQHQLNKERELIERLEDLKEQLAPLEKVRIEISRKAEKRTTLVLWGGLAYMATQFGILARLTWWEYSWDIMEPVTYFITYGSAMAMYAYFVMTRQEYVYPEARDRQYLLFFHKGAKKSRFDLEKYNQLKDAIAQAEMDLKRLRDPLQVHLPLRQIGEKD | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria . Constitutes the pore-forming and calcium-conducting subunit of the uniporter complex (uniplex) . Activity is regulated by MICU1 and MICU2. At low Ca(2+) levels MCU activity is down-regulated by MICU1 and MICU2; at higher Ca(2+) levels MICU1 increases MCU activity . Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. Involved in buffering the amplitude of systolic calcium rises in cardiomyocytes . While dispensable for baseline homeostatic cardiac function, acts as a key regulator of short-term mitochondrial calcium loading underlying a 'fight-or-flight' response during acute stress: acts by mediating a rapid increase of mitochondrial calcium in pacemaker cells . participates in mitochondrial permeability transition during ischemia-reperfusion injury (By similarity). Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake . Mitochondrial calcium uptake in skeletal muscle cells is involved in muscle size in adults (By similarity). Regulates synaptic vesicle endocytosis kinetics in central nerve terminal (By similarity). Involved in antigen processing and presentation (By similarity).
PTM: Phosphorylation by CaMK2 in heart leads to increased MCU current . The regulation of MCU by CaMK2 is however subject to discussion: another group was unable to reproduce these results . Phosphorylated on tyrosines by PTK2B/PYK2, promoting oligomerization .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39867
Sequence Length: 351
Domain: The N-terminal MCU domain is required for efficient Ca(2+) uptake and for interaction with MCUR1. It is not required for targeting to the mitochondria, oligomerization, interaction with MICU1 and MICU2, or assembly of the uniplex complex.
Subcellular Location: Mitochondrion inner membrane
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P53206 | MSCSQNKTSVSLAWRECISIASVLIGAYASYKYYKLFKTRDIPRPKEGVEELIGNTPLVKIRSLTKATGVNIYAKLELCNPAGSAKDRVALNIIKTAEELGELVRGEPGWVFEGTSGSTGISIAVVCNALGYRAHISLPDDTSLEKLALLESLGATVNKVKPASIVDPNQYVNAAKKACNELKKSGNGIRAVFADQFENEANWKVHYQTTGPEIAHQTKGNIDAFIAGCGTGGTITGVAKFLKERAKIPCHVVLADPQGSGFYNRVNYGVMYDYVEKEGTRRRHQVDTIVEGIGLNRITHNFHMGEKFIDESIRVNDNQAIRMAKYLSVNDGLFVGSSTAINAVAAIQVAKTLPHGSNIVIIACDSGSRHLSKFWKEAKEIDHDVSLEEVINI | Function: Putative cysteine synthase that catalyzes the conversion of O-acetyl-L-serine (OAS) into cysteine, the last step in the cysteine biosynthesis pathway. However, this CS-like protein is unlikely to function in cysteine biosynthesis. It seems that in S.cerevisiae cysteine biosynthesis occurs exclusively through the cystathionine pathway and not via direct incorporation of sulfur into OAS.
Catalytic Activity: hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 42801
Sequence Length: 393
Subcellular Location: Mitochondrion
EC: 2.5.1.47
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B9KIH0 | MRSSRSAKVSLVGAGNIGGALAHMLGASQVVKELVLVDVAGGMTEGKVLDVGQALALLGSDVYITGGSDYAAIEHSDAVVVTAGIPRKEGMSREDLLNTNAAVVRNIAENIAKYSPGALVIVVTNPLDAMVWCMYKYSGLPANRVVGMAGVLDSARFSFFLARHMNVSVSSVSAMVLGGHGDLMLPLLRYSTVGGVPVESLIESGRLNRGDIAAIVERTRKGGEEIVKLLKTGSAYCAPAASCAHMLESYVRDKRSIMPCSAYLDGQYGVRDLFVGVPVIIGEKGVEEVVEFPLTAEEQAVFDQSVELIRGSVSAIS | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 33320
Sequence Length: 317
EC: 1.1.1.37
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O08349 | MKLGFVGAGRVGSTSAFTCLLNLDVDEIALVDIAEDLAVGEAMDLAHAAAGIDKYPKIVGGADYSLLKGSEIIVVTAGLARKPGMTRLDLAHKNAGIIKDIAKKIVENAPESKILVVTNPMDVMTYIMWKESGKPRNEVFGMGNQLDSQRLKERLYNAGARNIRRAWIIGEHGDSMFVAKSLADFDGEVDWEAVENDVRFVAAEVIKRKGATIFGPAVAIYRMVKAVVEDTGEIIPTSMILQGEYGIENVAVGVPAKLGKNGAEVADIKLSDEEIEKLRNSAKILRERLEELGY | Function: Catalyzes the reversible oxidation of malate to oxaloacetate. Can also oxidize tartrate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 31874
Sequence Length: 294
Subcellular Location: Cytoplasm
EC: 1.1.1.37
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O84381 | MVSQTVSVAVTGGTGQIAYSFLFSLAHGDVFGLDCGIDLRIYDIPGTERALSGVRMELDDGAFPLLQRVQVTTSLHDAFDGIDAAFLIGSVPRGPGMERRDLLKKNGEIFATQGKALNTTAKRDAKIFVVGNPVNTNCWIAMNHAPRLLRKNFHAMLRLDQNRMHSMLSHRAEVPLSAVSQVVVWGNHSAKQVPDFTQALINDRPIAETIADRDWLENIMVPSVQSRGSAVIEARGKSSAASAARALAEAARSIYQPKEGEWFSSGVCSDHNPYGLPEDLIFGFPCRMLATGEYEVIPRLPWDAFIRGKMQISLDEILQEKASVSL | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 35708
Sequence Length: 326
EC: 1.1.1.37
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P61974 | MTESVKKIAVTGAAGQIAYSLLWRIANGDVYGKNTPVELQLLEIPQAIGGAEGVAMELLDSAFPLLKNIVVTDKAEVAFDGTNAAFLVGAKPRGKGEERADLLTANGKIFGPQGKALNDNAADDIRVLVVGNPANTNALIAQHAAKDIPADRFNAMMRLDHNRGIAQLSEKLGRDKNDIEKFVVWGNHSAGQFPDITYATIGGEAISGLVDHDWYTGEFIPRVAKRGAEIIEVRGKSSAASAASSAIDHMHDWINGTDGQWRTAAIPSDGSYGVPEGLIFGFPTISEDGQWKIVQDLELSDFQKDGIARNVTELEEEREAVKDLLG | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 34976
Sequence Length: 326
EC: 1.1.1.37
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Q8NN33 | MNSPQNVSTKKVTVTGAAGQISYSLLWRIANGEVFGTDTPVELKLLEIPQALGGAEGVAMELLDSAFPLLRNITITADANEAFDGANAAFLVGAKPRGKGEERADLLANNGKIFGPQGKAINDNAADDIRVLVVGNPANTNALIASAAAPDVPASRFNAMMRLDHNRAISQLATKLGRGSAEFNNIVVWGNHSATQFPDITYATVGGEKVTDLVDHDWYVEEFIPRVANRGAEIIEVRGKSSAASAASSAIDHMRDWVQGTEAWSSAAIPSTGAYGIPEGIFVGLPTVSRNGEWEIVEGLEISDFQRARIDANAQELQAEREAVRDLL | Function: Catalyzes the reversible oxidation of malate to oxaloacetate. Exhibits higher catalytic efficiency for oxaloacetate reduction than for malate oxidation in vitro. Almost equally active both for NADH and NADPH on the bases of the kcat values at pH 6.5, but catalytic efficiency for oxaloacetate reduction is 50-fold higher with NADH.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 34908
Sequence Length: 328
EC: 1.1.1.37
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P61897 | LRRKPGMDRSDLFNVNAGIVRNLVEQIAVTCPKACIGIITNPVNTTVAIAAEVLKKAGVYDKNKLFGVTTLDIIRSNTFVAELKGKQPQDINVPVIGGHSGVTILPLLSQVPGISFSEQEVADLTKRIQNAGTEVVEAKAGGGSATLSMGQVPG | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 16149
Sequence Length: 154
EC: 1.1.1.37
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P19980 | SKTPIRVAVTGAAGNIGYHLLFRIA | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 2626
Sequence Length: 25
EC: 1.1.1.37
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Q6L0C3 | MARSKISVIGAGAVGATVAQTLAIRQTGDIYIFDIVDGLAEGKALDILEGAPHWGYDLDIKGFCTADESKYAEMKGSDVIVVTAGLARKPGMSRDDLLLKNIGIMKSVGEAIKKYSPESKIVVVTNPADIMAYAIYKASGISPERIIGLGGSLDSTRFRTFLAQELNVSFEDVNAFVIGGHGDDMVPFIRYSNVSGIPIEDLLPREKIDEIVKRTRFGGGEIVNLYKTGSAFYAPGISIAVMVESIVNDRKRVIPCAAYITGEHSKTYLVNNLFIGVPIKIGKNGVEKIYDLKFNEDELEAWKKSVESVKKNSAIADDYFAKNQ | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 35215
Sequence Length: 324
EC: 1.1.1.37
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C0LGU7 | MGCRWNPIGFQFSCFMFLIITLQSRSSLSLESEGFVLLKFRARVDSDPHGTLANWNVSDHDHFCSWFGVTCVDNKVQMLNLSGCSLGGTLAPELSQLSELRSLILSKNKLSGDIPNEFASFAKLEFLDLRDNNLNGVVPPELNKVLTPENLLLSGNKFAGFMTVKFLRLQSLYKVQMNKNRELSSVSADVLDCVNRKLGYCVSRRSLITRNKAKAFVLRIRATSRHYMVRRESHGKNYVVNYHPSENETSIFKRRELLEETSNLAAMPAPDTPSPSPEIITIVFPRSSGSFPALTNAKKRIPPLIPPSSPPPLPTNNTIASDPPRKFEEKSKGFKDVWLYVVIGVAAFVAMLIIVAVIFFFRKRAVKSIGPWKTGLSGQLQKAFVTGVPKLNRSELETACEDFSNIIEAFDGYTVYKGTLSSGVEIAVASTAILETREWTRAMEMTYRRRIDTMSRVNHKNFINLIGYCEEDEPFNRMMVFEYAPNGTLFEHLHDKEMEHLDWNARTRIIMGTAYCLQYMHELNPPISHTKLVSSAIYLTDDYAAKVGEVPFSGQTGSKPRKPMSGDLDQSLLPLPPEPETNVYSFGVLMLEIISGKLSDSEEEGSILKWASKYLENDNLRDMIDPTLTTYKEEELEAICDVARHCLKLDESQRPKMKYVVQQLKEVINISQEQATPRLSPLWWAELEILSSEAT | Function: Involved in the pollen tube perception of the female signal.
PTM: Phosphorylated by MIK1.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 78476
Sequence Length: 695
Subcellular Location: Cell membrane
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Q9Y7M7 | MDPIRFGLSRVPFAHCYNKRVIFRANYLVPLTWLKNNVAYKSTNTLLLPTPNAEYYSTSKLSSQVNVSLNSLSQKASSGSKIYPFKNSFPLPFSRSILPIRSLAFLKLCVRHNSTVPSKDEQAQDISKINTNGTLQTPNKKVNVFRLFTLARGQGWNFFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMGIPSGTFYIGLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRLFELLDAKPKIAPTVGIPVPVTVGKAILSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANCSFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKLMRWQLGKVEP | Function: Mediates export of peptides generated upon proteolysis of mitochondrial inner membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79020
Sequence Length: 726
Subcellular Location: Mitochondrion inner membrane
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P33310 | MIVRMIRLCKGPKLLRSQFASASALYSTKSLFKPPMYQKAEINLIIPHRKHFLLRSIRLQSDIAQGKKSTKPTLKLSNANSKSSGFKDIKRLFVLSKPESKYIGLALLLILISSSVSMAVPSVIGKLLDLASESDGEDEEGSKSNKLYGFTKKQFFTALGAVFIIGAVANASRIIILKVTGERLVARLRTRTMKAALDQDATFLDTNRVGDLISRLSSDASIVAKSVTQNVSDGTRAIIQGFVGFGMMSFLSWKLTCVMMILAPPLGAMALIYGRKIRNLSRQLQTSVGGLTKVAEEQLNATRTIQAYGGEKNEVRRYAKEVRNVFHIGLKEAVTSGLFFGSTGLVGNTAMLSLLLVGTSMIQSGSMTVGELSSFMMYAVYTGSSLFGLSSFYSELMKGAGAAARVFELNDRKPLIRPTIGKDPVSLAQKPIVFKNVSFTYPTRPKHQIFKDLNITIKPGEHVCAVGPSGSGKSTIASLLLRYYDVNSGSIEFGDEDIRNFNLRKYRRLIGYVQQEPLLFNGTILDNILYCIPPEIAEQDDRIRRAIGKANCTKFLANFPDGLQTMVGARGAQLSGGQKQRIALARAFLLDPAVLILDEATSALDSQSEEIVAKNLQRRVERGFTTISIAHRLSTIKHSTRVIVLGKHGSVVETGSFRDLIAIPNSELNALLAEQQDEEGKGGVIDLDNSVAREV | Function: Mediates export of peptides with molecular masses of 2100 to 600 daltons generated upon proteolysis of mitochondrial inner membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75950
Sequence Length: 695
Subcellular Location: Mitochondrion inner membrane
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Q945K2 | MEKSTMSAILLVLYIFVLHLQYSEVHSLATTSDHDFSYLSFAYDATDLELEGSYDYVIVGGGTSGCPLAATLSEKYKVLVLERGSLPTAYPNVLTADGFVYNLQQEDDGKTPVERFVSEDGIDNVRGRVLGGTSIINAGVYARANTSIYSASGVDWDMDLVNQTYEWVEDTIVYKPNSQSWQSVTKTAFLEAGVHPNHGFSLDHEEGTRITGSTFDNKGTRHAADELLNKGNSNNLRVGVHASVEKIIFSNAPGLTATGVIYRDSNGTPHQAFVRSKGEVIVSAGTIGTPQLLLLSGVGPESYLSSLNIPVVLSHPYVGQFLHDNPRNFINILPPNPIEPTIVTVLGISNDFYQCSFSSLPFTTPPFGFFPSASYPLPNSTFAHFASKVAGPLSYGSLTLKSSSNVRVSPNVKFNYYSNLTDLSHCVSGMKKIGELLSTDALKPYKVEDLPGVEGFNILGIPLPKDQTDDAAFETFCRESVASYWHYHGGCLVGKVLDGDFRVTGINALRVVDGSTFPYTPASHPQGFYLMLGRYVGIKILQERSASDLKILDSLKSAASLVL | Function: Involved in cyanogenesis, the release of HCN from injured tissues. Catalyzes the stereospecific addition of HCN to a variety of aldehydes in vitro. Has no oxidase activity. The redox properties of the FAD cofactor appear to be unimportant for catalysis.
PTM: Glycosylated. Deglycosylation does not affect the enzymatic activity.
Catalytic Activity: (R)-mandelonitrile = benzaldehyde + hydrogen cyanide
Sequence Mass (Da): 61158
Sequence Length: 563
EC: 4.1.2.10
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P57551 | MKLFNQLRWFFVREWKRYLGAILLLIIIATLQLLPPKIVGVLIDLIIKKNMHGVQILPWILIIFLVAVIVYILRYLWRILLFGASYQLATELRVKFYTYLSQQSQIFFLKNRTGDLIARATNDVDRVVFAAGEGVLTLVDSLVMGFSVLIVMSTQISFLLTIISLIPMPIMAILIKKYGKELHETFRHAQISFSLLNNQTQEILTSIRMIRAFGLEKNQSNKFNIITRNTGKKNMEVAKIDARFDPVIYLSVAFSNLLAIIGGGWLVWNNQISIGQLTSFIMYLGLMIWPMLALAWMFNIVERGSAAWDRIHSIINKKLYIEDGKNNIPPYPGILNINIKKFYYPNNQKPSLKDIRILIKPGNTLGICGPTGSGKSTLLMLIQRQFNFKKEEIHYHSLSLLEIKIDDWRRRIAVVNQTSFLFSDTISNNISLGKPNASQKEIEEVAKLADVHKDIIDLPERYETQVGERGVMLSGGQKQRVCIARALLLNAEILILDDALSAVDAQTENNILKNINEWKKKKHSLIITTHRLSALINSDEIIVIKSGSIIQRGNHLKLIQEKNWYKSMYYYQQSEIELEDNEKTGEKNL | Catalytic Activity: ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67522
Sequence Length: 589
Subcellular Location: Cell membrane
EC: 7.6.2.2
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Q5BH33 | MTHFPVNIASDKQEFDPERWAKTPTTESSVNGENGTAPTSGLPSRHPSTGISVLIVGAGMGGLMTALECWRKGHDVAGILERSEGPVYSGDIIVMQPSAVSIIRHWPDMLHDMKAEQVHAVVSYETHDGRHIYGPTVPSFNDPEHLETRKGPFVAPAQVRRKFYRMLLRQVARCGLRVEYGKTVKSYFEDEKDGKGGVIIATTGEAEVRVADIVVAADGLKSPSEILIAGQHVPPRSSGLSIYRTAFPKDLAMQNELVRKRWSDSPPIWEYWLGPGMYLGVFVGDDIISFGFTPRDDIVEGTATESWEPDTDPETVAQAMLSGAGDWDPAVLALIRSAPKGAIVHWPLLWRDLRREWTSPAGRVVQVGDSAHSFIPTSGNGGSQALEDAITLATCLQLAGSSQRAYLGTKIYNLLRYERVSCAQKMSFVNSQLKTGTDWDAIWKDPAKIRTRFPKWIFQHDPEAYAYEKFGEAFAHLLDGREFVNTNYPPGHEFRAWTVEEVWRNIADGKRVEDLLDGDWS | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG . The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG . The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone . The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL . These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin . Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps .
Sequence Mass (Da): 57864
Sequence Length: 521
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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Q5BH31 | MAQPQQHKGGYKQINKALNICAFEDYLSAQLKHLPQLADVEQLSPRVIRVLGQNAGKGTNTYIVGTGPQRLIIDTGQGIPEWADILDATLKERSISLSHVFLSHWHGDHTGGVPDLLRLYPNLAGAIYKNSPGSDQQPIDDGQVFRVEGATIRAVHGPGHSHDHMCFILEEENAMFTGDNVLGHGTSAVEELGVYMETLRKLNSHHCAVGYPAHGDVITNLPAKIAGELAQKMRREKQVLLTLDRINKESRRTGQVVLVHGDGIDEEVRKMALEPFIDEVLRKLAEDGKVAFEMRGGVKRWFGVGVL | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Atrochrysone carboxyl ACP thioesterase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG . The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG . The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone . The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL . The short chain dehydrogenase mdpC converts the tautomers of emodin hydroquinone into the 3-hydroxy-3,4-dihydroan-thracen-1(2H)-one derivative . These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin . Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps .
Catalytic Activity: atrochrysone carboxyl-[ACP] + H2O = atrochrysone carboxylate + H(+) + holo-[ACP]
Sequence Mass (Da): 33839
Sequence Length: 307
Pathway: Secondary metabolite biosynthesis.
EC: 3.1.2.-
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P9WEV9 | MASLTTLKNTAIVTGSFLSGAMITLSTITVPVLLETSTHPPQLLHQWVRTYHYGHISLPTISIATAILYFYIAAYQGAREQPWRKAALVGFLTIVMVPFTWIVMSSTNGMLFGLEAGNRDHSQFFEQGANRSGLKGANSSQSHGLGNVSVGIGVEMATLEGVRELLVRWKWMHLVRSLFPLMAAVLGVGICV | Function: Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG . The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG . The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone by mdpH-1 and mdpH-2 . Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL . These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin . Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps .
Catalytic Activity: emodin anthrone + O2 = emodin + H(+) + H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20918
Sequence Length: 192
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.10.3.-
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A8AGX5 | MFYWILLALAIAAEITGTLSMKWASVSNGNTGFILMLVMITLSYIFLSFAVKKIALGVAYALWEGIGILFITLFSVLLFDEALSAMKIAGLVTLVFGIALIKSGTRKPVNAAKEATHAAV | Function: Catalyzes the excretion of spermidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12860
Sequence Length: 120
Subcellular Location: Cell inner membrane
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Q6FT96 | MTDQISHLGKTLSTAASVLIGSQDIEKNVENNLLSNSPRNPYRKTLQESLTAADFMNHETFDKLRKTRAIASTLSEDSKGLYSQRSREKYFTNKVSDKKTTFKVLSHLSDDLLKDLPETAESKSNTRDQGETKLLKESDSTDASQERIFSLYQGFEASIPVINRSVEKEHLLLEQNNQESAAQILPQMGNKPRIRSGPWEDLLESKEDTYISLDFNPERISNIKSKKELERINELANNNLVMLDIRKKLSADEIDEIKKQIQDLQLKQNLLVKKIAAIEENELFLEDIIRLIGHRSADFSNDTQIEFDQAKSLSGLNNPESMIDATRPTALERKNSIDIVETSLNEIRTSFDGSKQSIEGKDNHNALNGFFEDASNKKSRKAQPTVQKYYNSGKKLSTIPKAHDDAITCLDFDPHFSTLCTAGYMDHIVKLWDYTKKRQIGAMEGHVATISCMQVDKNYNMVATGSKDATVKLWNANDVIGRYEEGNNSEALHTLDAHLDEVSSLYIDGANLMTASQDKTIRRWDLYSGKCIQVFDVNFPSLSAYKSSFMKSNEDSMILKTVNTPIIGSIQSFDAALATGTKDGLIRLWDMRTGEVVRVLEGHMDAITSLKFDATTIISGSLDGTIRLWDLRSNNLTDIISYEKPISSLDFDAKHIVVASNEHNTHIYDRNDGNKWDLQDEEQDTTSLFVKYKERYTMEGRSNGDIGIWIV | Function: Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 80326
Sequence Length: 711
Subcellular Location: Mitochondrion outer membrane
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P0CS45 | MANHHDHDKPLRSALDPISSPYFSSLNGTLSIAKEVLIGPFQGDHRRSESARILSDLAPSLMQPRFLNAASSSQQSLSKSSHPGAPYPLLRLPTNLPFNKSSRPTASSLAILEAVDNLASLSLGDVSHPQNGQNSPSLIRGFKATIPSSELAKQRRRMVRGGIVDEDLGGKIGLKKLGDRARGLLTEKGEDEEDGELGVGRHAVKKRRKKRESRRFTEGRHLEGKLRLEDLAKQADEIGQDKENLHVRQSLIQSEIAEVGAKIDALEDIRRHLEASLLHLQEEDLELDDELEGVQELMASPAIKAAAGAKSLPLSSSGAGISNKSSRRRKGPAFLPSEHDELPSGVAFMTLNGHTAPITALDFDEPYGMLVTAGQDDVVKVWDLCDGEEIGQLRGHRGTVKALQVEDTLCLTGGADGNVRLWDLRMVEDYEERLHTQLAELARQDPLERIAEQRAHEEDGEHAEQDDELPDGTLQDPQPGDGSPCVRTLEGHSKSVTSLYYEDGCLVTGSSDKTIRQWDVATGQCVLTMDILWAISNPPPPPSSVPPQRPPRLSHRSSTSFGSNTYEDILPSPGASLVGMSGAALLGAATGQNFAVPTPPYADGTWEMYQDFVGGVQFWGYALASGSGDGGVRMWDMRTGQAHRTLIGHTAPVTCLQFDEQYIVTGSLDRTVRIWDLRMGSVSEVHKYEYPVTALQFDSRKVVACTGENGVEVYNRTTHAHSRLVVNGHTKPAEKMRFIDKYLVSGGRDGCAKVWAM | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 82615
Sequence Length: 757
Subcellular Location: Mitochondrion outer membrane
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Q5AXW3 | MDKHRRDDSPSGLSDIVERDGLLGTGITSRHIEAFGRKVTSTAGHLMGPSGDPSTSTHYQNAMVDIHRELRRPSTQRKVFALAQTTPTDLVRSKLSTSEIQSRAISSLPDELLLNIPDDTSSYSLFEGFQATQNDHEYRKAHRRGRSKGKKLLKDKDGEQADPPSTLTELKKERDLLSRRMELMGVRKNMCSSEIVDIDNKIANFHRMRQIVLDRLAGLEMEEAELEHEVNEIDNKLDDMAEEEAAQAAQAAAAAAAATTAGSETHEEPASEDPAMDASFMSESIYQKLPSPRSLKHRSIRKRSMPVLHEHFAPGSEIKEFQAHTDVVTALDLDYPFGTMITAALDDTVRVWDLNIGRCTGFLEGHNASVRCLQIEDNVVATGSMDATVKLWDLSRARTTHRDNRVNKDEDDDAVSVAYSTSLEDCHVYSLDAHVGEVTALHFKGNTLVSGSADKTLRHWDLVKGRCVQTLDVLWAAAQASSLGNESQWRPSGRLPDASADFVGAVQCFDAALACGTADGMVRLWDLRSGQVHRSLVGHTGPVSCLQFDDVHLVTGSLDRSIRIWDLRMGSIYDAYGYDKPVTSMMFDTKRIVAAAGENVVKVYDKADGHHWDCGAGVGADETGPDPAIVERVRLKDGFLIEGRRDGIVAAWTC | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 72066
Sequence Length: 654
Subcellular Location: Mitochondrion outer membrane
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A4RJV3 | MASPEDENPFQDDPGQEDEDGSILSPRGLEAFSRKVTTTASHLMGPVVDPSSSGHYQSAMTEVQKHLRRPNLQRSMFSMARTTPSDLVRSKLSTREIQHRALAHVPDDMLANIPEDDNNSYSLFQGFQASFPELTDEGKKHRRRVSRGRKLLDEGPTTPENGTTGLQKLRKERASMSHELEMLGIRKNMASSEIREIDIKIANLHGMRRIILERLAALEQEETLLEHDLMEVEARVEDAQMLADEAESTAQQSSPRDTDDADAEDNDGFMSQSIYEKIPSAASTPSKSRKPRIVRRKSMAVLHEHFEPGTSIRELRAHQDCITAMDFDAPFGTLVSAAMDDSVKVWDLNAGRCIGSLEGHTASVRALQVEDNILATGSRDATVRLWDLSKAHYDPHGSHYNGGDDDDDAMAFENPDDQPVDPPAGSMADCPLFTLSSHMDEVTALHFKGDTLVSGSSDKTIRQWDLVKGRCVQTLDVMWAAAQASVSLGTGDGAWRQTARSQAEDADFVGAVQVFDAALACGTADGMVRLWDLRSGQVHRNLVGHTGPVTALQFDNMHLVTGSHDRSIRIWDLRTGSIFDAFAYDHPVTSMMFDARRIVSAAGEDVVKVYDKVESRQWDCGAGIKAAEEMKNPPAIVERVRIRDGYMVEGRRDGIVGIWTC | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 73100
Sequence Length: 661
Subcellular Location: Mitochondrion outer membrane
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A8PTE4 | MGSSSANKKHASTSSAPSNDVRAPHADTNRLLNDMAPQLMTPAMMNAMARISLQSTPIATTRDPFPLQRATLLLAPRFSMENPARSLARISSSLLQFSGLSKHSKSGREQQRTPITSMDVGVLEESQRILATADADLDASLDTSLLDDDNDTSDVAAAADAPVSLFRGYKATVPQVSTSKTRRRQLQASENIRRSKHEPHLLSLQELEVQDRDMLAERRNLEIRRALYHAEIVHVDAKIAALEATKASLQQKLLHVREEELELDDERQGVSELLELQRHRRAMPGGRGLDAGTVLPIGAGSSRWRKTPVFLPSEHDDLPHGIAFMSLNLETGPITALDFSEPYGTLISAALEDTVRVWDLSTGEDVGRLRGHTDTVKCLQVEDELCVSGSLDSTLRVWDLRRVDAFETACRARMEGDGQDVPEADDPCIRTLAGHSRGITALAFDHETLVSGAADKTLRQWDLETSQCVLTMDILWAMSNPSTSVDLRVPLESSAPLLDPLHGANQFAGPFSYPQPPYEDGSWEMYTDFVGSVQFWGFALASGSGDGGVRLWDLRTGQAHRTLLGHTAPITCLQFDDTHLISGSLDKTIRVWDLRSGHVLETLHYDYPVTALQFDSRKIIAAAGACAVDVYNRTSEKHSSLIKHGHTAPVERLRYMDRYAVTGGRDSCIKVWSL | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74225
Sequence Length: 674
Subcellular Location: Mitochondrion outer membrane
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Q7S8R5 | MANSDQNRDVFPDDVSIDDDTSVISTRGLEAFGRKVTTTASHLIGPITDPTSHPHYQTAMTEIHKQLQKPTLQRGVFAIARTTPTDLVRSKLSSKEIQSRALAYVPDELLRNIPASSNSYSLFQGFQASFPDFTDDGKKHKRRVSRGRKMLDESPVQPGSPHAVQRLKKDKASMMHQLEMLGVRKNMASSEIREIDNKIANLHGMRKIILDRLANLEKEEAVLEHDIMDVESRLDEAQELADEAESLAMATPNKSEEDLSRTEEGFMSQSIYEKLPAANTPPGKKKPRNHRKKTLPILHEHFEPGTMIRSMRAHQDNITALDFDAPFGLMVSAAMDDSVRVWDLNAGRCIGTLEGHTASVRTLQIEDNFLATGSMDATIKLWDLSKAHYDPQGSQEVDEEDEDLAFVNPNDHAVDPPAGSMADCPLFTLEAHLDEITALHFRGDVLVSGSADKTLRQWDLTKGRCVQTLDVMWAAAQATAMGSSDGPWRQTSRSADGSADFVGALQVFESALACGTADGMVRLWDLRSGQVHRSLVGHTGPVTCLQFDDVHLVTGSLDRSIRIWDLRTGSIFDAYAYDHPITSMMFDTRRIVCAAGEDVVKVYDKVEGRHWDCGAGITEAEKAKSPAIVERVRIRDGYMVEGRQDGVVGVWTC | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 72365
Sequence Length: 653
Subcellular Location: Mitochondrion outer membrane
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Q0U2T3 | MASSFARDGSPSRGRSTSPRPRIPEESLEASLMDGLPDTRQLQAFGRKVTATAGSLIGTEGVGQHYQNALGELHRELRRPMLQRSVFSFAQTTPREIVRSRISVPEIQQRALAYVPDDMLANIPEDNNEFSLFQGFQATLPDEPETIKKKGKTHNARGQRLIGGELEDDEYSKLPPSMQRLQKQKHSMSHQLEMMGVRKHMCVAEIHEIDNKIANLNTMRKMVLDRLAGLEIQEEELAQDLLGVDNEIEDLQEELDDAAALAPPKEDSRPTTSGSEAVSETFMSESIYQKISPKSKNRGKKPIRRPSMRVLHEHLESGSKIKELPAHNDSITAMDFDAPWGTLVTASLDDTVRVWDLNAGRCIGMLEGHLSSVRCLQVEESIVATGSMDATIRLWDLSRAEYAPQDNRVNKRGGEGEGEGDGDAQEDEDGLAFENSSDAPPAPPPTIMQDVPLFTLESHVDEITAIHFKGDTLVSGSADKTLRQWDLVKGRCVQTLDVLWAAAQATATNNASSEWRPTGRSMDASADFVGAIQVFDAALACGTADGMVRLWDLRSGQVHRSLVGHTGPVTALQFDDVHLVTGSADRSIRIWDLRTGSIYDAYAYDNPVTSMMFDSRRIVSAAGESVVKVYDKTDGRHWNCGPGVGADEDDNTSHAMIERVRIKDGYLVEGRRDGTVGVWSC | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 75048
Sequence Length: 681
Subcellular Location: Mitochondrion outer membrane
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Q9P7I3 | MTDNNSKSKDSSQKIPNDSLTPTISKGLRKDVFYWTKAIAYTTWNFFDSSPVTPQRNPISLFVRGLSHPFLRHRLSKSQFNEWFLSHNGVDPVQAQTLPDPLLFDIPDHQETSYSLLEGYSVTAHDHSDTSPLPITSSNQKEGKKNVSSIDVSMVSDSSEFKPDSLQHEKLVKKCNQLRLQKLINSSELAQIDLELSKLYSRRRQVLERLSKIEEQNLKYTSKLASVEKLMLDSDAQDLYSSYSHDLIPSQIEAGKNGANPDVFDDTHDKYTDNLSARAISPRAPRPSTASEVVSDYFEQNSAFSKAPENTESSVNQNYIVGNLVKQFQAHSEYITSLDFSHPFGTLATASTDKTVKVWDMAGVVYLGSLKGHSDYVSCLAIQDSFIATGSMDTTVRLWNLDNDVLHKDNPVEESLNSPPDQPVDNATNVLTSHTAPVTALALSSDDVLITGADDKTVRQWDIVTGRCIQTLDFVWAETHDTSTSQILVSDTYKQEPFIRALDCLDAAVASGTVDGLIRIWDLRIGLPVRSFIGHTAPISSLQFDSNHLYSGSYDNSVRIWDLRSGSPINIIPMEKKVNSLRLYQGRLAVASDEPNVRIFDTVSNRNWICSIPSHSDSIAAEPNSVPTSVQYKDRFLVDGKSDGSVSVFSA | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 72373
Sequence Length: 651
Subcellular Location: Mitochondrion outer membrane
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Q4P8R5 | MSYSPLLGADRRAGEPSSGLASSTSIRDTLSGALNSTKAYLQPFTPASPYLGSNGVNGHNEPSRLLSDVAPQLMTTRMMAAVTNSNTALGLTPDGQRRARLLLTPGFSITSPARSLVRIGGSLIQSGIGRGPMNGITSNELFVLEESDRILATAARDLDLEANADAQLGARSAIEASKSKAAEPSVSLLRGFQATIPSSTEGRQRRRRVRALASGFEDGPEGPTKLGLKAMGDKARGLMVEGVDAEPVSAFQAREQRHARRNQASRILSRAKEGSRSSAIQLEELERQLREIEREQGDVGVRRSLIDSEMAAVDDKIKVLENIKAGLHKKLLGLREEELELNDEHEGVGELLAVQKHLRAMPGGPAAAANAAASGGATTSQGSSRRRKGPLFMPSEHDELPSGVAFMTLADHSAPITSLDFTEPYGTLVSASLDETVRVWDLASGEEVGRLRGHVGTVKCLQVEDEVCITGGSDHSIRIWDLTKVENFEARLTMTASGELRARRRSPDLNRSPPPVADESMDSIKIRDGDTTAGDGDEEEVRDEFDPCVKRLEGHSKSVTSLYFDDNCLVTGASDKTLRQWDLNTGQCVLTMDILWAISNPTSSQAISQSEFGFPESPSRKASSSSILGATRPDLSSRDSFSVLNNLSGAFSYPTPPYADGSWEMYQDFVGGVQFWGYALASGSGDGGVRMWDMRTGQAHRTLLGHTAPVTCLQFDEHHIISGSLDKSIRIWDLRMGSISDTVRYEHPVTALQFDSRKILAATGENGVKLFNRTTLQHGSLTLNGHTSPVERLRYMDRYAVSGGKDCVVKIWAL | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 87992
Sequence Length: 814
Subcellular Location: Mitochondrion outer membrane
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A7THX0 | MDDNEQFSQLRNVISTTASALLGIENLDKSILSSNSRYKKILSETIKNLGGDDSLVKLRKNFSNLKRQEESHDAYERYSGDDYFRNQLTDSRTTFRVLTYLSDEILKASLDDEKSNHDQGLLEFTNEEESGTKNTSSLFQGFEASLPILNERLENNDKNKYIKNSEGNDHNNNNDNNDDKNDKLFEFTNNYISSVSIDTEKISRSYSMKYLKTLSEDVLRKLNFTLIQEDVTKEEVEDLSIKLERLKERHQSACKRLETVEQDELFLENALSLIKDRMKFIQEYDLELESNDPEIEDINQNEKSYNEAKESNDLNTSQQNVEDLKPNTFVNNDKDVTVAKSEAIVSKVKTKNQKTINRLQRFYNEENRKSRKLPTTLLQSHYEPGTNIATIEKAHENGVYCMDFDMPFGTLCTAGYLDHTVNVWDLTRKVKVAEMSGHLATIQCMQLGSHYNMLITGGKDAMLKIWDINLATQLYQEDQSSIESDYNSCIHTFDSHSGGITALSFDSVHLVSASQDKTIRQWDLVNGKCIQTIDLSSVVKQNQTDIVNIPDFYSSSEPFVTGSLQCFDAALATGTRDGLVRLWDMRSGKVVRTFMGHTNAVTSLKFDSYNLISGSLDKSIRTWDLRTGSLSDLFAYDSPVYSIDFDSSNLVSAIGETSFKVYNRKDDKQWECVNSAEDTSSIYHVKYKNNYAVTGSNDGTIKAWVV | Function: Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 80436
Sequence Length: 706
Subcellular Location: Mitochondrion outer membrane
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Q6CB13 | MSDVTHFSKVVAATASTLVSGDLSQSHVMRDISRPAFQKRIFSFSKRPSELVRITSSSKDVLLPDEMLVDIPSNENQFSLFQGFQATLPEHSVGSQLLLGDGSKVGEKSAREQLVEGKKSLSHKLDLLEVRKALAANEITEIDARVAHLQSMRQIVFDRVASLEQQEFQLESEVLRIDAELEQMEEEKEEVIQRHDYETRTPEELEDDVVDLKSVSEKLQSASQKTLPRRNLSRRKTQPTLQQYYEPGNKIRQIKAHSDSVTCLDFDIPFGTMVSAGMDLGLKVWDLSRGDLVTDLKGHNASVTCLQVDNNVLATGSADATIRVWNLDQVVSNPDAQDEGDDAYTIHVLDSHVGEISAIHFSDHTLVSGSADKTIRQWDLNTGRCVQTLDVIWANSAQNALYSNDRLRTGFDANAPFIGAVQCRDAALATGTADGIVRLWDLRSGQVQRTLQGHTAAVTCLQFDDVHLATGSRDRSVRIWDLRMGNIFDAFAYDSPITSLDFDNRRIASTNGENTVKIYDRAAEKHWSLGRGEGDPEAPESTVVKTKEGYLVEGGGDGVVGVWAC | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 62531
Sequence Length: 565
Subcellular Location: Mitochondrion outer membrane
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P47025 | MSVNDQITHIGKTLSTTASAFLNYQKSNSNTQDVLTNNGPYKNLLSNTVNNASSTSYFYKRTEHGRFVKNASNTFEDIYSKTRRGDVFRNKFTDNKTCFRMLTYISDDLLNEIPTKEGLKSDADGKLLTEGGENENLRKNASKKETSLFQGFKSYLPIAELAIENTERLNYDTNGTSGTVGAKDVMSKTNERDEIHTELPNFQDSFLIPPGVETKKISSSYSPSALKSFSQTLVNSLEFLNIQKNSTLSEIRDIEVEVENLRQKKEKLLGKIANIEQNQLLLEDNLKQIDDRLDFLEEYGLEVIEANSDENAEDDGMSERKALKNDAIRNEGVTTESISSEASNLPPRRRQQLRDDNSLNRLGAFYSKSKKRHRKSFPTFQQLYEPGTKIGSIMSTHDDFLTCLDFDAPFGTLCTAGYLDHTVKIWDLSKQNKIGELAGHLATINCMQINRDYGTLVTGGRDAALKLWNLNLAQQLYQETQNLTSPTNHIDSPCVHTFEAHTDEVTALSLDPSFLVSGSQDRTIRQWDLRSGKCLQTIDLSFANVLTTSTNVDLSKSTLLTQRNERPSIGALQSFDAALATGTKDGVVRLWDLRSGKVIRTLKGHTDAITSLKFDSACLVTGSYDRTVRIWDLRTGLLNKFHAYSAPVLSLDLFQENAAVVVADEPSVQIYDSEKDESWSCVEQGNETSVSTVKYKENYMVEGRENGDVNIWAV | Function: Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein, binding to FIS1 on the mitochondrial outer membrane and recruiting the dynamin-like GTPase DNM1 to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 80032
Sequence Length: 714
Subcellular Location: Mitochondrion outer membrane
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O06989 | MVLLKKGFAILAASFLAIGLAACSSSKNPASSDGKKVLTVSVEETYKEYIESIKTKFEKENDVTVKIVEKQMFEQLEALPLDGPAGNAPDVMLAAYDRIGGLGQQGHLLDIKPSNTKSFGDKEMQQVTVDGKVYGMPLVIETLILYYNKDLLKTAPKTFKDLEKLTEDPRFAFASEKGKSTGFLAKWTDFYMSYGLLAGYGGYVFGKNGTDSGDIGLNNKGAVEAVKYAEKWFETYWPKGMQDNSSADDFIQQMFLEGKAAAIIGGPWSAANYKEAKLNYGAAPIPTLPNGEEYAPFAGGKGWVASKYTKEPELAEKWLEYAANDANAYAFYEDTNEVPANTAARKKADEQKNELTSAVIKQYETATPTPNIPEMAEVWTGAESLIFDAASGKKSTQTSANDAVNVIKENIKEKYVK | Function: Part of the ABC transporter complex involved in maltodextrin import. Binds maltodextrin. Can also bind maltose with low affinity, but is not involved in its uptake.
Location Topology: Lipid-anchor
Sequence Mass (Da): 45601
Sequence Length: 417
Subcellular Location: Cell membrane
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P51608 | MVAGMLGLREEKSEDQDLQGLKDKPLKFKKVKKDKKEEKEGKHEPVQPSAHHSAEPAEAGKAETSEGSGSAPAVPEASASPKQRRSIIRDRGPMYDDPTLPEGWTRKLKQRKSGRSAGKYDVYLINPQGKAFRSKVELIAYFEKVGDTSLDPNDFDFTVTGRGSPSRREQKPPKKPKSPKAPGTGRGRGRPKGSGTTRPKAATSEGVQVKRVLEKSPGKLLVKMPFQTSPGGKAEGGGATTSTQVMVIKRPGRKRKAEADPQAIPKKRGRKPGSVVAAAAAEAKKKAVKESSIRSVQETVLPIKKRKTRETVSIEVKEVVKPLLVSTLGEKSGKGLKTCKSPGRKSKESSPKGRSSSASSPPKKEHHHHHHHSESPKAPVPLLPPLPPPPPEPESSEDPTSPPEPQDLSSSVCKEEKMPRGGSLESDGCPKEPAKTQPAVATAATAAEKYKHRGEGERKDIVSSSMPRPNREEPVDSRTPVTERVS | Function: Chromosomal protein that binds to methylated DNA. It can bind specifically to a single methyl-CpG pair. It is not influenced by sequences flanking the methyl-CpGs. Mediates transcriptional repression through interaction with histone deacetylase and the corepressor SIN3A. Binds both 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC)-containing DNA, with a preference for 5-methylcytosine (5mC).
PTM: Phosphorylated on Ser-423 in brain upon synaptic activity, which attenuates its repressor activity and seems to regulate dendritic growth and spine maturation.
Sequence Mass (Da): 52441
Sequence Length: 486
Subcellular Location: Nucleus
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Q2KIA0 | MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESEDKYRKINEDIDLMISRQRLCAVPPPNFEMPVSIPVSSHNSLVYSNPVSSLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNMQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSEDVDLLLNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHSMPPSALSQLGDRTTTPSRYPQHTRHEAGRSPVDSLSSCSSSYDGSDREDHRNEFHSPIGLTRPSPDERESPSVKRMRLSEGWAT | Function: Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18. Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells. May also be involved in neurogenesis and in the development of cortical architecture (By similarity).
PTM: Phosphorylation on Ser-59 enhances DNA binding activity.
Sequence Mass (Da): 47844
Sequence Length: 441
Domain: The beta domain is required for enhancement of transcriptional activity.
Subcellular Location: Nucleus
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Q8CFN5 | MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESEDKYRKINEDIDLMISRQRLCAVPPPSFEMPVTIPVSSHNSLVYSNPVSTLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNIQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSEDVDLLLNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHNMPPSALSQLGACTSTHLSQSSNLSLPSTQSLSIKSEPVSPPRDRTTTPSRYPQHTTRHEAGRSPVDSLSSCSSSYDGSDREDHRNEFHSPIGLTRPSPDERESPSVKRMRLSEGWAT | Function: Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18 . May also be involved in neurogenesis and in the development of cortical architecture. Isoforms that lack the repressor domain are more active than isoform 1 (By similarity). Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells.
PTM: Phosphorylation on Ser-59 enhances DNA binding activity (By similarity). Phosphorylation on Ser-396 is required for Lys-391 sumoylation and inhibits transcriptional activity.
Sequence Mass (Da): 51278
Sequence Length: 474
Domain: The beta domain, missing in a number of isoforms, is required for enhancement of transcriptional activity.
Subcellular Location: Nucleus
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Q14814 | MGRKKIQIQRITDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNHSNKLFQYASTDMDKVLLKYTEYNEPHESRTNADIIETLRKKGFNGCDSPEPDGEDSLEQSPLLEDKYRRASEELDGLFRRYGSTVPAPNFAMPVTVPVSNQSSLQFSNPSGSLVTPSLVTSSLTDPRLLSPQQPALQRNSVSPGLPQRPASAGAMLGGDLNSANGACPSPVGNGYVSARASPGLLPVANGNSLNKVIPAKSPPPPTHSTQLGAPSRKPDLRVITSQAGKGLMHHLTEDHLDLNNAQRLGVSQSTHSLTTPVVSVATPSLLSQGLPFSSMPTAYNTDYQLTSAELSSLPAFSSPGGLSLGNVTAWQQPQQPQQPQQPQPPQQQPPQPQQPQPQQPQQPQQPPQQQSHLVPVSLSNLIPGSPLPHVGAALTVTTHPHISIKSEPVSPSRERSPAPPPPAVFPAARPEPGDGLSSPAGGSYETGDRDDGRGDFGPTLGLLRPAPEPEAEGSAVKRMRLDTWTLK | Function: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific, growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. Plays a critical role in the regulation of neuronal apoptosis (By similarity).
PTM: Phosphorylated on Ser-444 by CDK5 is required for Lys-439 sumoylation and inhibits transcriptional activity. In neurons, enhanced CDK5 activity induced by neurotoxins promotes caspase 3-mediated cleavage leading to neuron apoptosis. Phosphorylation on Ser-180 can be enhanced by EGF. Phosphorylated and activated by CaMK4.
Sequence Mass (Da): 55938
Sequence Length: 521
Domain: The beta domain, missing in a number of isoforms, is required for enhancement of transcriptional activity.
Subcellular Location: Nucleus
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P86889 | MGSAMVLSMSLLGFLPYAVFGPAIGVLVDRHDRKKIMIGADLIIAAAGSVLTIVAFYMELPVWMVMIVLFIRSIGTAFHTPALNAVTPLLVPEEQLTKCAGYSQSLQSISYIVSPAVAALLYSVWELNAIIAIDVLGAVIASITVLIVRIPKLGDRVQSLDPNFIREMQEGMAVLRQNKGLFALLLVGTLYMFVYMPINALFPLISMDYFNGTPVHISITEISFASGMLIGGLLLGLFGNYQKRILLITASIFMMGISLTISGLLPQSGFFIFVVCSAIMGLSVPFYSGVQTALFQEKIKPEYLGRVFSLTGSIMSLAMPIGL | Function: Confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides but not to 16-membered macrolides, lincosamides or analogs of streptogramin B. May function as an efflux pump to regulate intracellular macrolide levels (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34947
Sequence Length: 323
Subcellular Location: Cell membrane
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Q5XBB2 | MEKYNNWKLKFYTIWAGQAVSLITSAILQMAIIFYLTEKTGSAMVLSMASLLGFLPYAVFGPAIGVLVDRHDRKKIMIGADLIIAAAGSVLTIVAFYMELPVWMVMIVLFIRSIGTAFHTPALNAVTPLLVPEEQLTKCAGYSQSLQSISYIVSPAVAALLYSVWELNAIIAIDVLGAVIASITVAIVRIPKLGDRVQSLDPNFIREMQEGMAVLRQNKGLFALLLVGTLYMFVYMPINALFPLISMDYFNGTPVHISITEISFASGMLIGGLLLGLFGNYQKRILLITASIFMMGISLTISGLLPQSGFFIFVVCCAIMGLSVPFYSGVQTALFQEKIKPEYLGRVFSLTGSIMSLAMPIGLILSALFADRIGVNHWFLLSGTLIICIAIVCPMINEIRKLDLK | Function: Confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides but not to 16-membered macrolides, lincosamides or analogs of streptogramin B. May function as an efflux pump to regulate intracellular macrolide levels (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44279
Sequence Length: 405
Subcellular Location: Cell membrane
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Q8KBE8 | MNSKQITTLWCAVIVEELIRQEAGFFCISPGSRSTPLTLAVASNPKARFRMFPDERSAGFYALGYARATGMPAVLVCTSGTAVANYFPAVVEASADAQPMLVLSADRPFELLECGANQAIRQQNIFGSYTRWSFELPEPGIATPLASLLSTVDHAVRKSLSLPAGPVHLNLPFREPLEPEAPDPGHPWAAPLETWQASGEPWSRFARPLHEPSAESIVTLRELLAQAERPLFVAGSMSNAADGEAVAALAESLGVPLFADLTSGIRLSSDCTPWQLAFQNEAFVERFQPDVVIHFGGHVIGKQPAMALRKQPPLHYVVVREHPGRFDPDHNVTLTLEASPAAVASALEGCREPVPGIRCRDAFSAASGIIDKMACVPELAVSEISAPRIVSSLAGDGHALFVANSMPARDMDLYAAPVAQKPLQVALNRGVSGIDGIISTAAGFSAGLGKPTTLLIGDISFLHDLNALCLLNHPWNPLIVIVLNNHGGSIFSFLPIASQTDRLDECFATPQNFSIESAARTFGIDYACPETNGDFTQLYAEALTTKKSLIIEIRSDREKNLLLHRSLKARLDPVFEKADCSR | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 62690
Sequence Length: 582
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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A0M345 | MKYSKIPVARSVVALCVAKDIKHVVISPGSRNAPLTIGFTHHDEITPYSIVDERCAAFFALGLAQELKKPVALVCTSGSALLNYYPAIAEAYYSDIPLVIISADRPIERIDIGDGQTIRQKNVFENHILYSANLYSELVLENQSQDPKLQQKQFEAQKHNEREVNLALNKAIEEKGPVHINVPFYEPLYDTVENINVNPLQIFPEIKERHYSEKQLQNYANEWNRAERKMVIVGVAQPNAVEQKFLEGLATDPSVIVLTETTSNLHQEQFFTRIDTLIGPIEKDENREELFNRLQPDILLTFGGMIVSKKIKSFLRNYSPQHHWHIDSKKAYNTFFCLNKHFETDVNSFFSEFFPLTKRTESDYGSFWKDIKGKRQHRHEDYMAEIPYSDLKAMQEIYQKIPKNSVLHFGNSSTIRYAQLFEWDKSLKIYCNRGTSGIDGSVSTAVGASVSSEEPVTIITGDLSFFYDSNALWNNYIPSNFRIIILNNNGGGIFRILPGNKNSENFEKYFETTHNLKAKPICDLYNFDYEKANSEEEIQKVMKDFYSESGKPKLLEIFTPRKINDEVLLEYFNFMKS | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 66383
Sequence Length: 577
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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B0RCZ5 | MAAADALPTSSASASASADGPRTGNPSTDRAIAMLLALVREGVTDVVLCPGSRSQALALVAAELERVDGVRLHVRIDERAAGFLALGLGVESGRPAPVITTSGTAVANLHPAVLEGWHSGVPMLLLTGDRPAELRGIASNQTTRQPGMFGDRVACIDVPAPEETDDDLARDALLARDAYRRARDERTPVHVNVAFRDPLSVAVPDLTEAVAEVRAAAPATPAPAGPATADVLDLPHGPRTLVVAGHAAGEAAEELARAGGWPLAAEISSGSHFGPNLVVSFRELLAREGFGDRVERVIVFGHPTLTREVPLLVGREDVEAIVVGSTGGEDYDPRHRVTAHPAAVRVVGEPADPAEARRWLGTWVHESRAILDEATAAESAPLLPSGTTPAERRDFARAELAAVRADVTRRHLVRALWQATWPHDRLVLGASRLIREADRALPGKRVRVHANRGLAGIDGTISTGLGIALASQAGSGSAAAGITRVLVGDLTLLHDVGSLLIGTGERVPRIQVIVGNDGGGTIFDGLEVSRTAAPASIDRVMFTPQRVDLASLARAYGWAHLRAATHGELEAALTTASEAPLLIEVPLAR | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 61555
Sequence Length: 589
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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Q8FSB6 | MSVTPAQELAREVIEALSPHITDVVLCPGSRNSPLSLEVLSREDLRVHVRIDERSAAFLALGLARVQRRPVPVIMTSGTAVSNCLPAVTEAAHAHIPLLVVSADRPAHLIGTGSSQTIDQTDIFGALAPTVTVAAPEHVGRISQALGNGASQSPRHINVALDMPLVAPDLPELHGQRGPVDWEQRWVDHGVVDVDLSRNTLVIAGDEAWEIEELAEVPTIAEPTAPVAYHPVHPLAAEFLLKDQVSAEGYVVTTRPDHIIVVGHPTLHRGVLKLMTDPTIELTVLSRTDVITDPGRHADRVGSRVKVTGEQQKQWLKICDAASDLAAEGVREVLAKEEHGFTGLHVAAAVADGLGTGDTVFCAASNPIRDLSIVGLPFAGVDVHSPRGTAGIDGSVSQAIGTALAIQARHPDEIRAPRTVALLGDLAFIHDAGGLLIGPDEPRPENLTIVVANDNGGGIFELLETGAPGLRSRFERAFGTPHDVNISDLCDAYGVDYRRANTLQDLLMELEDTIEIPGFTVIEAVTVRDTRRALQRELTAKVR | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 57989
Sequence Length: 543
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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Q4JT09 | MRAGLVLVDQLIRSGVREAVLCPGSRNSPLNLAFVEAERVGRVRLHVRTDERSAAFLALGLAKVSRRPVPVVMTSGTAVANCLPAMVEATLSGVPLVVLSANRPLSMLGSGANQTIDQAEIFGTHSVCTLNTGELALEGAAAGAAGELRDLVRKLINAATDPIDGGGAHLDVPLREPLVPPTLDELSLWAGEIAAAEDAATTEGAHDSHAPSQPTRGPRKLPYGQVEVDLSRRTLVIAGSVSDVAWARSIMDELADVPTVAEPVAPAPDFPVHSAAVDMFSTQVVSDGEHSAVTIPEQIVVIGRPTLHRGVTKLLANKDINVIALSDTRNVTDVFDNVDEVGSTVRPRGEQPESWLQVARAISDMGVNQVRDGLAEREPFTAVHAVAVVADALRDGDLLVLGASTAVRDASRAGLPFDGVQAIANRGAAGIDGTISTAVGAAMAHAHADPTAIRAPRTIAVMGDLTFAHDLGGLNIGPLEPRPDNLLIVLTNDSGGGIFETLEPGAENLRTFADGTAAFERVFGTPLDLDFAELCAGFGVEHKLATSVEELATVIDEHAEIGGSGITVLEVKVSRRGRQEIEKRIAGTR | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 61567
Sequence Length: 589
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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Q6A9B0 | MNPSTAVARRLVNALVEAGVEHVVYCPGSRDAPIGYALADAETAGWLRVYVRLDERSAGFVALGLGRAGCPAALVTTSGTAVANIHPAVLEADAAGVPLIVLSADRPAEMWHTGANQTTVQTGIFGSAPRLSTDVPAGFPADERLDALVLRAVTAATGALSADPGPVHLNVSFRDSLVPDGPWQPQALVPRRVSSFPTAPTPLVMPARTVVVAGDGAGSLARELAQQGGWPLLAEPTSGSRVGDNALTDYQTVLGSELVDDVEAVLVLGHPTLSRPVSRLLARPDVTVVTDRSRWTDVAGVARVVTGPVELAEIDTDPAWLGRWKDADRPVVPTAKQRLCRDIWWACTTPNAPVLVIGASEVIRCFDRFAVPGDIAPTALANRGLAGIDGTIATAIGVGLGTGRPVRVVVGDLTFAHDAMSLLLGETEPEPDVQVVVLDDRGGAIFSGLEHAAAPAPVLRRMFLTPQRLDSAALAHALGASHRRVSPDDLQFLDEPVVGRQVVSVPLT | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 53075
Sequence Length: 508
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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Q11U88 | MQAIYDIPEILFQHGVTDVVLSPGSRCAPLSIAFSRHKKLQIKVVPDERSAAFIALGMSLQTQKPTVLICTSGSALYNYAPAIVEAYYQRVPLIVLSADRPPEWIDQNDGQTIRQQEIYGKHSKAFFQLSAEHELPDTQWETYRKVNEAVSISEAYPKGPVHINIPFREPFYPKGEIMFSGSPTVIKREQPLHTLSDEQWKSIQHKLDSYKKILFVGGQHLYDESLRLKIGNIKAPFIGEVVSNLHGVRNVIHTHDTLLTSIPLTDLEELKPDLVISFGGALLSKWLKQFIRSNESIDHWYVGPDVTTPDVFQHLCQIIPVQLNEFLSKTTIASNTQEQFVQRWIQQQTHIIPAIREFNTKEKVFNEFTAVFDVLNHLPAFAKLHLANSMSVRYANTLGISQRNAEVFANRGTSGIDGVISTAYGYALKTSQLVTIITGDLAFFYDRNAFWNNYKPSNLRVVLLNNHGGGIFRMIDGPSALPELDELFETKQTLSARYLATEHGLEYTLCKNLNGLNQALESFFQPSMFGKILEIETDSVKNTEVFKRFKKTIQQSYLS | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 63324
Sequence Length: 559
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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Q47DK0 | MTDIGTLNFTWSQAIIGGFVAAGITDAVISPGSRSTPLALAMLRQAGLRCHIAIDERSAAFFGLGLAKSSHCPVLLLATSGTAPANWLPAVIEASQSGIPLILISADRPPELQDCGANQTVSQPGLFGSHTRASYTLGTPEPGFNPGYLHRVARQACEQASWPHPGPVHINQPFREPMLPSEPVLSGEMPEKISISHPDLQPDLNALGDLARRISGRPGIIVCGEMPSRDGQNEALVALATRLRSPIFAEPLSGLRFGPHDRSHLCVRYNDWLGKTDLVSQYRPEWVIRFGAYPVTRNLQKLVSEITETHALVDPWPRWIDPARRLTHLLRSEPAAICKALLDLSLVPFSETWLSALAKFEGNAEADEQRNHIHVLLEEVPDDTDLFVGNSLAIRQMDTHSGSADKTLRIYANRGASGIDGNISTAAGIAASRGRAVALIGDLTCQHDLGGLALAQGQNIVIIVVNNGGGGIFDHLPQRDLPEFTQGWRTPQNVNFEHAAMAFGLGYAATHSDDDLRPALRHAFAAGGPHLIELRQC | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 57930
Sequence Length: 537
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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B8FTY8 | MTNYIAALVDELYQLGVREAVISPGSRSTPLSVLFCEYGFQVYVGIDERSAGFFALGIAKEKERPVVLVCSSGSAVAHYFPAIVEAKHSHVPLIVLTADRPPELRQVGAPQTIDQIKFYHDYAKYFEELALPEEREGMYRYVRGVMRKAYVSSLDQGYGVAHINIPLREPLSPDLDGVDFTAGRLDYPFAWKTGEKGLTMDSSVFQDKKGIIICGGDPYADYHREVLELAERLKAPLLADPLANFRNDDHPLIMDCYDAFLKSDAVKVELKPEFIIHFGQTPVSKRLQNFTAMHQDVLYFQVNDYFQYRDPSLSISRYLVASPKAFARSVKVHNTDDGYSGRWQHYQARMRRRLNLAQDEEELFEGKLVQKLQDSLPEGSRLFVANSMAIRDVDYFLEARRQRIKVLGNRGANGIDGTVSTALGVATSGHPTVLLTGDLAFFHDLNGLLIGKNHGLNLIIVLLNNNGGAIFKYLPQSENKYFELLFMTPHGMDFSGLKTLYDLTYYEPVDYESFAQNFQEALTLSGVKVLNVKIDARLSKELHDRLTNLD | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 62040
Sequence Length: 550
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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Q6ARP3 | MRAKQHISDLAHHCIAHGMRHLVISPGSRNAPLIRAFAASSQIECLSIVDERSAAFVALGLATELQAPVGVLCTSGTALLNYGPAIAEAYYLRAPLIVLSADRPARLVGQQDSQTICQDNLFANIVKGSYSLPEEPETVAELELSARVIAQAFSTALSPCFGPVHINIPLDEPLYGGELMAESLIALSPLQLAEPKGMSPALWQEVESAWRGAKRRMIVCGQGVADAELQALLARFAPDKTVTIIAENTANIVGPWLVDRPDAVLLACDEASRSLLAPDCLISFGGHLVAKHIKLLLREFKPAFHFRLDPAQMGIDTYQCLSAELDLAPTTFFRRLAQQVEPAAGFRDLWALPEGVAENQDDEFLVLKRLLGQLPAGSIAHLGNSMSVRHAQKLASRADLLYHSNRGVAGIDGCLSTAVGVALATDQLVLCCLGDLSFVYDSNALWNRNLPSNLRIVILNNQGGDIFRRLKGPSVSPGYQDFFVAHHPVQIGKMIEAYGVAYRRCLASEIDGFSEEFLGLQDGPLVLEVFVDPTKRD | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 58155
Sequence Length: 537
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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Q8CPQ5 | MNHSEALTEQVFSFASELYAYGVREVVISPGSRSTPLALAFEAHPNIKTWIHPDERSAAFFALGLIKGSEKPVAILCTSGTAAANYTPAIAESQISRLPLVVLTSDRPHELRSVGAPQAINQVNMFSNYVNFQFDLPIADGSEHTIDTINYQMQIASQYLYGPHRGPIHFNLPFREPLTPDLDRVDLLTSVTKTLPHYQKSISVDDIKDILQEKNGLIIVGDMQHQAVDQILTYSTIYDLPILADPLSQLRKEKHPNVITTYDLLYRAGLNLEVDYVIRVGKPVISKKLNQWLKKTDAYQIIVQNNDQIDVFPTPPHISYEISANDFFRSLMEEPLVERKKWLQQWQSLEQQARIEISDYLKHATDEAAYVGSLIQKLTKEDTLFVGNSMPIRDVDNLLFDSEASVYANRGANGIDGVVSTALGMAAHKNVILLIGDLSFYHDMNGLLMAKLNELHINIVLVNNNGGGIFSYLPQKRSATKYFERLFGTPTGLNFEYTALLYDFTFKRFDNLTDFKYAELSKMGSHMYEVITNRDENLHQHQNLYQKLSEIVNVTL | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 62865
Sequence Length: 556
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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Q49WG6 | MNNHTDALTKQVFTIVSELYAYGIREVVISPGSRSTPLAIAIEAHPKLKSWIHPDERSAAFFAMGLMKGSEKPVAILCTSGSAAANYTPAISESSLSHLPLVVLTSDRPHELRGIGAPQAINQTNMFANYVQYQFDFPIAEKNDNEDIMANTIKFQLQKASQFLYGPHRGPIHLNLPFREPLTPNTEKVEWLTSDTKILPHYQKTTSLNEISAMMKKRKGLIIVGDMQHQDVDQILTFSTIHDMPILADPLSQLRREHHPNVVTTYDLLLRSGLELEADFVIRVGKPVISKKLNQWLKVTEAFQILVQNNDRPDAFPITPHVSYEMSANDFFRQLSEMPTVERKQWLEKWQTVEKHAIVEIKDHLRTATDEAAYVGNVLDKLTKDDAIFVSNSMPIRDVDNLFIDCEAEVFANRGANGIDGVTSTALGMAVHKKITLLIGDLAFYHDMNGLLMSKLNDIQLNIVLLNNDGGGIFSYLPQKNEADAYFERLFGTPTGLNFEHTALLYDFAFDRFDTIEAFKYADLSQFGSHIYEIMTHREDNKQQHLKLYKKLSDIIDVTL | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 63321
Sequence Length: 560
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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Q2LXE3 | MPLSDNLNLLWSSLIVAELVKNGLDTFFISPGNRNAPLISALIHEERSVKKICVDERAAGYRALGHAKAAGRPGVLVCTSGTAPANYYPAVIEAFRDEIPLVILSADRPPELIGSDANQTIVQPDLYGRYCRDSLLIPCPSADYPLEALLARIDSLIARPVGPVHINCAFRDPLVPGIPDSRPIPDELLATAGRLYAREGAYTTYPSPGTLHTGLEDVEAILNRTARGLIVIGRLDGPRDAPALEELAKKLGWPVFCDIASSMKGRIPSDRQIFSLDHPEALRLVSAYAPETILQFGSGLVSKHYFASLLPHSEATVIQISPRAGLRDPAHRVNVRLSMPAFAFVEGLHLQENPSLDATACCLFLDSLETLYQALQRRIPEETLSFSRIASDLLGAVPDGEGLFLGNSLVIRAFDKFRSPFPRKISVISNRGVSGIEGNIATSVGFAEASRRRVTAVIGDISFLHDLNSLLLLAQSATPVVLIIINNGGGRIFERLPIRDFPEILEPYMTTPHGMTFDLLAAQFDLPYFRAATPDELRKAYESALDAERSAVLEVTLDPEEDLRTFQTFQNVRLP | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 62812
Sequence Length: 575
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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Q31NA4 | MGQAAAITMPIDPRNLNTLWSSVLAESFVRLGLQTVVICPGSRSAPLAIAFAEHPEIDAIPILDERSAGFFALGRAKASHRPVALICSSGTAGANFYPAVIEAKESGVPLLVITADRPPELRQCHAGQAIDQLRLFGSYALWEAELALPVLDLGLLRYLRQTAQQAWQQALRGGPVHLNQPLREPLAPIADPATQTWLAQQWPGENFFAELLTAVPTPQIQQPLPPLPSQGLITVGPIAPEDPAAFVQAIAQLSAHLGWPVLSDAVTPLRQFADHCPRLISSYDLILRQPHWRASLQPEAVLQIGELPTSKELRLWLTEQTCPRWIVSPRPENFDPLHGSSHHLPVTVEAIAIPATIAPASDYSRQWQQAETAVQAAIAQHLAQVPDLTEPGIARLLSQHLPAQTPIFVANSTPIRDLEWFWLANDQRRSLYCSRGANGIDGTLSTAIGIAHQNRPSVLITGDLSLLHDSNGFLQRSQLQGHLTVVLIDNSGGGIFELLPIRDCGPSFEPFVATPQTVDFAALCQAYGVDYQAIATEAELIKAIQTLPTSGIRVLHLFTDRRQNAAWRRALFAELAAIPSQS | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 63330
Sequence Length: 582
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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Q9XAP8 | MTRASLNKQPHEVASMFDHVAERYDLTNAVLSLGQDRAWRKAVARAVDARPAQKVLDLAAGTATSSLPFARTGAYVVPCDFSQGMLQVGKERHSWLPFTAGDATRLPFKDDVFDAVTISFGLRNVQDTDAALREMYRVTRPGGRVVICEFSHPTWAPFRTVYTEYLMRALPPVARAVSSNPDAYVYLAESIRAWPDQPALAGRLGRAGWSRVAWRNLTGGVVTLHRGFKAS | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25537
Sequence Length: 231
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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B1W525 | MTRASLEKQPHEVASMFDGVAANYDLTNDVISLGQARLWRRAVAAAVDARPAQKILDLAAGTATSSQPFVKAGAYVVPCDFSLGMLKVGKERHPWMPFTAGDGMRLPFKDETFDTVTISFGLRNIQDTEVALRELYRVTKPGGRVVICEFSQPTWTPFRTVYTEYLMRAIPPAARAVSSNPDAYVYLAESIRDWPDQPALAALLQKAGWSKVAWRNLTGGVVALHRATRA | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25343
Sequence Length: 230
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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Q67LE6 | MAPGYQPPSPEEKEQYVRELFDKIAENYDAMNQVMSAGQWEKWHREFVAQTHFRPGDHILDVACGTGDLTLLDAAQVAPDGKVIGVDISEGMLEVGRRRVAASPYKDLITLQLGNAMDLPFPDNTFDGVTMGWAMRNVASIPRTLSEIYRVLKPGGRFICLEASKPFSRFIRFGFFVYWKTFLPLIDWFVVKAGRQAKVRPYTYLSRSLDNYPFPDQLEELFREAGFVETDYQLLMLGTVAIHVGTKRREG | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28582
Sequence Length: 251
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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Q31P90 | MSVLAPDAVEGLFDQIAPIYDNLNDQLSFGLHRLWKRMAVKWSAAKPGDRVLDLCCGSGDLAFLLAKVVGSKGQVIGFDRSQALLSVAGDRARQLASALVIDWQRGDALDLPFPDDHFDAATLGYGLRNVPDIPTVLRQLQRVLKPGARAAILDMHRPYSPLLRQFQQVYLDRWVVPAAAAQNCAAEYEYIDASLEAFPQGQQQVALAIAAGFQRAKHYELAAGLMGVLVVEA | Function: Methyltransferase required for the conversion of 2-phytyl-1,4-beta-naphthoquinol to phylloquinol.
Catalytic Activity: demethylphylloquinol + S-adenosyl-L-methionine = H(+) + phylloquinol + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25441
Sequence Length: 233
Pathway: Cofactor biosynthesis; phylloquinone biosynthesis.
EC: 2.1.1.329
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Q12866 | MGPAPLPLLLGLFLPALWRRAITEAREEAKPYPLFPGPFPGSLQTDHTPLLSLPHASGYQPALMFSPTQPGRPHTGNVAIPQVTSVESKPLPPLAFKHTVGHIILSEHKGVKFNCSISVPNIYQDTTISWWKDGKELLGAHHAITQFYPDDEVTAIIASFSITSVQRSDNGSYICKMKINNEEIVSDPIYIEVQGLPHFTKQPESMNVTRNTAFNLTCQAVGPPEPVNIFWVQNSSRVNEQPEKSPSVLTVPGLTEMAVFSCEAHNDKGLTVSKGVQINIKAIPSPPTEVSIRNSTAHSILISWVPGFDGYSPFRNCSIQVKEADPLSNGSVMIFNTSALPHLYQIKQLQALANYSIGVSCMNEIGWSAVSPWILASTTEGAPSVAPLNVTVFLNESSDNVDIRWMKPPTKQQDGELVGYRISHVWQSAGISKELLEEVGQNGSRARISVQVHNATCTVRIAAVTRGGVGPFSDPVKIFIPAHGWVDYAPSSTPAPGNADPVLIIFGCFCGFILIGLILYISLAIRKRVQETKFGNAFTEEDSELVVNYIAKKSFCRRAIELTLHSLGVSEELQNKLEDVVIDRNLLILGKILGEGEFGSVMEGNLKQEDGTSLKVAVKTMKLDNSSQREIEEFLSEAACMKDFSHPNVIRLLGVCIEMSSQGIPKPMVILPFMKYGDLHTYLLYSRLETGPKHIPLQTLLKFMVDIALGMEYLSNRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWAFGVTMWEIATRGMTPYPGVQNHEMYDYLLHGHRLKQPEDCLDELYEIMYSCWRTDPLDRPTFSVLRLQLEKLLESLPDVRNQADVIYVNTQLLESSEGLAQGSTLAPLDLNIDPDSIIASCTPRAAISVVTAEVHDSKPHEGRYILNGGSEEWEDLTSAPSAAVTAEKNSVLPGERLVRNGVSWSHSSMLPLGSSLPDELLFADDSSEGSEVLM | Function: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the cell surface induces autophosphorylation of MERTK on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with GRB2 or PLCG2 and induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization and engulfment . Functions in the retinal pigment epithelium (RPE) as a regulator of rod outer segments fragments phagocytosis. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3.
PTM: Autophosphorylated on Tyr-749, Tyr-753 and Tyr-754 in the activation loop allowing full activity. Autophosphorylated on Tyr-872 leading to recruitment of downstream partners of the signaling cascade such as PLCG2 (By similarity).
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 110249
Sequence Length: 999
Subcellular Location: Cell membrane
EC: 2.7.10.1
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Q60805 | MVLAPLLLGLLLLPALWSGGTAEKWEETELDQLFSGPLPGRLPVNHRPFSAPHSSRDQLPPPQTGRSHPAHTAAPQVTSTASKLLPPVAFNHTIGHIVLSEHKNVKFNCSINIPNTYQETAGISWWKDGKELLGAHHSITQFYPDEEGVSIIALFSIASVQRSDNGSYFCKMKVNNREIVSDPIYVEVQGLPYFIKQPESVNVTRNTAFNLTCQAVGPPEPVNIFWVQNSSRVNEKPERSPSVLTVPGLTETAVFSCEAHNDKGLTVSKGVHINIKVIPSPPTEVHILNSTAHSILVSWVPGFDGYSPLQNCSIQVKEADRLSNGSVMVFNTSASPHLYEIQQLQALANYSIAVSCRNEIGWSAVSPWILASTTEGAPSVAPLNITVFLNESNNILDIRWTKPPIKRQDGELVGYRISHVWESAGTYKELSEEVSQNGSWAQIPVQIHNATCTVRIAAITKGGIGPFSEPVNIIIPEHSKVDYAPSSTPAPGNTDSMFIILGCFCGFILIGLILCISLALRRRVQETKFGGAFSEEDSQLVVNYRAKKSFCRRAIELTLQSLGVSEELQNKLEDVVIDRNLLVLGKVLGEGEFGSVMEGNLKQEDGTSQKVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCIELSSQGIPKPMVILPFMKYGDLHTFLLYSRLNTGPKYIHLQTLLKFMMDIAQGMEYLSNRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWAFGVTMWEITTRGMTPYPGVQNHEMYDYLLHGHRLKQPEDCLDELYDIMYSCWSADPLDRPTFSVLRLQLEKLSESLPDAQDKESIIYINTQLLESCEGIANGPSLTGLDMNIDPDSIIASCTPGAAVSVVTAEVHENNLREERYILNGGNEEWEDVSSTPFAAVTPEKDGVLPEDRLTKNGVSWSHHSTLPLGSPSPDELLFVDDSLEDSEVLM | Function: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the cell surface induces autophosphorylation of MERTK on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with GRB2 or PLCG2 and induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization and engulfment. Functions in the retinal pigment epithelium (RPE) as a regulator of rod outer segments fragments phagocytosis. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3.
PTM: Autophosphorylated on Tyr-744, Tyr-748 and Tyr-749 in the activation loop allowing full activity (By similarity). Autophosphorylated on Tyr-867 leading to recruitment of downstream partners of the signaling cascade such as PLCG2.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 110157
Sequence Length: 994
Subcellular Location: Cell membrane
EC: 2.7.10.1
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P57097 | MVLAPLLLGLLLLSALWNGGTAEKEEEIKPDQPFSGPLPGSLPADHRPFFAPHSSGDQLSPSQTGRSHPAHTATPQMTSAASNLLPPVAFKNTIGRIVLSEHKSVKFNCSINIPNVYQETAGISWWKDGKELLGAHHSITQFYPDEEGVSIIALFSITSVQRSDNGSYICKMKVNDREVVSDPIYVEVQGLPYFTKQPESVNVTRNTAFNLTCQAVGPPEPVNIFWVQNSSRVNENPERSPSVLTVAGLTETAVFSCEAHNDKGLTVSKGVQINIKVIPSPPTEVHILNSTAHSILVSWVPGFDGYSPLQNCSIQVKEADQLSNGSVMVFNTSASPHLYEVQQLQALANYSVTVSCRNEIGWSAVSPWILASTTEGAPAVAPLNITVFLNESSNNLEIRWTKPPIKRQDGELVGYRISHVWESAGTSKELSEEVSQNGSWAQVPVQMHNATCTVRIAVITKGGIGPFSEPVDVAIPEHSRVDYAPSSTPAPGNTESMLIILGCFCGFVLMGLILYLSLAIKRRVQETKFGGAFSEEDSQLVVNYRAKKSFCRRAIELTLQSLGVSEELQNKLEDVVVDRNLLILGKVLGEGEFGSVMEGNLKQEDGTSQKVAVKTMKLDNFSLREIEEFLSEAACMKDFNHPNVIRLLGVCIELSSQGIPKPMVILPFMKYGDLHTFLLYSRIESVPKSIPLQTLLKFMVDIAQGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWAFGVTMWEIATRGMTPYPGVQNHEMYDYLLHGHRLKQPEDCLDDLYEIMYSCWSADPLDRPTFSVLRLQLEKLSESLPDAQDKESIIYINTQLLESCEGLANRSSLAGLDMNIDPDSIIASCTAGAAVSVVMAEVHENNLHEERYILNGGNEEWEDVASTPFATVTAGKDGVLPEDRLTKNGISWSHHSTLPLGSPSPDELLFADDSSGDSEVLM | Function: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the cell surface induces autophosphorylation of MERTK on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with GRB2 or PLCG2 and induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization and engulfment. Functions in the retinal pigment epithelium (RPE) as a regulator of rod outer segments fragments phagocytosis. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3 (By similarity).
PTM: Autophosphorylated on Tyr-744, Tyr-748 and Tyr-749 in the activation loop allowing full activity. Autophosphorylated on Tyr-867 leading to recruitment of downstream partners of the signaling cascade such as PLCG2 (By similarity).
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 109423
Sequence Length: 994
Subcellular Location: Cell membrane
EC: 2.7.10.1
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P94700 | MSEPQKSEPQKSEPQNGRGALFAGGLAAILASACCLGPLVLIALGFSGAWIGNLTVLEPYRPIFIGAALVALFFAWRRIYRPAQACKPGEVCAIPQVRATYKLIFWIVAALVLVSLGFPYVMPFFY | Function: Involved in mercury resistance. Probably transfers a mercuric ion from the periplasmic Hg(2+)-binding protein MerP to the cytoplasmic mercuric reductase MerA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13664
Sequence Length: 126
Subcellular Location: Cell inner membrane
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P04140 | MSEPKTGRGALFTGGLAAILASACCLGPLVLIALGFSGAWIGNLAVLEPYRPIFIGVALVALFFAWRRIYRQAAACKPGEVCAIPQVRATYKLIFWIVAALVLVALGFPYVMPFFY | Function: Involved in mercury resistance . Probably transfers a mercuric ion from the periplasmic Hg(2+)-binding protein MerP to the cytoplasmic mercuric reductase MerA (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12498
Sequence Length: 116
Subcellular Location: Cell inner membrane
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Q12650 | MANAPHGGVLKDLLARDAPRQAELAAEAESLPAVTLTERQLCDLELIMNGGFSPLEGFMNQADYDRVCEDNRLADGNVFSMPITLDASQEVIDEKKLQAASRITLRDFRDDRNLAILTIDDIYRPDKTKEAKLVFGGDPEHPAIVYLNNTVKEFYIGGKIEAVNKLNHYDYVALRYTPAELRVHFDKLGWSRVVAFQTRNPMHRAHRELTVRAARSRQANVLIHPVVGLTKPGDIDHFTRVRAYQALLPRYPNGMAVLGLLGLAMRMGGPREAIWHAIIRKNHGATHFIVGRDHAGPGSNSKGEDFYGPYDAQHAVEKYKDELGIEVVEFQMVTYLPDTDEYRPVDQVPAGVKTLNISGTELRRRLRSAHIPEWFSYPEVVKILRESNPPRATQGFTIFLTGYMNSGKDAIARALQVTLNQQGGRSVSLLLGDTVRHELSSELGFTREDRHTNIQRIAFVATELTRAGAAVIAAPIAPYEESRKFARDAVSQAGSFFLVHVATPLEHCEQSDKRGIYAAARRGEIKGFTGVDDPYETPEKADLVVDFSKQSVRSIVHEIILVLESQGFLERQ | Function: Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 63917
Sequence Length: 572
Domain: The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme.
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.7.4
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Q0V6P9 | MANPPHGGVLKDLIARDAPRRQELYAEAEKLPAIVLSDRQLCDLELILNGGFSPLEGFMNEKDYTGVVAENRLADGNLFSIPITLDVSKETIDEVGVKAGARIALRDSRDDRNLAIITVDDIYKPDKVKEANEVFGDNDEAHPAVKYLHHTAKEFYVGGKVEAIDRLEHYDYVGLRYTPAELRLHFDKLGWQKVVAFQTRNPMHRAHRELTVRAARARQANVLIHPVVGLTKPGDIDHFTRVRVYQALMPRYPNGMAVLALLPLAMRMGGPREAIWHAIIRKNHGATHFIVGRDHAGPGKNSKGVDFYGPYDAQDAVEKYRDELGIEVVPFQQMTYLPDSDEYKPKDEVAKDIKTLDISGTELRKRLRTGQEIPEWFSYPEVVKVLRESHPPRNQQGFTVFLTGYQNSGKDAIARALNVTLNQQGGRSVSLLLGETVRSELSSELGFSREDRDKNIARIAFVAAELTKAGAAAIVAPIAPFQKSRQQARETVEKYGSFFLVHVATPLDHAEKTDRRGVYAKARAGEIKGFTGVDDPYEAPENADLVVDTSKTNVRTAVHQIVLLLESQGLLTQL | Function: Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 64037
Sequence Length: 574
Domain: The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme.
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.7.4
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P78937 | MTKALLKDLNARDAPLREQLEQEATSLPKIVLSERQFCDVELILNGGFSPLDGFMNQKDYLNVVENLRLSTGEVFPIPITLDLNESQADSLKAGDRVALLDPRDGQTVIAILTVEDKYTPDKANEAEKVFGANDRAHPAVDYLFGRAGNVYVGGKLQAVTPIRHFDFVEYRYSPAQLRSDFQRNNWNRVVAFQTRNPMHRAHRELTVRAAKQHGARVLIHPVVGMTKPGDIDHFTRVRVYEAILQRYPKGSAKLSLLPLAMRMAGPREALWHAIIRKNYGASHFIIGRDHAGPGKNSQGEDFYGPYDAQYLVEQYAQEIGITIVPFQMMTYLPDEDIYKPVDKVEPGTRTLNISGTELRRRLRVGANIPEWFSYPEVVAILRQSYPPKYSQGFVLAVPATSDKLLPSALVSALNEDGRRHVTLLPRLDAISVFYAQELQRAGAAVVVSLADADASVKVPAEWTTVNIKPKDSVSEVTFAVLSQLSDEGYL | Function: Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 54754
Sequence Length: 490
Domain: The oligomerization domain is distantly related to APS kinases, but it is not functional and does not bind APS. It is required for oligomerization of the enzyme, although the oligomerization state has no effect on the catalytic activity of the enzyme.
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.7.4
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Q4P460 | MANAPHGGVLKDLLVRDAPIAAQLRQEADTLPEIVLTERQLCDLELIINGGFSPLQGFMNQTDYNGCLDNMRLADGNLFPMPITLDVDEQQIEALKIQQGARIALRDPRDDNAIAIITVTDVYAVDKVREATAVFGSDDLAHPAITYLHKSVKNFYVGGDVQAVSKPAYYDYVALRYTPAELRQHFAKISWRKVVAFQTRNPMHRAHRELTVRAARQRQANVLIHPVVGMTKPGDVDHYTRVRVYQSLMPRYPNGMATLALLPLAMRMGGPREALWHAIIRKNFGVTHFIVGRDHAGPGKDSSGKDFYGPYDAQTLVTKYTEELGIEMVPFQQMTYIPSTDEYQPVDEVTPGTQTMDISGTELRRRLRTGAAIPDWFSYESVVKTLRESYPPKAKQGFTLFLTGLHNSGKDQIARALQVKLNEQGGRSVSLLLGETVRSELSSELGFSPDDRQKNIQRISFVAAELTRAGAAVIAAPIAPYEKSRATARDIITKTGGAGNFFLIHVATPLEYCEATDRKGNYAKARAGQIKGFTGVDDVYEEPTDADLVVDISRQSVAEITHSIILLLEAQSLI | Function: Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 63597
Sequence Length: 574
Domain: The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme.
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.7.4
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P08536 | MPAPHGGILQDLIARDALKKNELLSEAQSSDILVWNLTPRQLCDIELILNGGFSPLTGFLNENDYSSVVTDSRLADGTLWTIPITLDVDEAFANQIKPDTRIALFQDDEIPIAILTVQDVYKPNKTIEAEKVFRGDPEHPAISYLFNVAGDYYVGGSLEAIQLPQHYDYPGLRKTPAQLRLEFQSRQWDRVVAFQTRNPMHRAHRELTVRAAREANAKVLIHPVVGLTKPGDIDHHTRVRVYQEIIKRYPNGIAFLSLLPLAMRMSGDREAVWHAIIRKNYGASHFIVGRDHAGPGKNSKGVDFYGPYDAQELVESYKHELDIEVVPFRMVTYLPDEDRYAPIDQIDTTKTRTLNISGTELRRRLRVGGEIPEWFSYPEVVKILRESNPPRPKQGFSIVLGNSLTVSREQLSIALLSTFLQFGGGRYYKIFEHNNKTELLSLIQDFIGSGSGLIIPNQWEDDKDSVVGKQNVYLLDTSSSADIQLESADEPISHIVQKVVLFLEDNGFFVF | Function: Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 57725
Sequence Length: 511
Domain: The oligomerization domain is distantly related to APS kinases, but it is not functional and does not bind APS. It is required for oligomerization of the enzyme, although the oligomerization state has no effect on the catalytic activity of the enzyme.
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.7.4
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P32389 | MKQEQSHEGDSYSTEFINLFGKDTATHPSSNNGANNNGMGSTNSLDQFVATASSSSSLVTSSENRRPLIGDVTNRGNTNLYDHAVTPEILLEQLAYVDNFIPSLDNEFSNVDWNVNTTHNNANNNGADTFSSINANPFDLDEQLAIELSAFADDSFIFPDEDKPSNNNNNSNNGNDDHSNHDVLHEDPSTNNRQRNPHFLTQRRNTFLTSQYDQSKSRFSSKNKRNGNNGETNNFGDNMQNNHPFEPNFMGSPSQFPADATNMTSIDHGGFTNVDITSTENNTTGDNGVDALSNLLHRTTHTPNRSSPLSNVTSAQNSSSQQRKHSESKVDSNSDNNSSNKAPNITVPDYSIIPTSVLVTLLPRVNVPNGAYNSLISAGFDNDQIDAIAAIMAYHHQKKIRENNSNNNKNINTNDSQEAPILKNINELLSVLIPPSPAETRGPTTLSTSPSFNEHGVVAEASFLSSILELGIKHPKSNNIHNQRQPSRNDHKISRESDGNNGNDNVHHNNAVIKSSTTRGDEIAKIRSEPTLNASSSDHKENSLKRSHSGDLKNKKVPVDRKYSDNEDDEYDDADLHGFEKKQLIKKELGDDDEDLLIQSKKSHQKKKLKEKELESSIHELTEIAASLQKRIHTLETENKLLKNLVLSSGETEGIKKAESLKKQIFEKVQKE | Function: Positive trans-acting factor capable of stimulating the transcription of the MET genes from the methionine biosynthetic pathway. MET4, MET28 and CBF1 are required for full induction of MET25 and MET16 gene transcription. MET4 controls as well the derepression of MET6. Required for the transcription of genes necessary for sulfur amino acid biosynthesis. Involved in the transcription activation of MET28 and MET30. Required for MET3 gene expression via assembly of the MET4-MET28-MET31 and MET4-MET28-MET32 complexes. Involved in response to cadmium and arsenic. Cadmium-activated MET4 also induces glutathione biosynthesis.
Sequence Mass (Da): 74373
Sequence Length: 672
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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P38675 | MPPFELGDPIPSETAHAVSVSLPTWSANVGYEEGQDWVVKRMATGYPRFFIHRTIQAFAADIVATHVSTKAKRTSDITAMLFPTPTIASRCVDFIRSRAPADVCSNIEVVNLVLDMSDPEARALEPLCPSISAVIMPQDGFPFAKQYWQHSGDGVSSRRAEFCHGLFKDGLLRPDTELRNAAVSAAKPCRGPKRYQRQASLDAGGNQQTIMHGHIHRATGETAMIQETSRFLEERFGRNLDLSFVHPAKSAIKRRIAGALRSADHDLGGSPSLSEKQMSSNTRGIANLREEDIYLFPCGMNAIFHAHRALYSIRTPPGSTPLKSVNFGFPYVDTLKILEKFNPSGALFYGHGSKSDLDDLETRLESGERYLALFCEFPGNPLLTCPDLVRIRELADKYEFAVVVDETIGTFANVNVLQFADIVVSSLTKIFSGDCNVMGGGAIFNPNSRYYSALKSFVQQQLEDTYWPEDVIFMERNSRDFVARIDRVNANAEAICRVLQDHPLVKTLYYPKYNDSRANYEAVKLPQGGYGGLISVVLKGKKQAVAFYDAIETAKGPSLGTNFTLTSPYVLLAHYQELDWAEQYGVDRNLIRISVGLEGTDELINVFTRALKVAEEQSQYP | Function: Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia (By similarity).
Catalytic Activity: L-cysteine + O-succinyl-L-homoserine = H(+) + L,L-cystathionine + succinate
Sequence Mass (Da): 68938
Sequence Length: 621
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-cystathionine from O-succinyl-L-homoserine: step 1/1.
EC: 2.5.1.48
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O74314 | MSANISYLVNPPTEVGSSIPADTEHAISVTLPTWKSNVGYEEGDPNVTTKMKSGYPRFFISAHVKDCISIIKKFPEIEILKLKDYDMFLYPSLSVAKQSAAFLESKGPIDSAEVIIYDATKGLRKHLDSIDRNRKYTEEIHIPQVYSVLFPSKYFGIAKQFWQHTGDGISSRRAAAFLHSYKKIQSISEFLVAQRSISHLKSKSRSRYASHPDLQALNTWMTNEGNQANDEMEDVSLYLEERYGRNLDLSLATAAKLVLRRRIAGTLKDEVDLQKALPKEGSQYLREVKGLSHDDVFLFPTGMSAIYNTHRILRLVLDDSRKSVCFGFCYVDTLKILQKWGSGCYFYGLGNDEQLDEFEKRLESGEKVMALFCEFPSNPLLNSPDLVRIRKLADSYDFAVVVDETIGNFVNVEVLPLADVVVSSLTKIFSGDSNVMGGSMVLNPSSRYYSRIKDAMKALYEDLLYDEDALTLERNSRDFAERSQVINHNAETICNLLYQNPKIKTLYYPKYNTSKEHFEACRRENGGYGGLLSVVFHNPEDARQFYDKIQVAKGPSLGTNFTLASPYAILAHYQELDWAGENGIDRNLVRVSVGMEPSEHLKNVFINALS | Function: Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia (By similarity).
Catalytic Activity: L-cysteine + O-succinyl-L-homoserine = H(+) + L,L-cystathionine + succinate
Sequence Mass (Da): 68968
Sequence Length: 610
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-cystathionine from O-succinyl-L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.48
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P47164 | MISRTIGESIPPNTKHAVSVCLPTWEATVGYEEGESSIINSLTTGYPRFFIHKSIKKLCEILSAKYSMEDEACLCFPSYKVANRCREFIKVKTGLSTKVRILQLCTPKPMNQEEKLWRRECKITVVFVDQEIFPVMKQYWQHSGEIVSSRMAEYILHELQVKDNLKKMETVDNGKKFMTEDENRVNEEYIETRFGRNLNFLAADKAKYLIRKRIATKVVEKIDSEGLSDLFSFEHYNESNGPFNVGSGEALDDDQLNSDIPAETITSMGESGSNSTFENTATDDLKFHVNPNTDVYLFPSGMASIFTAHRLLLNFDAKRLSRSSSRQDKLIGYGPPFKKTVMFGFPYTDTLSILRKFNHTHFLGQGDSTSMNALKNILHSGEQILAVFIEAPSNPLLKMGDLQELKRLSDLYSFYIVVDETVGGFVNIDVLPYADIVCSSLTKIFSGDSNVIAGSLVLNPRGKIYEFARKFMKTEDGYEDCLWCEDALCLERNSRDFVERTIKVNTNTDILLKRVLLPQVGKLFKKIYYPSLTSEDTKRNYDSVMSTKDGGYGGLFSLTFFNIEEAKKFFNNLELCKGPSLGTNFTLACPYAIIAHYQELDEVAQYGVETNLVRVSVGLENSDVLCNVFQRAIEKALGE | Function: Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia.
Catalytic Activity: L-cysteine + O-succinyl-L-homoserine = H(+) + L,L-cystathionine + succinate
Sequence Mass (Da): 72351
Sequence Length: 639
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-cystathionine from O-succinyl-L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.48
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O14172 | MASKYQSVQPGGSLIIAWRAQGKKVLIVGGGVVAAGRILHVLNADAHVIVVSPKAGLCKEVAWRIQEKQVEWRDRGFLVEDLSDDVNMVLTAIDDPSLSSEIYKLCKSKKIPVNAADIPPECDFYFGSEIRNGPLQIMVSTNGKGPKLASLIRKKIESSINPATGMALEKTGLLRQKLRDIVPEPENSRKRMRWMIEICELWSLEELAMLDENLINRLLGYFPKKTPSYREITTPAYSKIDNYIWFGAIIISGAVLLKHVSKAR | Function: Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme (By similarity).
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Mass (Da): 29444
Sequence Length: 264
Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1.
Subcellular Location: Cytoplasm
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P15807 | MVKSLQLAHQLKDKKILLIGGGEVGLTRLYKLIPTGCKLTLVSPDLHKSIIPKFGKFIQNEDQPDYREDAKRFINPNWDPTKNEIYEYIRSDFKDEYLDLEDENDAWYIIMTCIPDHPESARIYHLCKERFGKQQLVNVADKPDLCDFYFGANLEIGDRLQILISTNGLSPRFGALVRDEIRNLFTQMGDLALEDAVVKLGELRRGIRLLAPDDKDVKYRMDWARRCTDLFGIQHCHNIDVKRLLDLFKVMFQEQNCSLQFPPRERLLSEYCSS | Function: Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme.
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Mass (Da): 31918
Sequence Length: 274
Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1.
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E3HDJ8 | MCCIAGAPSLSGRERAEKEGIRFKENKGELKIGIINLMPFKEEVEYQFYAVLGRFDISVEVEFLYPENHVFKNTDGSYIKDNYYPLGELNNRNYDAIIMTGAPVELLDFQKVNYWDEIKNLIKSNKLPALYICWGAQAALYVKYGIEKFTLNEKLLGIFRHRTNKNPFVSGEFWAPHSRNTQNSSKDIKNAGLRILAESDEAGVYMASDRDYREFYISGHGEYQRERLKYEYSRDQNLFPKNYFPEDDPKKEPPMKWDSHRKEFYYKWLSHIREKKFSNISDKR | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 33537
Sequence Length: 284
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
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P06721 | MADKKLDTQLVNAGRSKKYTLGAVNSVIQRASSLVFDSVEAKKHATRNRANGELFYGRRGTLTHFSLQQAMCELEGGAGCVLFPCGAAAVANSILAFIEQGDHVLMTNTAYEPSQDFCSKILSKLGVTTSWFDPLIGADIVKHLQPNTKIVFLESPGSITMEVHDVPAIVAAVRSVVPDAIIMIDNTWAAGVLFKALDFGIDVSIQAATKYLVGHSDAMIGTAVCNARCWEQLRENAYLMGQMVDADTAYITSRGLRTLGVRLRQHHESSLKVAEWLAEHPQVARVNHPALPGSKGHEFWKRDFTGSSGLFSFVLKKKLNNEELANYLDNFSLFSMAYSWGGYESLILANQPEHIAAIRPQGEIDFSGTLIRLHIGLEDVDDLIADLDAGFARIV | Function: Primarily catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis . Also exhibits cysteine desulfhydrase activity, producing sulfide from cysteine . In addition, under certain growth conditions, exhibits significant alanine racemase coactivity .
Catalytic Activity: H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate
Sequence Mass (Da): 43212
Sequence Length: 395
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.4.1.13
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P85217 | HDVYGGDYRITGDDGHS | Catalytic Activity: H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate
Sequence Mass (Da): 1864
Sequence Length: 17
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.4.1.13
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Q52811 | MKDKDSLLQNAGINTRLTHIGNDPFDYHGFINPPVVHASTVLFPNARAMETRTQKYTYGTRGTPTTDALCEAIDALEGSAGTILVPSGLAAVTIPFLGFVAAGDHALVVDSVYGPTRHFCDTMLKRLGVEVEYYHPEIGAGIETLFRSNTKLVHTEAPGSNTFEMQDIPAISAVAHRHGAVVMMDNTWATPVYFRPLDHGVDISIHASTKYPSGHSDILLGTVSANAEHWERLKEANGVLGICGAPDDAYQILRGLRTMGLRLERHYESALDIAKWLEGRDDVARVLHPALPSFPSHHLWKRDFKGASGIFSFVLAADGPEKSRAKAHAFLDALRIFGLGYSWGGFESLALHAYLNDRTVAKAPTDGPVIRLQIGIEDVADLKADIERGFAAASAV | Function: Catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis.
Catalytic Activity: H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate
Sequence Mass (Da): 43004
Sequence Length: 396
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.
EC: 4.4.1.13
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Q4L332 | MSLSKETEVIFDEHRGVDYDSANPPLYDSSTFHQKVLGGNAKFDYARSGNPNRQLLEEKLAKLEGGQYAFAYASGIAAISAVLLTLKANDHVILPDDVYGGTFRLTEQILNRFDIQFTTVNATQPKEIERAIQPNTKLIYVETPSNPCFKITDIRAVAAIAKRHHLLLAVDNTFMTPLGQSPLALGADIVVHSATKFLGGHSDIIAGAAITNRKDVADALYLLQNGTGTALSAHDSWTLAKHLKTLPVRFKQSTSNAEKLVAFLKEREEIAEVYYPGNSSLHLSQANSGGAVIGFRLKDETKTQDFVDALTLPLVSVSLGGVETILSHPATMSHAAVPEDVRNERGITFGLFRLSVGLEQPQELIADLNYALKEAFNESIIESITEQRFSS | Function: Catalyzes the transformation of cystathionine into homocysteine . Can also catalyze, at low levels, the conversion of cystathionine into methionine and the conversion of methionine into methanethiol .
Catalytic Activity: H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate
Sequence Mass (Da): 42697
Sequence Length: 391
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.
EC: 4.4.1.13
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P43623 | MIDRTELSKFGITTQLSVIGRNPDEQSGFVNPPLYKGSTIILKKLSDLEQRKGRFYGTAGSPTIDNLENAWTHLTGGAGTVLSASGLGSISLALLALSKAGDHILMTDSVYVPTRMLCDGLLAKFGVETDYYDPSIGKDIEKLVKPNTTVIFLESPGSGTMEVQDIPALVSVAKKHGIKTILDNTWATPLFFDAHAHGIDISVEAGTKYLGGHSDLLIGLASANEECWPLLRSTYDAMAMLPGAEDCQLALRGMRTLHLRLKEVERKALDLAAWLGNRDEVEKVLHPAFEDCPGHEYWVRDYKGSSGLFSIVLKNGFTRAGLEKMVEGMKVLQLGFSWGG | Catalytic Activity: H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate
Sequence Mass (Da): 36971
Sequence Length: 340
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.
EC: 4.4.1.13
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O50008 | MASHIVGYPRMGPKRELKFALESFWDGKSTAEDLQKVSADLRSSIWKQMSAAGTKFIPSNTFAHYDQVLDTTAMLGAVPPRYGYTGGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYLLLSKAAKGVDKSFELLSLLPKILPIYKEVITELKAAGATWIQLDEPVLVMDLEGQKLQAFTGAYAELESTLSGLNVLVETYFADIPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLVKAGFPEGKYLFAGVVDGRNIWANDFAASLSTLQALEGIVGKDKLVVSTSCSLLHTAVDLINETKLDDEIKSWLAFAAQKVVEVNALAKALAGQKDEALFSANAAALASRRSSPRVTNEGVQKAAAALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKVSEEDYVKAIKEEIKKVVDLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPVIYGDVSRPKAMTVFWSAMAQSMTSRPMKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKGGIGVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQDSTQIHTHMCYSHFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSSEEIADRVNKMLAVLEQNILWVNPDCGLKTRKYTEVKPALKNMVDAAKLIRSQLASAK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 84357
Sequence Length: 765
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.1.14
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Q9SRV5 | MASHIVGYPRMGPKRELKFALESFWDGKSSADDLQKVSADLRSDIWKQMSAAGIKYIPSNTFSHYDQVLDTTAMLGAVPSRYGFTSGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVETVPVLVGPVSYLLLSKLAKGVDKSFDLLSLLPKILPVYKEVIAELKAAGASWIQLDEPLFVMDLEGHKLQAFSGAYAELESTLSGLNVLVETYFADIPAEAYKTLTSLKGVTAFGFDLVRGTKTIDLIKSGFPQGKYLFAGVVDGRNIWANDLAASLITLQSLEGVVGKDKLVVSTSCSLLHTAVDLINETKLDAEIKSWLAFAAQKVVEVDALAKALAGQTNESFFTANADALSSRRSSPRVTNESVQKAAAALKGSDHRRTTEVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQEDLDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKGGIGVIQIDEAALREGLPLRKAEHSFYLDWAVHSFRITNCGVQDSTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTDEIADRINKMLAVLEQNILWVNPDCGLKTRKYTEVKPALKAMVDAAKLIRSQLGSAK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 84584
Sequence Length: 765
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.1.14
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Q8XS05 | MTTIHTLGYPRIGAQRELKFALESFWKGASTEADLRDTGRALRERHWNAQRDAGLDFVTVGDFAWYDQVLQTAALLGALPTRYGFDPAQLTLAQSFVLARGNADHAAMEMTKWFDTNYHYLVPELTPDLRFGPGTGWLFDEVREAQAAGHRVKVALLGPVTFLHLAKARGGLADKLSLLPQLLPAYAAVLKRLAAEGVEWVQIDEPALVLDLPQAWSDAYGPAYATLAAAGGPRLLLATYFEAASHHAALIRSLPVAGVHLDLVRAPQQLEAFAPWPADKVLSAGVVDGRNIWRTDLEQALARVAPLAQTLGERLWLAPSCSLLHVPVDLAAETRLDDELKGWLAFARQKLDELAVLKRAVIDGRDAAHAALAGSAAAIASRAASRRVHNDSVKKRAAAIRAQDAERAAPYPVRAAAQQARLNLPLLPTTTIGSFPQTAEIRQARAQYKRGELQALTYLERMRAEIADVVQRQEALGLDMLVHGEAERNDMVEYFGELLWGYAFTANGWVQSYGSRCVKPPVIYGDVYRPEPMTVEWSRYAQSLTAKPMKGMLTGPVTMLQWSFVRDDQPREQTALQIALALRDEVRDLEAAGIAAIQIDEPAFREGLPLRAGDVAVYLEWAARVFRVSASGVRNDTQIHTHMCYSEFNDILPAIASMDADVITIETSRSNMELLDAFGEFAYPNEIGPGVYDIHSPRVPRVEEMEALLDKAAQVVPVQRLWVNPDCGLKTRGWPEVEAALRGMVEATRRLRARHAGAVHAGTPATRAEHAESALA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 85308
Sequence Length: 776
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
EC: 2.1.1.14
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Q0S6X7 | MTFSFTATVLGSPRIGPNRELKKAVESYWAGRLDAEGLDALARDLRRRTWTSLRDAGLDSVPVNTFSYYDHVLDTAAMLGALPDRVAGIESDLDRYFAAARGNDTVAPLEMTRWFDTNYHYLVPEISPTTTFALDPSKVLRELEEARALDIPARPVVVGPVTFLLLSKAVGSDAPLLDRLDELVPLYADLLGRLAGAGADWVQIDEPALVADRNPKEIAAAKRAYDRLSGLELRPAILVASYFGSLGDALPAIASTGVEGIAIDLVAGSDTLATVPDLTRKHVVAGVVDGRNIWRTDLDAALASLGTLLGSTGSLAVSTSCSLLHVPYTLDAETGIDKALRSWLAFGTEKVREVVTLGTALTSGRESVDDEFALARAAASTRNTDRRLHDATVRARLDALTASDPGRSPAAERREAQSALSLPVLPTTTIGSYPQTTQIRVARAARRKGEIDEAEYLKRMRAEVADVVALQEKLDLDVLVHGEPERNDMVQYFAEQLDGFFATDNGWVQSYGSRCVRPPILYGDVRRSNPMTVEWITYAQSLTQRPVKGMLTGPVTILAWSFVRDDQPLADSANQVALAIRDETVDLQGAGIRIVQVDEPALRELLPLRAADQPGYLDWSVGAFRLATSGVSDSTQIHTHLCYSEFGEVIEAIARLDADVTSIEAARSHMEVLDDLSAVGFDLGVGPGVYDIHSPRVPGVEEIAASLREALKAVPVERLWVNPDCGLKTRGPAEVEASLRNLVDAAKLVRAEL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 81533
Sequence Length: 753
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
EC: 2.1.1.14
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Q8EA52 | MTEWNGEYISPYAEHGKKNEQVKKITVSIPLKVLKVLTDERTRRQVNNLRHATNSELLCEAFLHAYTGQPLPDDADLSKECPDSIPAEAKRLMDEMGIEWEDME | Function: This regulatory protein, when combined with SAM (S-adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis.
Sequence Mass (Da): 11959
Sequence Length: 104
Domain: Does not bind DNA by a helix-turn-helix motif.
Subcellular Location: Cytoplasm
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Q72I53 | MRALRLVTSESVTEGHPDKLADRISDAILDALIAQDKKARVAAETLVTTGLVFVAGEITTEGYVDIPNLVRKTVREVGYTRAKYGFDADTCAVLTAIDEQSPDIAGGVNLSYEWRVLKSTDPLDRVGAGDQGLMFGYATDETPELMPLPITLAHRLTMRLAEVRKTGLLPYLRPDGKAQVTVVYEGDKPLYVKTVVVSAQHSPEVEQEQLREDLIREVVRQAIPPEYLKDGETEYLINPSGRFILGGPHADTGLTGRKIIVDTYGGAVPHGGGAFSGKDPTKVDRSASYYARYMAKNIVAAGLARRALVELAYAIGKARPVSLRVETFGTGVLPDEKLTEIAKKVFDPRPLAIIEELDLLRPIYTPTSAYGHFGRPGFPWEETDRVEALRREAGL | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 43247
Sequence Length: 395
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.6
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Q73JR4 | MKNDINYFTSESVSEGHPDKLCDQISDAVLDACLRDDPESHVACETFASTALVLVGGEITTNTYVDIQEIARSIAEEIGYTNTDFGLDCHSMAVMNMIHSQSPDISQGVDGTGLDEYKGQQGAGDQGMMFGFACKETPELMPAPIMFSHSVLRYAAKLRKEKVIPWLRPDSKTQITVKYEGFKPIKIDTVVLSHQHYPDVQYDELKDTLINRVIKPVLGPTGLLADDTKYFINPTGRFVIGGPFGDTGLTGRKIIVDTYGGMGRHGGGAFSGKDPSKVDRSAAYMARYIAKNVVAADLARRCEVQLAYAIGVPFPVAVRVDTFGTGEVPEEKIEKAIKEVFDMSPAGIIKTLDLKRPIYKETAAYGHFGRPEFSWEKTDKTEALKKAIK | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 42736
Sequence Length: 389
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.6
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Q8NSN2 | MSHTASTPTPEEYSAQQPSTQGTRVEFRGITKVFSNNKSAKTTALDNVTLTVEPGEVIGIIGYSGAGKSTLVRLINGLDSPTSGSLLLNGTDIVGMPESKLRKLRSNIGMIFQQFNLFQSRTAAGNVEYPLEVAKMDKAARKARVQEMLEFVGLGDKGKNYPEQLSGGQKQRVGIARALATNPTLLLADEATSALDPETTHEVLELLRKVNRELGITIVVITHEMEVVRSIADKVAVMESGKVVEYGSVYEVFSNPQTQVAQKFVATALRNTPDQVESEDLLSHEGRLFTIDLTETSGFFAATARAAEQGAFVNIVHGGVTTLQRQSFGKMTVRLTGNTAAIEEFYQTLTKTTTIKEITR | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39103
Sequence Length: 360
Subcellular Location: Cell membrane
EC: 7.4.2.11
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Q6A6X6 | MSTDITPSSAPQCPDHIVFEHVTKEFRTRSGTVRALDDVSLAIKRGSISAVIGHSGAGKSTLVRLINGLETPTRGRVLVDGTDVSQLSDKAMRPLRADIGMIFQQFNLFGSRTIYDNVAYPLKLAHWKKADEKKRITELLSFVGLTSKAWDHPDQLSGGQKQRVGIARALATKPSILLADESTSALDPETTADVLSLLKRVNAELGVTVVVITHEMEVVRSIAQQVSVLAAGHLVESGSARQVFAHPQSETTQRFLATIIGQHPNGEEQARLQSENPHARLVDVSSVASHSFGDALARISHTGASFQIVHGGVIEVHDGSLGNYTVALSGPAQAVEQAVQILEEVSNSAAPTTSATVPTPTEEAH | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39015
Sequence Length: 365
Subcellular Location: Cell membrane
EC: 7.4.2.11
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P30750 | MIKLSNITKVFHQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVLVDGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEVKRRVTELLSLVGLGDKHDSYPSNLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLDIPEDYQERLQAEPFTDCVPMLRLEFTGQSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQQDTQAAIAWLQEHHVKVEVLGYV | Function: Part of the ABC transporter complex MetNIQ involved in methionine import . Responsible for energy coupling to the transport system . It has also been shown to be involved in formyl-L-methionine transport .
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37788
Sequence Length: 343
Domain: Contains a regulatory C-terminal extension (C2) with a ferredoxin-like fold. The C2 domains from each MetN subunit in a transporter dimerize to form an eight-stranded beta sheet.
Subcellular Location: Cell inner membrane
EC: 7.4.2.11
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Q5Z1C4 | MSTDQSPCPSATGAELLPPPDGTLAIVPVGDIRLESGAVIPDVHLGVQRWGELSPGLDNVVLVEHALTGDSHVVGPADDVHQLPGWWNGMVGPGAPMDTDEWCVIATNVLGGCKGSTGPGSTAPDGKPWGSRFPAISIRDQVTAEAALFDRIGIHRLAAVVGGSMGGMRVLEWMVGAPERVAAALVLAVGARATADQIGTQTTQIAAITADPDWQGGDYHDTGRAPTTGMGIARRIAHLTYRTEDELDHRFANHAQDGEDPFDGGRWAVQSYLEHQAEKLCRRFDPATYVLLTEAMNRHDVGRGRGGVAAALAATPVPCVVGGVDSDRLYPLHTQQELADLLPGCARLEVVHSRDGHDGFLTETAAIGKLLVETMRLARAHR | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 40409
Sequence Length: 382
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
Q4FP51 | MNINVNIKNIIIDKPLKLDCGQTINNYSLAYETYGSLNENKDNAILIFHALTGDQFVSGINPITKKEGWWSYAVGSGKAIDTDKYFVICANVIGGCMGSYGPSEINPDTNKKYGTTFPVITINDMVNAQFNLLNFFNIEKLFAVMGGSMGGMQTLQFVNNFPDKAKVAIPIACTASHSAQNIAFNELGRQSIMADANWENGDYSNQNKNPNKGLSVARMAAHITYLSKNGLQEKFGRKLQERDDLKFGFDADFQIESYLRYQGSVFVDRFDANSYLYITRAMDYFDLVKEHHGNLSKAFEKTKTKFLIISFTSDWLYPTSENKEIVIALNAIGAEVGFVEIESDKGHDSFLLKVPKFLNTLGDYIKTAYSKN | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 41643
Sequence Length: 372
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
K4ICC9 | MPEIFKYQDPFQLENGEVLPELEVSYSTLGKLNKEKSNVIWVCHALTANAQPEDWWRGLIGNEKGIDTEKYFIVCANIIGSCYGSTNPKSINPETGEVYGLNFPLFSIRDVTKSLELLSEALEIEHIQFLIGGSMGGMQAMEWAIEKPDKIKNLILLATNAKHSSWGIALNETQRMAIEADSTFYKKETNSGKKGLEAARAIALLSYRNYNTYRHTQVDQEHTADHFRASTYQKYQGEKLSKRFNAKCYWYLSKAMDSHNVGRNRGDCKKALAKIKAETLVIAVQSDLLFPVEEQRFLAQYIPKGKLEIIDSIYGHDGFLIEVEKIKSLVHKHFKL | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 38209
Sequence Length: 336
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
Q98G09 | MAALRAGKTNNEADQPSSPVLRFGADKPLKLDAGTLLSPFQIAYQTYGTLNDARSNAILVCHALTGDQHVANTNPVTGKPGWWEVLIGPGRIIDTNRFFVICSNVIGGCLGSTGPASTNPATGKPYGLDLPVITIRDMVRAQQMLIDHFGIEKLFCVLGGSMGGMQVLEWASSYPERVFSALPIATGARHSSQNIAFHEVGRQAVMADPDWHGGKYFENGKRPEKGLAVARMAAHITYLSEAALHRKFGRNLQDREALTFGFDADFQIESYLRHQGMTFVDRFDANSYLYMTRSMDYFDLAADHGGRLADAFAGTKTRFCLVSFTSDWLFPTEESRSIVHALNAAGASVSFVEIETDRGHDAFLLDEPELFAAINGFIGSAARARGLSA | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 42364
Sequence Length: 389
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
Q2S5A6 | MSQTLTVPTLTLENGTTLRDVPVAYRTWGTLNATGTNAVLVCHALTGDTNVADWWGGLLGPGRALDPTEDFVVCLNVPGSPYGSVAPVTVNPDTGERYGAGFPPFTTRDTVRLHRRALETLGVQRVACAVGGSMGGMHVLEWAFEATDDGAPFVRSLVPIAVGGRHTAWQIGWGAAQRQAIFADPKWRDGTYPPDDPPTNGLATARMMAMVSYRSRPSLDGRFGRDAMPEQDGTPYAVESYLHHHGNKLVDRFDANCYVALTRQMDTHDVARGRGDYAKVLRAIEQPSLVVGIDSDVLYPLSEQEELAEHLPSATLEVLSAPHGHDTFLIELDALNDLVSTWRANICSSVAA | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 38064
Sequence Length: 352
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
E0UR96 | MSLNLQTYTEHFTNPLYLESGRILEPYDITYETYGTMNEDKSNVVVVCHALTGSHHAAGLYEDETKPGWWDGFIGSGKAIDTDKYFVICSNVIGSCFGSTGPMSLQHPYQEPYRYKFPVVSIKDMVKAQRILFDRLDIHRVHAIVGGSMGGMQALQFAIHYPNFANKIIALATTHATQPWAIAFNKVAQESILNDPDFKQGYYDPDLLKEQGLSGMAVGRMAGHISFLSHESMREKFGRDYKLTDGLYELFGKFQVESYLEYNGYNFTKWFDPLAYLYITKAINIYDLSRGFDSLAEALKRVTSALYLVSFKNDLLFKNFEMKEIADELDKIGNKNHSYIDVKSDYGHDAFLVELNKFENHVKDALNG | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 41872
Sequence Length: 368
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
Q67NS3 | MNAAPVPILLTQRRYARVATPENPLVLESGQRLTDVTLCYEVFGRLNPAGDNAILVCHALTGDSHVAGRYRPDDPKPGWWDDAVGPGKALDTDRYCVICSNVLGGCQGSTGPSSVNPATGRPYGLDFPLVTVRDMVRAQARLLDLLGVRRLLAVIGGSLGAMQALEWAATYPDRMRGIIPIGGAGRFHPQGIAFNEVQRQAILNDPGFLGGQYYGTPGPVRGLATARMLGMITYRSDESMWTQFGRNPQGEANPLHQGFAVAYQVESYLHYQGRKLVERFDANSYLYLTRAMDLMDLGRGRGSYEEAHARIQARVLAVGIRSDLLFPTYLQRETVELVRASGGRAEYVEMDSPWGHDAFLLDFPLIEEPIRRFLQELEAEENA | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 42255
Sequence Length: 383
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
Q47L17 | MSHDTTPPLPATGAWREGDPPGDRRWVELSEPLPLETGGELPGVRLAYETWGSLNEDRSNAVLVLHALTGDSHVVGPEGPGHPSPGWWEGIIGPGLALDTDRYFVVAPNVLGGCQGSTGPSSTAPDGRPWGSRFPRITIRDTVRAEFALLREFGIHSWAAVLGGSMGGMRALEWAATYPERVRRLLLLASPAASSAQQIAWAAPQLHAIRSDPYWHGGDYYDRPGPGPVTGMGIARRIAHITYRGATEFDERFGRNPQDGEDPMAGGRFAVESYLDHHAVKLARRFDAGSYVVLTQAMNTHDVGRGRGGVAQALRRVTARTMVAGVSSDFLYPLAQQQELADGIPGADEVRVIESASGHDGFLTEINQVSVLIKELLAQ | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 40833
Sequence Length: 379
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
Q9RA51 | MSEIALEAWGEHEALLLKPPRSPLSIPPPKPRTAVLFPRREGFYTELGGYLPEVRLRFETYGTLSRRRDNAVLVFHALTGSAHLAGTYDEETFRSLSPLEQAFGREGWWDSLVGPGRILDPALYYVVSANHLGSCYGSTGPLSLDPHTGRPYGRDFPPLTIRDLARAQARLLDHLGVEKAIVIGGSLGGMVALEFALMYPERVKKLVVLAAPARHGPWARAFNHLSRQAILQDPEYQKGNPAPKGMALARGIAMMSYRAPEGFEARWGAEPELGETYLDYQGEKFLRRFHAESYLVLSRAMDTHDVGRGRGGVEEALKRLRAIPSLFVGIDTDLLYPAWEVRQAAKAAGARYREIKSPHGHDAFLIETDQVEEILDAFLP | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 42251
Sequence Length: 380
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
|
Q69Z36 | MPSSLFADLERNGSGGGGGGGGGGGGGGSGGGETLDDQRALQLALDQLSLLGLDSDEGASLYDSEPRKKSVNMTECVPVPSSEHVAEIVGRQGGSGRDGDRRGFSISPTPSLEPWLPGCKIKALRAKTNTYIKTPVRGEEPVFVVTGRKEDVAMARREIISAAEHFSMIRASRNKNTALNGAVPGPPNLPGQTTIQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVDRAREEIEAHIALRTGGIIELTDENDFHANGTDVGFDLHHGSGGSGPGSLWSKPTPSITPTPGRKPFSSYRNDSSSSLGSASTDSYFGGGTSGSAAATSRLADYSPPSPALSFAHNGNNNNNGNGYTYTAGEASVPSPDGGPELQPTFDPAPAPPPGTPLLWAQFERSPGGGSAAPVSSSCSSSASSSASSSSVVFPGGGASSTPSNANLGLLVHRRLHPGTSCPRLSPPLHMATGAGEHHLARRVRSDPGGGGLAYAAYANGLGTQLPGLPSSDTSGSSSSSSSSSSSSSSSSGLRRKGSRDCSVCFESEVIAALVPCGHNLFCMECANRICEKSEPECPVCHTAVTQAIRIFS | Function: RNA-binding protein. May be involved in post-transcriptional regulatory mechanisms (By similarity).
PTM: Phosphorylation at Ser-494 creates a docking site for 14-3-3, which stabilizes the protein and modulates its ability to bind RNA.
Sequence Mass (Da): 61781
Sequence Length: 601
Domain: Binds RNA through its KH domains.
Subcellular Location: Cytoplasm
|
A1L3F4 | MPSSLFADMERNGSGGGGGETLDDQRALQIALDQLSLLGLDNDESAMYDNEPRKKSINMTECVQVPSSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEEPVFVVTGRKEDVALARREIISAAEHFSMIRASRNKNAAALNGGSVPAPPNLPGQTTIQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVDRAREEIEAHIAVRTGGLIEVADENDFHANGTDVGFDLHGSLWSKSNQSSGSRKALSNYRNDSSSSLGSASTDSYFGGTRMADYSPPSPDLSYTNNNNNNNGNGYVYSTGISPDCTDLTFESGFDPAPAPPPSAYTWSQLERSTGSAPYHNNANGILLNQRRLNGVGCTTAPRLSPPLHTCNGLSEHPLARRVRSDPGGGLSYSAYSNMACDSSSSSSSSSSSSSSSSSSSSSSSSSGMRRKGSRECSICFESEVIAALVPCGHNLFCMECANRICEKNQPQCPVCHAGVTQAIRIFS | Function: RNA-binding protein. May be involved in post-transcriptional regulatory mechanisms (By similarity).
Sequence Mass (Da): 54164
Sequence Length: 507
Domain: Binds RNA through its KH domains.
Subcellular Location: Cytoplasm
|
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