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stringlengths 6
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stringlengths 11
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stringlengths 108
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Q9X839 | MTQQPFQLPHFYLPHPARLNPHLDEARAHSTTWAREMGMLEGSGVWEQSDLEAHDYGLLCAYTHPDCDGPALSLITDWYVWVFFFDDHFLEKYKRSQDRLAGKAHLDRLPLFMPLDDAAGMPEPRNPVEAGLADLWTRTVPAMSADWRRRFAVATEHLLNESMWELSNINEGRVANPVEYIEMRRKVGGAPWSAGLVEYATAEVPAAVAGTRPLRVLMETFSDAVHLRNDLFSYQREVEDEGELSNGVLVLETFFGCTTQEAADLVNDVLTSRLHQFEHTAFTEVPAVALEKGLTPLEVAAVGAYTKGLQDWQSGGHEWHMRSSRYMNKGERPLAGWQALTGPGTSAADVGALLADAVAQRARSYTYVPFQKVGPSVIPDIRMPYPLELSPALDGARRHLSEWCREMGILSEGVWDEDKLESCDLPLCAAGLDPDATQDQLDLASGWLAFGTYGDDYYPLVYGHRRDLAAARLTTTRLSDCMPLDGEPVPPPGNAMERSLIDLWVRTTAGMTPEERRPLKKAVDDMTEAWLWELSNQIQNRVPDPVDYLEMRRATFGSDLTLGLCRAGHGPAVPPEVYRSGPVRSLENAAIDYACLLNDVFSYQKEIEYEGEIHNAVLVVQNFFGVDYPAALGVVQDLMNQRMRQFEHVVAHELPVVYDDFQLSEEARTVMRGYVTDLQNWMAGILNWHRNVPRYKAEYLAGRTHGFLPDRIPAPPVPRSSPALTH | Cofactor: Magnesium. Fe(2+) or Cu(2+) ions are very less efficient as cofactors.
Function: Tow-domain protein where the N-terminal domain catalyzes the cyclization of farnesyl diphosphate (FPP) to a 85:15 mixture of the sesquiterpene alcohol germacradienol and the sesquiterpene hydrocarbon germacrene D. The C-terminal domain partially converts the germacradienol formed into geosmin, the characteristic odoriferous ('earthy aroma') constituent of Streptomyces species.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O = (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + diphosphate
Sequence Mass (Da): 81474
Sequence Length: 726
Domain: Consists of 2 homologous sesquiterpene synthase domains. The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; geosmin biosynthesis.
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P38909 | MLWKNYVLSSSRITRRLHKSPRKSSFSKNFFITGCLLTVGAVSSYLTYRYTSERENKHELSPSYFVKYKISHKRDIDSSHFLLEVTPLFKQKVNIWSLMTAENLWSVEIKQPEVMVVRNYTPLPLKFNPASKEIEILKDGDNADGKLSFYIKKYENGEVARWLHHLPKGHIIEIRGPFIDYEFPHLPNELKRSRDCLYMDNRNERGNNVRENSQFIYQPYDIMMFTAGTGIVTALQLLLTESPFRGTIKLFHTDKNIKQLGPLYPILLRLQASNRVQLKIFETDRQTKQDVLKSIQKSITKPYPYKGLLPFSNVNNKNIMPVLALVCGPESYISSISGRKYDLNQGPVGGLLSKEGWNSDNVYKLS | Cofactor: Binds 1 FAD per monomer.
Function: Redox component that participates in c-type cytochrome biogenesis in the mitochondrial intermembrane space. May play a role in the reduction of heme prior to its ligation to apocytochrome c by cytochrome c heme lyase. Has oxidoreductase activity in vitro.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42368
Sequence Length: 366
Subcellular Location: Mitochondrion inner membrane
EC: 1.-.-.-
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P81078 | ADSLTQFDGIKGRYSHEAFYEEKACDSCHLNK | Function: Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin.
PTM: Binds 1 heme group per subunit.
Sequence Mass (Da): 3664
Sequence Length: 32
Subcellular Location: Periplasm
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P00076 | GDAERGKKLFESRAAQCHSAQKGVNSTGPSLWGVYGRTSGSVPGYAYSNANKNAAIVWEEETLHKFLENPKKYVPGTKMAFAGIKAKKDRQDIIAYMKTLKD | Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 11210
Sequence Length: 102
Subcellular Location: Mitochondrion intermembrane space
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P00004 | MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE | Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 11833
Sequence Length: 105
Subcellular Location: Mitochondrion intermembrane space
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P99999 | MGDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE | Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 11749
Sequence Length: 105
Subcellular Location: Mitochondrion intermembrane space
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Q2JUP0 | MKRIYLALCALLLLLGTGSRPAAAYPYYAQMAYDNPREATGKIVCANCHLNAMPARAEVPQAVTPGQVFTIKVGIPYDLSKQQVLADGSKGGLNVGAVVVLPEGFRLATEEEMTEEQRQETAETYITPYSDEKPNILLVGPLPGEQHQEIVFPVVAPDPKEDPSVAFMKYRVYIGANRGRGQINPDGSLSNNNVFRAPATGRLTSIATIESDLSDLPPELAALVPPEYELPGTRVLSFETEGGLKHLVVPPGPELVVNIGDSVQEGDPVTNNPNVGGFGQVERDLVLQNPERVKWLVAFLAAVAITQLLLVLKKKQVELIQAAELLG | Cofactor: Binds 1 heme group covalently.
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 35284
Sequence Length: 327
Subcellular Location: Cellular thylakoid membrane
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A8NV38 | MTPAVSPAHTVLFEAKARKGISFEQIGKAIGRDEVWVASAFYGQAKFNEEELKKLSEVLEISSAQIVKELGDQWFPNRGLGPVPPSDPVIYRLFEGVLVYGHPIKAIIHEKFGDGIMSMIDCNINVERKPDPKGDRVVVTFDGKFLPYSKW | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 16876
Sequence Length: 151
EC: 4.2.1.104
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P0CN03 | MFNLPYHCKALLTAKQERGLTFDDVAKAINKPEVWTTALFYGQASTDKSTAEAILKALGGEQFWTDYNDRLEAGQEKIDIRRVLNGLSGNGEENMGVKGMVTRGATFEVPPKDPVLYRLYEVLVVYGYSYKALIYEKFGDGIMSAIDFRTSLERKKDPKGDRVVITMDGKFLPYSDPSAWGTQ | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 20538
Sequence Length: 183
EC: 4.2.1.104
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Q0K572 | MNRSDVTDLIIEAKVTRGIAWAQVAERVGRSKEWTTAACLGQMAFDAAGARAVMELFGLPPEAEPWLREVPYKGSLPTQVPADPLIYRFYELISVYGTTFKALIHEEFGDGIMSAIDFRMDLQREPDPNGDRVRIEMSGKFLPYKTY | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 16578
Sequence Length: 147
EC: 4.2.1.104
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P58704 | MIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARQVGAKLDLDEDAILLLQMIPLRGCIDDRIPTDPTMYRFYEMLQVYGTTLKALVHEKFGDGIISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPF | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 17048
Sequence Length: 156
EC: 4.2.1.104
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P0ABJ0 | MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQFHTMLMIAASGAVLIALGILCLVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGEAYKKPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQHFDEITKAGLKNGN | Cofactor: Binds 1 copper B ion per subunit.
Function: Cytochrome bo(3) ubiquinol oxidase is the terminal enzyme in the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Catalyzes the four-electron reduction of O2 to water, using a ubiquinol as a membrane soluble electron donor for molecular oxygen reduction; ubiquinol-8 is the natural substrate for E.coli. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron and generating a proton motive force. All the redox centers of this enzyme complex are located within the largest subunit, subunit I. Protons are probably pumped via D- and K- channels found in this subunit.
Catalytic Activity: 2 a ubiquinol + n H(+)(in) + O2 = 2 a ubiquinone + n H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74368
Sequence Length: 663
Subcellular Location: Cell inner membrane
EC: 7.1.1.3
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Q9I426 | MFGKLTLSAVPYHEPIVMVTLAVVALLGLGVVGAITYYRKWTYLWTEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLALAEGANHGYLPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPEVYILILPAFGIFSEVTATFAGKRMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNPLWKPYLVVAFFGAVLIFCGIACQLIQLFVSVRNRKQLADVNGDPWEGRTLEWATSSPPPFYNFAELPKVQDVDAFHDMKKAGTAYRKLPAYQPIHMPKNTAAGFSIAVFAFVFGFAAIWHIWWLMAVGFVGMIGSFIVRSYNQDVDYYVQPEEIEKIESARFQQLAKQV | Cofactor: Binds 1 copper B ion per subunit.
Function: Cytochrome bo(3) ubiquinol oxidase is the terminal enzyme in the aerobic respiratory chain. Catalyzes the four-electron reduction of O2 to water, using a ubiquinol as a membrane soluble electron donor for molecular oxygen reduction. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron and generating a proton motive force. All the redox centers of this enzyme complex are located within the largest subunit, subunit I. Protons are probably pumped via D- and K- channels found in this subunit.
Catalytic Activity: 2 a ubiquinol + n H(+)(in) + O2 = 2 a ubiquinone + n H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73934
Sequence Length: 658
Subcellular Location: Cell inner membrane
EC: 7.1.1.3
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P57542 | MIENKFNNTILNSNSSTHDKISETKKLFGLWIYLMSDCIMFAVLFAVYAIVSSNISINLISNKIFNLSSILLETFLLLLSSLSCGFVVIAMNQKRIKMIYSFLTITFIFGLIFLLMEVHEFYELIIENFGPDKNAFFSIFFTLVATHGVHIFFGLILILSILYQIKKLGLTNSIRTRILCFSVFWHFLDIIWICVFTFVYLNGAI | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23639
Sequence Length: 205
Subcellular Location: Cell membrane
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Q89AA5 | MKKKYKIDTNIFSKELLGFWLYLMSDCIIFCTLFSVYFILVDNVAQGPSGHNIFQNNLIIIETFLLLFSSFSCNLVLFEMKNKNLYMVFLWLGITFLLGLLFVFLELFEFFHLINLGFGPTRSGFLSSFFVLIATHGIHVISGLIWIIVMIKYVYTFNITNLIYYRMLCLNLFWHFLDIVWVFIFSFVYLFGMV | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22941
Sequence Length: 194
Subcellular Location: Cell membrane
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Q9I425 | MSTAVLNKHLADAHEVGHDHDHAHDSGGNTVFGFWLYLMTDCVLFASVFATYAVLVHHTAGGPSGKDIFELPYVLVETAILLVSSCTYGLAMLSAHKGAKGQAIAWLGVTFLLGAAFIGMEINEFHHLIAEGFGPSRSAFLSSFFTLVGMHGLHVSAGLLWMLVLMAQIWTRGLTAQNNTRMMCLSLFWHFLDIVWICVFTVVYLMGAL | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22847
Sequence Length: 209
Subcellular Location: Cell inner membrane
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Q8K996 | MNKYKKIKNNFDKEKKSYIVGFLFSLFLTIIPFFCTLNHLFSRKINFFVILLCALSQIIIHFIYFLHLDFSKKNSWNIISLLFILIIVFIIVFGSIWIMYNLNHHVIL | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12995
Sequence Length: 108
Subcellular Location: Cell membrane
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Q89AA6 | MLKNRYLKYLFILILLSILSIMPIFAIIYRIFSRNYLYAFIIVCLFFQILAHIKFFLNLDFSLEQRWKLISVIFSLVVGLIILLGSIWVIKNLNNNLCIM | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11923
Sequence Length: 100
Subcellular Location: Cell membrane
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P0ABJ7 | MSHSTDHSGASHGSVKTYMTGFILSIILTVIPFWMVMTGAASPAVILGTILAMAVVQVLVHLVCFLHMNTKSDEGWNMTAFVFTVLIIAILVVGSIWIMWNLNYNMMMH | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12029
Sequence Length: 109
Subcellular Location: Cell inner membrane
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Q9I424 | MSSAAHDNHGAGHGSLGSYAIGFVLSVILTAIPFYMVMDGGFSRHATILTMVVLGLVQVVVHLICFLHMNMSSEGRWNVMAFIFTVIVILLVVGLSLWIIFSADMLMMPMP | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12070
Sequence Length: 111
Subcellular Location: Cell inner membrane
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Q9MUN1 | MSILIDNISKKFGNFQALNHINLEIKSGSIIALLGPSGSGKSTLLRIIAGLDTPDEGTIWISGKNASGYSIQSRNIGFVFQNYALFKNMTVYDNIAFGLELRRISFNDISRKVNKLLELVQLQNLGHRYPAQLSGGQRQRIALARALAIEPKVLLLDEPFGALDARVRKNLRAWLRDLHNKFSITTIIVTHDQQEAMEIADEIVVFNSGRIEQIGKPQDIYDQPATPFVFSLLGYVNKISFDNEIANFLLSSFPEKQSVLMQEKQFYIRPHQIVISKQSNESNYSAKIENLLYIGNWIHLDIYVASFNVNLKVHVSPKEFDNLQLKSFQENIYVSLRSKGKEPIRFLE | Function: Part of the ABC transporter complex involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in)
Sequence Mass (Da): 39517
Sequence Length: 348
Subcellular Location: Plastid
EC: 7.3.2.3
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P0A4W3 | MTYAIVVADATKRYGDFVALDHVDFVVPTGSLTALLGPSGSGKSTLLRTIAGLDQPDTGTITINGRDVTRVPPQRRGIGFVFQHYAAFKHLTVRDNVAFGLKIRKRPKAEIKAKVDNLLQVVGLSGFQSRYPNQLSGGQRQRMALARALAVDPEVLLLDEPFGALDAKVREELRAWLRRLHDEVHVTTVLVTHDQAEALDVADRIAVLHKGRIEQVGSPTDVYDAPANAFVMSFLGAVSTLNGSLVRPHDIRVGRTPNMAVAAADGTAGSTGVLRAVVDRVVVLGFEVRVELTSAATGGAFTAQITRGDAEALALREGDTVYVRATRVPPIAGGVSGVDDAGVERVKVTST | Function: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37444
Sequence Length: 351
Subcellular Location: Cell membrane
EC: 7.3.2.3
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Q73XU8 | MIDAGTDRGDIAITVRDAYKRYGDFVALDHVDFVVPTGSLTALLGPSGSGKSTLLRTIAGLDQPDTGTVTIYGRDVTRVPPQRRGIGFVFQHYAAFKHLTVRDNVAYGLKVRKRPKAEIKAKVDNLLEVVGLSGFQGRYPNQLAGGQRQRMALARALAVDPQVLLLDEPFGALDAKVREDLRAWLRRLHDEVHVTTVLVTHDQAEALDVADRIAVLNQGRIEQIGSPTEVYDAPTNAFVMSFLGAVSTLNGTLVRPHDIRVGRTPEMAVAAEDGTAESTGVARAIVDRVVKLGFEVRVELTSAATGGPFTAQITRGDAEALALREGDTVYVRATRVPPITAGATTVPALSRDGADEATLTSA | Function: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38813
Sequence Length: 362
Subcellular Location: Cell membrane
EC: 7.3.2.3
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Q5YZY9 | MITVTNARKNYGNFAALDDVTIEIPSGELTALLGPSGSGKSTLLRSIAGLEALDDGVVVIAGKDVTRVAPQKRDIGFVFQHYAAFKHMTVRDNVAFGLKIRKRPKAEITKRVDELLGIVGLDGFQHRYPAQLSGGQRQRMALARALAVDPQVLLLDEPFGALDAKVRADLRTWLRRLHEEVHVTTVLVTHDQEEALDVADRIAVMNKGRIEQVGTPEDVYDRPANEFVMSFLGDVARLNGHLVRPHDIRVGRDPSMALAAHEGTAESAGVTRATVERVVHLGFEVRVELRNAATGDLFSAQVTRGDAEALRLTDGETVYARATRIPELPTQ | Function: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36232
Sequence Length: 331
Subcellular Location: Cell membrane
EC: 7.3.2.3
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Q8Z0H0 | MGIVVENVSKQFGSFRAVDQVNLEIQSGKLVALLGPSGSGKSTLLRLIAGLEKPDDGRIILTGKDATNQSVQERNIGFVFQHYALFKHLTVRQNIAFGLEIRKAPANKVKGRVEQLLELVQLSGLGDRYPSQLSGGQRQRVALARALAVEPSVLLLDEPFGALDAKVRKDLRAWLRRLHDEVHVTTVFVTHDQEEAMEVSDEVVVMNQGRVEQVGTPAEIYDNPATSFVMSFIGPVNVLPSSSRIFQSSQLEIEHPNVFLRPQDVVIEKSANGTTAPATVTRLIHLGWEIKVELTLDDGQVVNAHLTRDRYDELQLEPKQKVYVKPKDAKSFPLYYSI | Function: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37567
Sequence Length: 338
Subcellular Location: Cell inner membrane
EC: 7.3.2.3
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Q9I6L0 | MSIEIRNVSKNFNAFKALDDINLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDAGNIVFHGEDVSQHDVRDRNVGFVFQHYALFRHMTVFDNVAFGLRMKPKGERPGESAIKAKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKILLLDEPFGALDAKVRKELRRWLARLHEEINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGEVYENPASDFVYHFLGDSNRLQLGNDQHLLFRPHEVSLSRSAVAEHRAAEVRDIRPLGAITRVTLKVDGQDELIEAEVVKDHDSLAGLARGETLYFKPKAFQPVANL | Function: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36795
Sequence Length: 329
Subcellular Location: Cell inner membrane
EC: 7.3.2.3
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Q12QM6 | MTDIVWHQHSIDQAARGAQKSQNPVLLWFTGLSGAGKSTLAGALERALFDAGFHTYLLDGDNVRHGLCKDLGFSLSDRDENLRRVGEVAKLMVDAGLVVLSAFISPTRAERDRVRALFPEGRFIEVHVSTPLSVCEARDPKGLYVKARSGEIKEFTGISSPYEAPTAAELTIDTSRGDLATQVQAMLAYLTAIEVIDANKLSALA | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 22214
Sequence Length: 205
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
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Q8EB13 | MSNIVWHQHSVDQAARARLKGQNPVLLWFTGLSGAGKSTLAGALERALFEAGFHTYLLDGDNVRHGLCKDLGFSVADRDENLRRVGEVAKLMVDAGLVVLSAFISPTREERDSIRARFPEGQFIEVHVSTPLSVCELRDPKGLYVKARKGEIAHFTGISSPYEAPLSAELTIDTSKGDLASQVHALIDYLTAIDVISSNRLASLA | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 22298
Sequence Length: 205
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
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P06106 | MPSHFDTVQLHAGQENPGDNAHRSRAVPIYATTSYVFENSKHGSQLFGLEVPGYVYSRFQNPTSNVLEERIAALEGGAAALAVSSGQAAQTLAIQGLAHTGDNIVSTSYLYGGTYNQFKISFKRFGIEARFVEGDNPEEFEKVFDERTKAVYLETIGNPKYNVPDFEKIVAIAHKHGIPVVVDNTFGAGGYFCQPIKYGADIVTHSATKWIGGHGTTIGGIIVDSGKFPWKDYPEKFPQFSQPAEGYHGTIYNEAYGNLAYIVHVRTELLRDLGPLMNPFASFLLLQGVETLSLRAERHGENALKLAKWLEQSPYVSWVSYPGLASHSHHENAKKYLSNGFGGVLSFGVKDLPNADKETDPFKLSGAQVVDNLKLASNLANVGDAKTLVIAPYFTTHKQLNDKEKLASGVTKDLIRVSVGIEFIDDIIADFQQSFETVFAGQKP | Function: Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway . Required to efficiently reduce toxic levels of hydrogen sulfide generated when the sulfate assimilation pathway (SAP) is active . Also catalyzes the conversion of O-acetylserine (OAS) into cysteine, the last step in the cysteine biosynthesis pathway . However, it seems that in S.cerevisiae cysteine biosynthesis occurs exclusively through the cystathionine pathway and not via direct incorporation of sulfur into OAS . It therefore has no metabolic role in cysteine biosynthesis and may only have a regulatory role controlling OAS levels .
Catalytic Activity: methanethiol + O-acetyl-L-homoserine = acetate + H(+) + L-methionine
Sequence Mass (Da): 48672
Sequence Length: 444
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from O-acetyl-L-homoserine.
Subcellular Location: Cytoplasm
EC: 2.5.1.47
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O65039 | MQKFILLALSLALVLAITESFDFHEKELESEESLWGLYERWRSHHTVSRSLHEKQKRFNVFKHNAMHVHNANKMDKPYKLKLNKFADMTNHEFRNTYSGSKVKHHRMFRGGPRGNGTFMYEKVDTVPASVDWRKKGAVTSVKDQGQCGSCWAFSTIVAVEGINQIKTNKLVSLSEQELVDCDTDQNQGCNGGLMDYAFEFIKQRGGITTEANYPYEAYDGTCDVSKENAPAVSIDGHENVPENDENALLKAVANQPVSVAIDAGGSDFQFYSEGVFTGSCGTELDHGVAIVGYGTTIDGTKYWTVKNSWGPEWGEKGYIRMERGISDKEGLCGIAMEASYPIKKSSNNPSGIKSSPKDEL | Function: Involved in programmed cell death. Shows a pronounced preference for hydrophobic residues in the P2 position and no obvious preference in the P1 position of the cleavage site. Accepts proline at the P1 and P1' positions.
PTM: The potential N-glycosylation site at Asn-115 is not glycosylated.
Sequence Mass (Da): 40111
Sequence Length: 360
Subcellular Location: Cytoplasmic vesicle
EC: 3.4.22.-
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O06737 | MNETITYDTWNDMLSKQITDQLIDELDVLKWAYRTYGEKIVYACSFGAEGMVLLDLISKINKNAHIIFLDTGLHFQETYELIETVKERYPGFAIQMLEPELSLTEQGTKYGGELWKHNPNLCCQLRKIEPLKKHLSGMTAWISGLRRDQSPTRKHIQYVNLDQKFELIKICPLIHWTWDDVWTYIRLHNLPYNKLHDQHYPSIGCEMCTLPSPDPNDERAGRWAGREKTECGLHQE | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
Catalytic Activity: [thioredoxin]-disulfide + AMP + 2 H(+) + sulfite = [thioredoxin]-dithiol + adenosine 5'-phosphosulfate
Sequence Mass (Da): 27671
Sequence Length: 236
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate.
Subcellular Location: Cytoplasm
EC: 1.8.4.10
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Q5WKF5 | MAYVFEQMEATDYEKVNTKLKNRDSLDILRWANQTYGEKLVYACSFGAEAMVLLDLLSKIQKEAHILFLDTDFHFAETYELIERVKERYPTFRINMAKPALSPEEQAERYGDELWLKNPDQCCQIRKLDVLARELEPYDAWLSGLRREQSPTRANTEFVNQDKRFKKVKVCPLIHWTEEEIWMYIKLHQLPYNELHDQHYPSIGCTYCTKAVMPGEDARSGRWAGTGKTECGLHAPTKGDS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
Catalytic Activity: [thioredoxin]-disulfide + AMP + 2 H(+) + sulfite = [thioredoxin]-dithiol + adenosine 5'-phosphosulfate
Sequence Mass (Da): 28151
Sequence Length: 241
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate.
Subcellular Location: Cytoplasm
EC: 1.8.4.10
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D3RNJ4 | MTERRQPSLSTDTLPTREAAAIELLSQVCRELDSIVFATSLGAEDMVLTEIIRRERLPIRIFTLDTGRLPTETLELIEVVERHYGTRIERYAPHPDAIADYVSRYGLDGFYDSVPARQACCRVRKLEPLKRALAGQSAWVTGLRAEQSVTRAELPAREWDAANGLEKINPLADWSEHEVWAFIRHHRVPYNPLHNQGYPSIGCAPCTRAITVGEDVRAGRWWWENPETKECGLHRREFAPRQPSAHPAIERDRSAA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
Catalytic Activity: [thioredoxin]-disulfide + AMP + 2 H(+) + sulfite = [thioredoxin]-dithiol + adenosine 5'-phosphosulfate
Sequence Mass (Da): 29144
Sequence Length: 256
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate.
Subcellular Location: Cytoplasm
EC: 1.8.4.10
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B4RYS5 | MTNSTAEKQQPLTLDISKEALADINDMLEKTTAQQRVAWALNNLPDTHIVSSSFGAQSAVMLHMLTQVQPDIPVVLTDTGYLFPETYKFIDELVEKLNLNLHVYRADMSSAWQEARFGRLWEQGVEGIEKYNKLNKVEPMQRALRELNAGTWFAGLRRSQSDTRGKLPVLQKVGQQFKLYPIIDWSNKDLHYYLKDNELSYHPLWEQGYVSIGDWHTTQSLQEGMSEQDTRFFGLKRECGLHEFGDGI | Function: Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor.
Catalytic Activity: [thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2 H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol
Sequence Mass (Da): 28527
Sequence Length: 248
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 3/3.
Subcellular Location: Cytoplasm
EC: 1.8.4.8
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O32213 | MVTKILKAPDGSPSDVERIKKESDYLRGTLKEVMLDRISAGIPDDDNRLMKHHGSYLQDDRDLRNERQKQKLEPAYQFMLRVRMPGGVSTPEQWLVMDDLSQKYGNGTLKLTTRETFQMHGILKWNMKKTIQTIHSALLDTIAACGDVNRNVMCASNPYQSEIHSEVYEWSKKLSDDLLPRTRAYHEIWLDEERVAGTPEEEVEPMYGPLYLPRKFKIGIAVPPSNDIDVFSQDLGFIAIVEDGKLIGFNVAIGGGMGMTHGDTATYPQLAKVIGFCRPEQMYDVAEKTITIQRDYGNRSVRKNARFKYTVDRLGLENVKEELENRLGWSLEEAKPYHFDHNGDRYGWVEGIEDKWHFTLFVEGGRITDYDDYKLMTGLREIAKVHTGEFRLTANQNLMIANVSSDKKEEISALIEQYGLTDGKHYSALRRSSMACVALPTCGLAMAEAERYLPTLLDKIEEIIDENGLRDQEITIRMTGCPNGCARHALGEIGFIGKAPGKYNMYLGAAFDGSRLSKMYRENIGEADILSELRILLSRYAKEREEGEHFGDFVIRAGIIKATTDGTNFHD | Cofactor: Binds 1 siroheme per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate (Probable).
Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite
Sequence Mass (Da): 64810
Sequence Length: 571
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1.
EC: 1.8.1.2
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A9IT77 | MQSTDNDLSQSPPKLSADEQLKAASDQLRGTILRSLADPLTGAVSDSDAKLLKFHGIYQQDDREQRDERRRQKLEPAYQFMIRVRLPGGVCSAAQWLKLDELARAYGGDSLRLTTRQTFQFHWVLKHNLQATLQGLHEVLLDTIAACGDDARGVMCTADPRLSALHAAVYDIARQASDHAIPRMRAYHEIWWGEQRVASSDAGPEEPFYGQTYLPRKFKIGFVIPPVNDIDVYAQDLGFIAIAGDDGALQGFNVAIGGGMGRTDQAPATYPRLADVIGFVPPEAVIATCDAVMGVQRDYGNRKDRARARFKYTIDEHGLDAVKAEIERRLGFALQPARPFRFDSNGDALGWQTGEDGRHHVTLFIQNGRLVNLPGLPLLEGLREIARVHTGSFRITPNQNVVIADIGDAERPRIEALLRQYQLEAGPSTSALRLNSMACVALPTCGLAMAESERYLPELVGKIEALLRTHGLEREPITIRMSGCPNGCSRPYIAEIGLTGRAPGKYNLYLGGGFHGQRLNRMVLENAAEAAILALLDTTLAHYARDRHEGEHFGDFAVRAGYVEAVTAGRDFNQRRAPGAGATAPHA | Cofactor: Binds 1 siroheme per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite
Sequence Mass (Da): 64505
Sequence Length: 587
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1.
EC: 1.8.1.2
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P0C0B2 | MKKDYKKVFLKNTKEERIKENSNYLRGTIIDDLKDEITNGFTGDNFSLIRFHGMYQDDRDLRLERNEQKLEPRYAMMLRCRLPRGIIKAKKWLKIDHFASKNTLYGTIRLNNLQTFQFHGILKKTLKDAHKMLNKIGLDSLGTANDVNRNVLCTSNPMESLIHQQCYEWVSKISNFLLPQTKAYAEIWLNQKKIATTDQEPILGKTYLPRKFKTTVVVPPYNDVDLYANDMNFIAITKNNKIVGFNVLIGGGLSINHGNKNTWPFLAVELGYITLEKTLSVAESIVTTQRDWGNRTDRKNAKTRYTIAKVGLSVFKKEVEKRANMTFETIKPYYFISRGDRFGWTKNINNDWSLTVFIQNGRIYDNDKQLVKSGLLKIANLHTGNFRLTANQNIVISEILDKNKKKIEEIAISHGLIKKVSSLRENSMACVSFPTCPLAIAESERILSFFITKVENIMLKYGIEKEIIILRISGCPNGCGRSLLAEIGLIGKSLGRYNLYIGGNRIGSRIPKIYKENITEQEILIHLDFLIKIWSIERQKKEHFGDFVIRRNVVKKVVNPIYDFWN | Cofactor: Binds 1 siroheme per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite
Sequence Mass (Da): 65353
Sequence Length: 566
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1.
EC: 1.8.1.2
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Q9JS45 | MSEHDMQNTNPPLPPLPPEITQLLSGLDAAQWAWLSGYAWAKAGNGASAGLPALQTALPAAEPFSVTVLSASQTGNAKSVADKAADSLEAAGIQVSRAELKDYKAKNIAGERRLLLVTSTQGEGEPPKEAVVLHKLLNGKKAPKLDKLQFAVLGLGDSSYPNFCQAGKDFDRRFEELGAKRLLERVDADLDFTASANAWTDNIAALLKEEAAKNRATPAPQTTPPAGLQTAPDGRYCKAAPFPAALLANQKITARQSDKDVRHIEIDLSGSDLHYLPGDALGVWFDNDPALVREILDLLGIDPATEIQAGGKMMPVARALSSHFELTQNTPAFVKGYAAFAHYEELDKIIADNAVLQDFVQNTPIVDVLHRFPASLTAEQFIRLLRPLAPRLYSISSAQAEVGDEVHLTVGVVRFEHEGRARTGGASGFLADRLEEDGTVRVFVERNDGFRLPEDSRKPIVMIGSGTGVAPFRAFVQQRAAENAEGKNWLIFGNPHFARDFLYQTEWQQFAKDGFLHRYDFAWSRDQEEKIYVQDKIREQAEGLWQWLQEGAHIYVCGDAAKMAKDVEAALLDVIIGAGHLDEEGAEEYLDMLREEKRYQRDVY | Cofactor: Binds 1 FAD per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.
Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite
Sequence Mass (Da): 66386
Sequence Length: 604
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1.
EC: 1.8.1.2
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A1KU06 | MSEHDMQNTNPPLPPLPPEITQLLSGLDAAQWAWLSGYAWAKAGNGASAGLPALQTALPAAEPFSVTVLSASQTGNAKSVADKASDSLEAAGIQVRRAELKDYKAKNIADERRLLLVTSTQGEGEPPEEAVVLHKLLNGKKAPKLDKLQFAVLGLGDSSYPNFCRAGKDFDRRFEELGAKRLLERVDADLDFAAAADGWTGRIVARLKEEAAKNRATPAPQTTPPAGLQTAPDGRYCKADPFPAALLANQKITARQSDKDVRHIEIDLSGSDLHYLPGDALGVWFDNDPALVREILDLLGIDPATEIQAGGKTLPVASALLSHFELTQNTPAFVKGYAPFADDDELDRIAADNAVLQGFVQSTPIADVLHRFPAKLTAEQFAGLLRPLAPRLYSISSSQAEVGDEVHLTVGAVRFEHEGRARAGGASGFLADRLEEDGTVRVFVERNDGFRLPEDSRKPIVMIGSGTGVAPFRAFVQQRAAENAEGKNWLIFGNPHFARDFLYQTEWQQFAKDGFLHRYDFAWSRDQEEKIYVQDKIREQAEGLWQWLQEGAHIYVCGDAAKMAKDVEAALLDVIIGAGHLDEEGAEEYLDMLREEKRYQRDVY | Cofactor: Binds 1 FAD per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.
Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite
Sequence Mass (Da): 66179
Sequence Length: 604
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1.
EC: 1.8.1.2
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Q8EAZ9 | MLLKELSSLASPLSQSQVDKLKQLTAELNSVQLAWVSGYLAATANTSGSAIQVAASVTEAQAAQTVTILYGSQTGNGRGIAKALAEKAKTQGYSVNLASMGEYNVRQLKQETLLLLVVSTHGEGEAPDDAIELHKFLATKRAPQLNNLHYSVLALGDSSYEFFCQTGKDFDARLSALGAKALLPLVECDVDYEAAAGQWHADVLTAVKPLIQTTANVVALNEINSTSAQVASESEFTKQNPYRAEVLVSQKITGRDSDRDVRHVEIDLGESGLHYEVGDALGVWFSNSEILVGEILAGLGLAADAKVTVGSESISLKQALIDKKELTQLYPGLVKAWAELSASSELLALSEDKEQLRQFILNHQFVDLVTNYKLPAEANLDANKLLELLRPLTPRLYSIASSQTEVDTEVHLTVALVEDEHQGQTRFGGASHFLASAQEGAEVKVYVEPNKHFRLPENPDTPVIMIGPGTGVAPFRAFMQERVAQGAKGDSWLFFGNPHFEQDFLYQTEWQQYLKNGDLTRIDVAFSRDQAHKIYVQHRIKEQGQALWQWLQNGAHLYICGDAERMAKDVHQALLAVAVEFGGLSSEAAEEYFETLRSHKRYQKDVY | Cofactor: Binds 1 FAD per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.
Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite
Sequence Mass (Da): 66620
Sequence Length: 607
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1.
EC: 1.8.1.2
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P25779 | MSGWARALLLAAVLVVMACLVPAATASLHAEETLTSQFAEFKQKHGRVYESAAEEAFRLSVFRENLFLARLHAAANPHATFGVTPFSDLTREEFRSRYHNGAAHFAAAQERARVPVKVEVVGAPAAVDWRARGAVTAVKDQGQCGSCWAFSAIGNVECQWFLAGHPLTNLSEQMLVSCDKTDSGCSGGLMNNAFEWIVQENNGAVYTEDSYPYASGEGISPPCTTSGHTVGATITGHVELPQDEAQIAAWLAVNGPVAVAVDASSWMTYTGGVMTSCVSEQLDHGVLLVGYNDSAAVPYWIIKNSWTTQWGEEGYIRIAKGSNQCLVKEEASSAVVGGPGPTPEPTTTTTTSAPGPSPSYFVQMSCTDAACIVGCENVTLPTGQCLLTTSGVSAIVTCGAETLTEEVFLTSTHCSGPSVRSSVPLNKCNRLLRGSVEFFCGSSSSGRLADVDRQRRHQPYHSRHRRL | Function: Hydrolyzes chromogenic peptides at the carboxyl Arg or Lys; requires at least one more amino acid, preferably Arg, Phe, Val or Leu, between the terminal Arg or Lys and the amino-blocking group.
Catalytic Activity: Broad endopeptidase specificity similar to that of cathepsin L.
Sequence Mass (Da): 49836
Sequence Length: 467
EC: 3.4.22.51
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Q8FAG5 | MLDQVCQLARNAGDAIMQVYDGTKPMDVVSKADNSPVTAADIAAHTVIMDGLRTLTPDIPVLSEEDPPGWEVRQHWQRYWLVDPLDGTKEFIKRNGEFTVNIALIDHGKPILGVVYAPVMNVMYSAAEGKAWKEECGVRKQIQVRDARPPLVVISRSHADAELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAAAAGAHVHDWQGKPLDYTPRESFLNPGFRVSIY | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27190
Sequence Length: 246
Subcellular Location: Cell inner membrane
EC: 3.1.3.7
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P22255 | MLDQVCQLARNAGDAIMQVYDGTKPMDVVSKADNSPVTAADIAAHTVIMDGLRTLTPDVPVLSEEDPPGWEVRQHWQRYWLVDPLDGTKEFIKRNGEFTVNIALIDHGKPILGVVYAPVMNVMYSAAEGKAWKEECGVRKQIQVRDARPPLVVISRSHADAELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAAAAGAHVHDWQGKPLDYTPRESFLNPGFRVSIY | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP. May also convert adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS). Has 10000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2).
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27176
Sequence Length: 246
Subcellular Location: Cell inner membrane
EC: 3.1.3.7
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P44332 | MLTLNEHLLNQVLLIAYQSGKHLQQFYQKQVHVELKEDNTPVTEADLFVSQFLTEKLTALFPNVPVLSEENCHISFEERKNWKEYWLIDPLDGTQQFINRTDQFSVLITLVRKNKPVLSVIHAPILSTTYYAMCDFGTFKKQLDQVKKLTKNTTNFDRPLRIAVGATTSQEKVRSILPKDFPCEFVVVGSSSLKSGLVAEGAVDCYVRLGQTGEWDTAGAEVLLGETHGAIFDSHFEPLTYNQRETLINPHFVMVGDQSFDWRSIFQFN | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30723
Sequence Length: 269
Subcellular Location: Cell inner membrane
EC: 3.1.3.7
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P46726 | MASHDKRDYQAELTDAALAADLATAAGELLLEIREEIGFDQPRALGDAGDRLANSLLLSRLRAERPGDAVLSEEAHDDRVRLQAGRVWIIDPLDGTREFSTAGRTDWAVHIALWQRTTGGVADGRREITDAAVALPARGNRVYRSDTVTAGAVTGGVPNILRIAVSATRPPTILHRIRQKLAIEPVAIGSAGAKAMAVVDGDVDAYLHVGGQWEWDSAAPAGVVLAAGMHASRLDGSPLRYNQLDPYLPDFVMCRADIAPILLGVIREVWQ | Function: Phosphatase with a broad specificity. Its primary physiological function is to dephosphorylate 3'-phosphoadenosine 5'-phosphate (PAP) and 3'-phosphoadenosine 5'-phosphosulfate (PAPS). Thus, plays a role in mycobacterial sulfur metabolism, since it can serve as a key regulator of the sulfate assimilation pathway by controlling the pools of PAP and PAPS in the cell. To a lesser extent, is also able to hydrolyze inositol 1-phosphate (I-1-P), fructose 1,6-bisphosphate (FBP) (to fructose 6-phosphate (F-6-P)) and AMP in vitro, but this might not be significant in vivo (By similarity).
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Sequence Mass (Da): 29119
Sequence Length: 271
Pathway: Sulfur metabolism; sulfate assimilation.
EC: 3.1.3.7
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Q85AI0 | MSQLIFIPLLISLLVTKGKIRFLNNFESVLALSLHYGILVLALPIFILLYKAKKQPCSILLKVTTEPIILSAYATTFSTAFLAITINALFGLIIAWILVKYEFTGKETLDAIVDLPFALPASVGGLTLMTVYSDRGWMGPICSGLGLKIVFSRLGVPMATIFVSLPFVVRTIQPVLQDVEEELEEAAWCIGASPWTTFCQISLPLLTPSLLTGTALGFSRAIGEYGSIVLIACNIPMKDLVISVLIFQKLEQYDYQGAIVVATIVLIASFGGLLIINKVQLWKQNLSK | Function: Part of the ABC transporter complex cysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31474
Sequence Length: 288
Subcellular Location: Plastid
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A2CI71 | MSTNEMNQKKRLNRSGSLSSHLTRSWPWQLTLSYLFFMLILPVIALLSRASDELFKDFWQIAAEPVAISTYVVTLMTALFATLINGFFGVIIAWVLVRYNFPGKRIIDAAIDLPFALPTSVAGLTLATVYSDQGWIGHLFESIGIKVAFTRVGVAVAMIFVSFPFVVRTLQPVLVEIDQELEEAAWSLGASTWRTFWRVIFPPLTPAIVTGVALAFSRAIGEYGSVVIVASNIPFKDLTAPVLIFQRLEQYDYTGATIIGTVILSISLFLLFGINFIQSLNQLYVK | Function: Part of the ABC transporter complex cysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31812
Sequence Length: 286
Subcellular Location: Plastid
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C0HL14 | GVFCGEACAQASCSIAGCECIAGLCYKN | Function: Probably participates in a plant defense mechanism.
PTM: This is a cyclic peptide.
Sequence Mass (Da): 2772
Sequence Length: 28
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
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Q7XI14 | MARRAAAGLLRRHLGPLAAGETLQARGMYPKQYGAANHAFSRFYSIQGQQRSLYGFRTNVETDDTQQSARMNFEVQKRSFSSAAAHVQRNPAYSVLNSDDVSYFKSILGDSGVVQDEDRVSVANMDWMGKYKGSSQLLLLPKSTAEVSKILSYCNSRRLAVVPQGGNTGLVGGSVPVYDEVIISLGGMDKIITFDNVNGILTCEAGCVLENLSSYVENKGFIMPLDLGAKGSCHIGGNISTNAGGLRFIRYGSLHGSVLGLEVVLADGTVLDMLTTLRKDNTGYDLKHLFIGSEGSLGIVTKIAILTPAKLPSTNVAFLSCNDYISCQKLLLAARRSLGEILSAFEFMDRHCINLAMKYLEGVHNPLPVSPFNFYVLIETTGSDESYDKAKLEAFLLRSMEDGLVADGVIAQDISQASNFWRIREGISEASVKVGAVYKYDLSIPVEKLYDIVEEMRSRVGDMGQVLGYGHLGDGNLHLNILSTKYSDKMLAQIEPFVYEWTSKQRGSISAEHGLGLMKAEKIHYSKSSEAVQLMASIKKLLDPNSILNPYKVLPQSVL | Cofactor: Binds 1 FAD per monomer.
Function: Catalyzes the oxidation of D-2-hydroxyglutarate to alpha-ketoglutarate.
Catalytic Activity: (R)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 61097
Sequence Length: 559
Subcellular Location: Mitochondrion
EC: 1.1.99.39
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Q88EH0 | MIAQLSTVAPSANYPEFLEALRNSGFRGQISADYATRTVLATDNSIYQRLPQAAVFPLDADDVARVATLMGEPRFQQVKLTPRGGGTGTNGQSLTDGIVVDLSRHMNNILEINVEERWVRVQAGTVKDQLNAALKPHGLFFAPELSTSNRATVGGMINTDASGQGSCTYGKTRDHVLELHSVLLGGERLHSLPIDDAALEQACAAPGRVGEVYRMAREIQETQAELIETTFPKLNRCLTGYDLAHLRDEQGRFNLNSVLCGAEGSLGYVVEAKLNVLPIPKYAVLVNVRYTSFMDALRDANALMAHKPLSIETVDSKVLMLAMKDIVWHSVAEYFPADPERPTLGINLVEFCGDEPAEVNAKVQAFIQHLQSDTSVERLGHTLAEGAEAVTRVYTMRKRSVGLLGNVEGEVRPQPFVEDTAVPPEQLADYIADFRALLDGYGLAYGMFGHVDAGVLHVRPALDMKDPVQAALVKPISDAVAALTKRYGGLLWGEHGKGLRSEYVPEYFGELYPALQRLKGAFDPHNQLNPGKICTPLGSAEGLTPVDGVTLRGDLDRTIDERVWQDFPSAVHCNGNGACYNYDPNDAMCPSWKATRERQHSPKGRASLMREWLRLQGEANIDVLAAARNKVSWLKGLPARLRNNRARNQGQEDFSHEVYDAMAGCLACKSCAGQCPIKVNVPDFRSRFLELYHGRYQRPLRDYLIGSLEFTIPYLAHAPGLYNAVMGSKWVSQLLADKVGMVDSPLISRFNFQATLTRCRVGMATVPALRELTPAQRERSIVLVQDAFTRYFETPLLSAFIDLAHRLGHRVFLAPYSANGKPLHVQGFLGAFAKAAIRNATQLKALADCGVPLVGLDPAMTLVYRQEYQKVPGLEGCPKVLLPQEWLMDVLPEQAPAAPGSFRLMAHCTEKTNVPASTRQWEQVFARLGLKLVTEATGCCGMSGTYGHEARNQETSRTIFEQSWATKLDKDGEPLATGYSCRSQVKRMTERKMRHPLEVVLQYAQR | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Catalyzes the oxidation of D-2-hydroxyglutarate (D-2-HGA) to 2-oxoglutarate (Probable). Is involved in a D-lysine catabolic pathway .
Catalytic Activity: (R)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 110945
Sequence Length: 1006
Pathway: Amino-acid degradation.
EC: 1.1.99.39
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P84850 | MVLHLVPRWSASLFRASPRWKKTYSQRASAQLKWLGCPRSVYSPLACRAYSKVSGSPEVMLTPERYPVQRLPFSTVSEEDLAAFECIIPGRVITDPEQLQTCNVDWLRTVRGCSKVLLRPQTSEEVSQILRHCYKRNLAVNPQGGNTGMVGGSVPVFDEVILSTALMNQVISFHDVSGILVCQAGCVLEELSRYVQERDFIMPLDLGAKGSCHIGGNVATNAGGLRFLRYGSLRGTVLGLEVVLADGTILNCLTSLRKDNTGYDLKQMFIGSEGTLGVITAVSIVCPPRPKAVNVAFLGCPGFTEVLQTFRTCKGQLGEILSAFEFMDAECMQLVGQHLHLTNPVQESPFYVLVETSGSSAGHDAEKLTNVLEQVLNSGLVIDGTMATDQRKVQMLWALRERITEALSRDGYVFKYDLSLPVERLYDLVIDLRTRLGPRAKHVVGYGHLGDGNLHLNVTAEAFSQELLGALEPYVYAWTAEQRGSVSAEHGLGFKKKNVLGYSKPPVAVKLMQQLKAMLDPKGILNPYKTLPARA | Function: Catalyzes the oxidation of D-2-hydroxyglutarate (D-2-HG) to alpha-ketoglutarate . Also catalyzes the oxidation of other D-2-hydroxyacids, such as D-malate (D-MAL) and D-lactate (D-LAC) . Exhibits high activities towards D-2-HG and D-MAL but a very weak activity towards D-LAC (By similarity).
Catalytic Activity: (R)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 58805
Sequence Length: 535
Subcellular Location: Mitochondrion
EC: 1.1.99.39
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A4VGK4 | MTDPALIDELKTLVEPGKVLTDADSLNAYGKDWTKHFAPAPSAIVFPKSIEQVQAIVRWANAHKVALVPSGGRTGLSAAAVAANGEVVVSFDYMNQILEFNEMDRTAVCQPGVVTAQLQQFAEDKGLYYPVDFASAGSSQIGGNIGTNAGGIKVIRYGMTRNWVAGMKVVTGKGDLLELNKDLIKNATGYDLRQLFIGAEGTLGFVVEATMRLERQPTNLTALVLGTPDFDSIMPVLHAFQDKLDLTAFEFFSDKALAKVLGRGDVPAPFETDCPFYALLEFEATTEERAEQALATFEHCVEQGWVLDGVMSQSEQQLQNLWKLREYISETISHWTPYKNDISVTVGKVPAFLKEIDAIVGEHYPDFEIVWFGHIGDGNLHLNILKPDAMDKDEFFGKCATVNKWVFETVQKYNGSISAEHGVGMTKRDYLEYSRSPAEIEYMKAVKAVFDPNGIMNPGKIFAA | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the dehydrogenation of (R)-2-hydroxyglutarate (D-2-hydroxyglutarate or D-2-HG) to 2-oxoglutarate and of (R)-malate (D-malate) to oxaloacetate. Is functionally tied to L-serine biosynthesis, via its coupling with the D-3-phosphoglycerate dehydrogenase SerA, encoded by the adjacent gene in the locus. Is required for the utilization of D-2-hydroxyglutarate as well as D-malate as the sole carbon source for growth of P.stutzeri. Active in vitro with artificial electron acceptors such as 2,6-dichlorophenolindophenol (DCPIP) and appears to couple with electron transfer flavoprotein (ETF) for efficient oxidation of both D-2-hydroxyglutarate and D-malate in vivo. Cannot catalyze the oxidation of L-2-hydroxyglutarate, D-lactate, D-tartrate, D-2-hydroxybutanoate, D-mandelate, D-glycerate and D-phenyllactate.
Catalytic Activity: (R)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 51086
Sequence Length: 464
EC: 1.1.99.39
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P0DV35 | MTDPRILSLQQAVPALRLKTEPADLEHYGRDWTRRWTPNPLAIALPGSVEEVQAVVRWANAQAVAVVPSGGRTGLSGGAVAANGELVLSLERLNKPLDFNAVDRTLTVQAGMPLEAVHNAAREQGLVYPVDFAARGSCSIGGNIATNAGGIRVIRYGNTREWVAGLKVVTGSGELLELNNALVKNSSGYDFRHLMIGSEGTLGIVVEATLRLTDPPPPSNVMLLALPSFDVLMQVFAAFRAQLRLEAFEFFTDRALEHVLAHGAQAPFAEIHPYYVVTEFAAGDEAQEAAAMAAFETCMEQGWVSDGVISQSDAQAAQLWRLREGITEALARYTPYKNDVSVRISAMPAFLAETQALLHDAYPDFDVVWFGHIGDGNLHINVLKPDATSQADFVAACDQVTKLLAQALQRFDGSISAEHGIGLVKKSYLWSTRSAEEIALMRGIKHVLDPHLLLNPGKLFETHDAPTNIPAG | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the dehydrogenation of (R)-2-hydroxyglutarate (D-2-hydroxyglutarate) to 2-oxoglutarate. Has also a low activity on D-malate in vitro . Is functionally tied to L-serine biosynthesis, via its coupling with the D-3-phosphoglycerate dehydrogenase SerA, encoded by the adjacent gene in the locus (By similarity). Active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCPIP), but not with NAD, NADP, or cytochrome c. Also displays a very low oxidase activity in vitro on D-2-hydroxyglutarate and L-2-hydroxyglutarate with O2 as the electron acceptor, but this activity is most likely not physiological .
Catalytic Activity: (R)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 51032
Sequence Length: 472
EC: 1.1.99.39
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Q8MPP3 | MFSKYVLATLLALFAQSMCIQELSLPPEGSHSTAATRSKKAKTAISEDIMYNYLMQFDYLPKSDLETGALRTEDQLKEAIRSLQSFGNITVTGEIDSATARLIQKPRCGVGDRRSADSFSPDNLYHEIGSNVRVRRFALQGPKWSRTDLTWSMVNRSMPDASKVERMVQTALDVWANHSKLTFREVYSDQADIQILFARRAHGDGYKFDGPGQVLAHAFYPGEGRGGDAHFDADETWNFDGESDDSHGTNFLNVALHELGHSLGLAHSAIPDAVMFPWYQNNEVAGNLPDDDRYGIQQLYGTKEKTWGPYKPQTTTTTTTTTTMRAMIYRADKPAYWPWNNPSNNPNNDRNRARERQEEERRRQEKERRRQEEERRHQEEERRRQVEERQRQEEERWRQEQERQEEENRRRKIEHKSQWERNPSKERNRPRERQEMERRRQEQERQEQERQEQEDRRRERERDRQLEWERRNRNGAREPVTPTANTTPRPTNKPYPTVHRQHHHHNKPRKPKPDSCMTYYDAISIIRGELFIFRGPYLWRIGTSGLYNGYPTEIRRHWSALPENLTKVDAVYENKQRQIVFFIGREYYVFNSVMLAPGFPKPLASLGLPPTLTHIDASFVWGHNNRTYMTSGTLYWRIDDYTGQVELDYPRDMSIWSGVGYNIDAAFQYLDGKTYFFKNLGYWEFNDDRMKVAHARAKLSARRWMQCARSANEVDDEQRWTASLVSEGEETGRSGSRELRINHFILSILLLAIANWRS | Function: Has metalloproteinase activity . Required for larval tissue histolysis during metamorphosis and is involved in pupal head eversion and fusion of the wing imaginal tissue . Required for growth of the dorsal air sac primordium and development of the dorsal air sacs . Promotes embryonic motor axon fasciculation . Cleaves and activates frac to promote motor axon bundling during outgrowth . Promotes the reshaping of adult sensory neuron dendrites from a radial to lattice-like shape which occurs after eclosion by degrading the basement membrane on which the dendrites grow . Involved in inhibition of follicle stem cell proliferation by cleaving Dlp, inhibiting its interaction with wg and preventing Dlp-mediated spreading of wg to follicle stem cells to enhance their proliferation . Plays a role in wound healing . Involved in fat body dissociation which occurs during metamorphosis by degrading basement membrane components, leading to destruction of cell-basement membrane junctions . Required for posterior follicle cell degradation and ovulation .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 89137
Sequence Length: 758
Subcellular Location: Cell membrane
EC: 3.4.24.-
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O34688 | MGITSVLTKDNVKKIDTDIDVQERDLNVFITSASRVIAPLWPISTFAARNPWMGLENQPFDQVASWLKNTRDVDIYPSASMIRSAKNKGEIDEDFVEMGLQRWLDSHSYHIPRDVAERFCHAALKLDPLPSDLLSSHELEKLVSECSGLDHIENVFMQPLSSYIENQDGERLVNILDHHVIKWSKLYLDDSQAGWTMPNREEGFYRAWQHLIQYDPALSKKQRERVKGWPKEAHLALQEALFALEIPESEIQTYLEGHLLSLPGWAGMMLWRSQQSSHEHALLTEYLAVRISMEWALIKPYLPLTNERSKKTISIAPLIAAWIHWGGLTLEEWSQMTASEQNEYLSFAYSFDEKLRKKLWLEAWEQTYTDRLSQKIISKQRETGREKSALAQLAFCIDVRSEPFRRQLEKEGPFETIGIAGFFGVPIATCELGSKHSHASLPIIQKPQNKIKEFADEDVFKKYNQRKQAIHSLSHTFKTMKQNALSSLLLPELSGPWLTLQMAARSFVPRKAGRFIRNLREAWLRKPDTKLSLHHDATEAEIPVGFTDEEKVNYARQALKMMGLTENIAPLVVICGHGSQSTNNPYSAALDCGACGGAAGGFNARVLAALCNLSEVREALLAEGIKIPEDTVFAAAEHNTTVDELHWLYVPELSEAAQEAFEQIEAVMPKVRHHVNAERLAQLPNFQSKLKNPKAEANRFAEDWSEIRPEWGLARNAAFIIGKRELTQDCDLEGRAFLHNYDWKQDESGELLANIIVGPGTVAQWINLQYYASTVAPHYYGSGNKATQTVTAGLGVMQGNASDLLAGLPWQSVMESDHEAYHSPLRLLILIQAPREYVERLLNHDSAFLQKVQNGWVRLASLDPEGCWESW | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 98767
Sequence Length: 871
Subcellular Location: Cell membrane
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A9WCK3 | MTMIETQLRSLLVTTKPIRDLTIDAVIAATKRAEQRIAPLWPLRYFVAVNPYLGLIDHTFADAAQLLARRTDARMTAPRDFYAQAIKSGRITDADLAAAIADEKLPSPAPASVAALKEFAFSKDPDPATTPLPTIADVATTVTGINWADFVTDAISTWAGAYFDLGQSYWRSPWAQLPAYAAWRAEAAHDRTAQARGVHGMRRALRELPETALETIVTAVKMLNIPEQGLEAYLHRLLLTIHGWASYARYLRWDAELYGGEDHTLTDLLAIRLVWEVALWHSFADRGVAEAWHKCKPELSNEQLTETARYALAGNILLQRAFEKSYQRQLFARLGTARPATTPQRKRVQAAFCIDVRSEIFRRALETTTDDIETIGFAGFFGFPIEYVPLAEVHGGAQCPVLLTPQFVIAEAVDGASTDEVAKIIERRALRQRVAKAWRMFKFAPISCFGFVGPVGLAYLRKLVLDTLGITRPVPHPAQFGLDARTREHVAPILEPGLIGDRPTGMTLEQRVAAAAGALKAMSLTDNFARIVLLAGHGSTTVNNPHATGLDCGACGGHTGEANVRVAVRILNDPAVRTKLKEQGIVIPDDTVFVAALHDTTTDDITIFDKHMIPASHADDLKRLEADLAAAGRLARAERAALLKIDRKADIDRQVRQRSKDWSQVRPEWGLAGCAAFIAAPRDRTAGIKLDGRSFLHSYTWQQDSDFSVLELIMTAPMIVASWINLQYYGSTVDNRLFGSGNKTLHNVVGTLGVLEGNAGDLRVGLPWQSVHDGENYVHEPMRLHVLIEAPIPAMTAIIAKHEQVRQLLDNGWLYLFALDDRGVVTHKYAGNLQWEPV | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 92482
Sequence Length: 838
Subcellular Location: Cell membrane
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Q7NT42 | MAAIAPAWPLDSLVASSPYWGLREQSFSQAADTLRLVADSPLHLPRGEYLAAWRRGEISAAALETALSETGWTGGAQAWLDAEPRDVDPVPPPRLLAACHREAAGPLSAQSWTDVVIQQISQYCAAWFDRDQANWHLDHERGFYAAWLEQMRHPYGLSALPERREQLRLRAERLPGDAEAMLAAGLAQLQAEPEWLKPWLQALLMRNNGWAAWCAYLGWQAGLKGETDGHLRQLLAIQMAWECLLDDGARGPDSAWAAWHRDWGLRLHGRADPRTLIWQRAHELSLHAPLAQALCRESAAEDGTRPAMQAVFCIDVRSEPLRRALEQTVPASRTYGFAGFFGLPLAYRVPGSDVAQPRLPVLLAPGWEASAAPASKPSAARRGWRAFQRSPLSGFALVESAGLAKLAALAGRSKARGRQAALPQLDPWLTPDSAKPVPRDGLGLERRAEIVSGLLPAMGLAGALAPWVLLVGHASHVSNNPQAAALQCGACGGHGGHQHVRLLAGWLNDPALRERLAALGRAIPADTVFLPALHLTHSDEILLLDADTLSADARARLPGLQAQLRAASALARRRRAPLVGLAPEADDAILLNKMRQKGDDWAETRPEWGLAGNALFIAAPRAKTRKLDLGGRAFLHEYDWRADPDGKGLQAILAAPMVVAHWINMQYFASTADPRRFGSGNKLLHNVVGGRIGVFEGNSGDLRIGLAWQSVHDGQRLRHAPLRLAACIDAPPDRLAEALAAQPVPRQLAENGWLHLYCVHGDTPLRWHADGGWRHD | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 84575
Sequence Length: 776
Subcellular Location: Cell inner membrane
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Q47IK9 | MSAAHELPIRERLAHWVEHLTHVLPAQAPIRDFVHHNTLHGFQHLPFTEALASAQALTGATTYWPESRFRECLASGRISPDDLSAALDDFGVGDLDQPVVRNLTRRDILLASLRFGCEAPNACRQAWLLDETSLADDPLFAYFCRSVELAPSKGASENWQVQALARWDALCGRVGRTWTWRALLEYLSGEDVLEWTRSILQRHLAAHLDLGVAAWRNPAQGQGFFAAWRASAGLDMAWEMDELPNARDEILHLPDSPLDVLLEELPRLVPDHSQWYGYLERLSLELPGWSGMFLWRDRNPGRGDGTPIAMLDYLTVRVLLERLLTDDLLRRLAGSPLSLAELHAYYAARPEEFLVRAALHEPGLPEDLLGRAAHLVQLAREGHVDVAEWRRLAAALAPAMAAAQDDGAAWQMAGLSRQLGLTPADLEMLSGDDLTALQTCAASLSSLQRGHIWLLAYERHYREQLFSALTANHPRQATPAAPSAQVVMCMDDREEGTRRHLEEIAPDVATYGAAGFFGVPMFWQGLDDAGKTALCPVVVQPTHLLRELPAAGEEGSLAGHAARREKRLRWNERLYQATRRRAVAGPVLTALGAVPALASLLAVTLVPGWFGETARRWREQYEGRVSTRLGLTAEQPVAATPEQPQLGLTDAEQIERVEAFLRMIGLTAGFAPLVLMFGHGSGSQNNPHLSAYDCGACSGKHGGPNARVFAAMANRPAVRAGLAARGLSIPDSTWFVAAEHNTCDDGIEWYDLDSTPERFQAAVDRLLGQMAEACRAHAAERCRRLASAPFKPSPWKARQHMIGRANDISQARPELGHATNAAAFIGRRQMSRGLFLDRRVFLISYDPVGDDDGCIVEGILLAAGPVGAGIALEYYFSTVDNERFGCGSKITHNITGLFGVMEGADSDLRTGLPWQMVEIHEPMRLLVVVEQTPEVLTAIVGRQPPLQELINNEWIIVAAKHPITGAIDLYCPRRGWLPWSGQAVLPQVARSVDWFAGESQPLAPAIILGGVR | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 111281
Sequence Length: 1012
Subcellular Location: Cell inner membrane
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Q5L2V2 | MSRSVISLERSTEAKKAAACPLEVIVSEAAKVIAPLWPISAFIARHPWMGMEDKSFVDAADRLQEAYGIDLYPPMAVFHAALSKGEIDVSFIERRLQRWLDDEPLPAPRHEAERLCRALLWNDAVPEEALQMPKLIELAAAMPLRSVSIRTRSVRLGLEKRLDQQMIKWCKLFYDRGEAVWALPHREHGFYGSWRRLAPLDPSLSKEERKRLFDWPHHPEEALQRALEQLGVQDEEAVAYLEAHLLALPGWAGMMVWQSRRAGDEIGGLINYLAVRLSLEWVFTAPHLPLKEEENEDDRAVGPLLAAWIHWGGMTLDDWRRLPLEDRQARLVFADRFWRIGRRHLWLEAWEDTYEAKLKEAVLTRQPEEPKEQAAAQLLFCIDVRSEPFRRHVEAVGPFETYGCAGFFGLPIQTRVLDSDDAHPSCPAIVAPRHEINETASPETAAPYRRRRDLFRFVGRTFKKIKRHLLAGLLLPEMSGPWLGLHTIARSAAPAWAGQAIHQAEMSAQQKPKTTLSLDCQGHDETTGLPIGLTKEEQVQYVKQLLVNIGLTSSFAPLVVVCGHESETTNNPYASALDCGACGGAAGAFNARVFAALANLPHVRDGLAKEGIVIPDETVFVAAEHITTVDELRWVEVPPLSEAAEAAFRQLKQALAGVSRQANAERMAKLPHVGAMPRDPVAEARRRAVDWSEIRPEWGLAGNAAFLIGRRALTKGVHLDGRVFLHSYDWREDPTGEALAGIIAGPATVGQWINLQYYASTVAPNYYGSGDKTTQTVTGGIGVMQGNGSDLLAGLPWQSVAASDREWFHSPLRLLVIIEAPFSYIERLLDENSEFRRKVQNGWLRLASIDPDSGAWVNWEAGRLASVQQR | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 97317
Sequence Length: 870
Subcellular Location: Cell membrane
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Q18H12 | MTTESTSESKTKTETETETETEQRNDLSNSSNSSEDASCPGSSPVSTESDPDNDDTSVSANTIVRQYIESAAESVGALWPIHSFVTANPLSGFEDQPFHKAVAAGATRFGGDGYPDSDVFEHAWKTGQINQEILKKTLDEYETDHTPASAIAAIDSGTQATSGRDTGVRMGTGVDDEINNWDEIDKRVIKWLSAFLDAGSAEWEMPNRGSGFYTAFQSVATYDTMIPDTDLIEDPPADPIDAVSTVLASYPRSQWSEIIEAQITALPGWTGLICYRTENETAWQTAYPITLVGYLAARMMLADALSIPLDSISRPAHSVTSTEESTADIETYPLQEIILIAWERTYREELIEQIADTADNHKHEHDHDHDADKTIGDDVEPQADSRSSSVRPDAQLVFCIDTRSEIIRRHIESTGQYETYGYAGFFGIPMRYRGYDDAVSIDACPPIVDAQHRISESAKHADENKTPNGQYNSRYERIRDIYDAGIDIVDSLASNVTTAFNFVETTGSGYGVGLALRTLFPQRVYDILTRIENRLPRIDVISQPQLNTATGEVNQYSHNETDGSHSEDVLPYGLTHQERVEYAASAFELMGLKTFGRVVGFIGHASQTANNPFGSSLDCGACAGNAGGPSARVLAQICNDDAVKTSLRDRGIDIPVDTVFIAGEHTTTTDKITLYTEAIPDSHQDDIRSLQADLSIAQEDAAAERLESLSGDTTVDAIQDIERRAADWAETRPEWGLAGNAGFVIGPRRLTDDVDLEGRVFLHSYDWQQDETGSALESILTGPLIVTQWINAQYYFATVDTAVYGSGSKVTQNPVGNVGIYQGNGGDLMRGLPVQSVRKSTDNLYHQPIRLSTVVHAPVSKVTHALADLESVTELLDNNWISLTVIDPTRENDAFHYVKGLKWLPHGEGYKHDATECISPQINQTVSSSSD | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 102008
Sequence Length: 931
Subcellular Location: Cell membrane
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Q31HC3 | MMLHNAKASDNNELDQAKPLIPQLSDKQKEALNDACGRIAPTWPLDELIAVNPWWEMRDQHISKVSAKLSALSQAQCVMPKSYFQEVWMETLQPQHVQQAIDEMEKDYTVDNLERYLLEEDEHTHWHNVSDFVDSGRDRKYKMAWRDEITHQISQFCADFFRLKDSQGTFSKTYQGLYHEWLATTRQDKGIEILMGEDGLTEHFMDLPESSESLLAEALVGLRVPDSQIADYAHALLLDANGWASWVAYLRWQDRLSNAENDLMMDFLAIRVAWEWVLWQHQKDSDRSVFNELKVMWHHQMSILPDLIATHEAAQAKSWIWQRAAEIAYQSELQQQLKHASRTDQKVETESPPVLLQAAFCIDVRSEVIRRALEAQDSRVETLGFAGFFGLPIEYQPAGTDVSRPQLPGLLKSGIKVTPVMTKVSKGATKQALNRKARWIEWGNAPPATFSMVEATGLMYAFKLLRNSLFPESHTNPINAIPATDAFELTQNDSPLTLDQKVELAAGILHAMGLDHDLAETVMLVGHGSTSCNNPHAAGLDCGACGGQTGEINVRVLAFLLNDESVRQGLLEKDIKIPAQTRFVAAMHNTTTDEFTCFGLNHVDETIQKWLARATEFARQERSTRLGLNHLEGQNLHQSIQRRAKDWSQVRPEWGLSNNAAFIVAPRARTRGVDFQGRAFLHDYDWQQDADNSLLTLIMTAPMVVTNWINLQYYASVCDNHVYGSGNKVLHNVVDGCIGVFEGNGGDLRIGLPMQSLHNGEKWMHEPLRLSVYIDAPQKTIAQVVAENDVVRHLIDNEWLYCFSWAPDGRIHRYFNNQWLESA | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 93448
Sequence Length: 823
Subcellular Location: Cell inner membrane
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B4U7X3 | MVKAYLDNVRKYIPHYWPMTTFVHHNPLHGFEDMPFKEALKQASKLYKAKVYMDPDYYVELYKEGIIKRDILEKNLFEFLKSIGLQMYFAESKKFITEISQDWKYYKVKSSTTPDINLIDYFNQKIVKDEDTLFQELIEDMMLSEILDAILEDNTTDIIEKEILEFVARFLDEGQTTMSMPEREKGMFGAFKLYEGLNTSLNEEEYADTILHELSPKNVERYILNHLLKDFGWAAFIKYREDNEDYYFQQIHPASLLEYLAVRLHYEKKYLNHYPISNFVELQKAFEQNKTLFVLKLLKAKNILPSKYIDRLEEKDSPKAILSDYLSEEVFLEAYRIQNIANELLLHLDKQKDITDFAFLIEKLKEEEGYIWLKSLEDSYIKEYTIDFLQSNEKIQRDILASAVFCIDVRSEAIRRHIERLGNYNTYGVAGFFGTPIAFIEFDKGHEQYLCPALIKPQKIIFELPEDEHHDYKTKHNINYTFKKTLESLKNNPYTPFFMVEAMGWLFGVNLFGKTLFPDFTLKILSFIKAKKPKTRFTIDKLSQEEIEFYAQKFFIQKIQEAYHQEFKKHINDKKAKDLFEAIINENHKGIDERILEILKTKYNINKESFELEKIRLSNVGYTEEEQIKLVENFLKLIGLTENIPKFVLLIAHGSTSDNNPFESALDCGACGGNNGLPNVRILASIANRNQIRKGLEKVGIKIPEDTIFIPGIHNTTTDEITFYDTEVMPQKDRALFDKIVKDFKIASQKTREERAKTLPYAGSGDRIPVRAIDWSETRPEWGLSKNMGVYVGKRSSTQNIALKNRFFMQSYTWEIDKDNKILKNILSGPFIIGEWINMEHYFSTTDNERLGAGSKVYHNVVAKVGVWTGNYGDLRTGLPYQTVYHDGVPYHEPIRLLTFIEAPAEKVLEAAQEVKEALKLVVNEWVRLIIIDKLKGVAYTFKDGNLEVLVDSRGINQFVI | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 112277
Sequence Length: 961
Subcellular Location: Cell inner membrane
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Q5R077 | MSTANRLATIAGQVSKAIAPQWPLSQWIAVNPFWHYRQQPVAGVAAHWRYSAGTRLLMSPDFYWQQWQQNRIDAALVTNKMVNELEQRSLLKAQLPQWRNLSRLVDKYTRRRRKMRWNDEVVLQISQTCGLFMQFPTRFQQAGKDSSLYQHWLTISRADRGIETLMDEAELTELFAQLPDDPHKLIQVCHDNFLSDASDYALRCYSQALISDLWGWAAAFSYQDARQDSQWVFELLCIRLAWEYILWQLAERTNTKVYQQLQQALSAQVENCEGQVAHIEQHNSLLWQWQAAYERSQLNRLQFKSDTVEESNAPDVQAVFCIDVRSERYRRALEQAGKSLGSYVQSKGFAGFFGVPLAIQRKGRDVPHVPGLLQPAYYIKAPARKQSVGSLLSNMFNAPVSMFSGVEALGLSKLKSLLTGVPGQLATANNAYIADGSICEHNGEASMESLVGICQQALAGMQFTRFARHIVLVGHGSHHSNNAQRAGLNCGACGGQTGALSARVLVRLLNNQNIREHLREQGVAIPDATQFHSAMHETVTDKVIWLSNTVPDSVKQVFRAATEKLTQACGESEKDRKTRSGHWAELRPEWGLADNNVLFFGQADRLTSADTIGSNFLHDYNSINDPDGELLAQLMSAPGLVANWINWQYYCSVTEPKQLGSGNKLLHNRVANDIGVFEGNGGDLRQGLAWQSVHNGSDFVHRPMRLQVIVEADEATIQRALAKAVAFNELFEQQWINLHRLNARGELCPVTTPVTAK | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 85144
Sequence Length: 757
Subcellular Location: Cell inner membrane
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Q28SY7 | MTTVHDLSSDTMTTAADRAARAIPPVWPLASSVAVNPFLGQTEEHLAQVSARLGRIGNVPVTMPPAHYAALIEDGTITDDDIASASAASRIDNAPDLAEIKRSAAVPFDRPEPHSTIADLAARMSGIDWPGILADRFGHWASGFFDQGQALWAAPRRRGAYDAWRQTATHDLTPEITGLTGFAQFVSETPDTAQEARLRAAKRLGLDDDMLETYLHQLLFSLGGWAQVARYHLWQAELSQTTDETIADLLTIRLLWEEALFLQYEDRIGDRWEATKTAHAQPVTPQRGEIINAILQEAWEHAVQRDLASTIAAPSPERGEDRPTLQAAFCIDVRSEVFRRALEAVNPGIQTLGFAGFFGLTASHKSFASDVDELRLPVLLNAGVTSTSTGENVTAEQTARFKARAKRAWGRFKLAAVSSFAFVEATGPIYAGKLVRDALNIGSDPHDYGPAPVLDPPLPLDAQIDAAETILRAMSLTTDFAPLVVLAGHGANVVNNPFASGLHCGACGGYAGDVNARLLAALLNTPDVRAGLADRGIDVPSDTLFLGALHDTTTDAITLFAKDHPSAAHDAGIAQAETWFAQAGTVTRAERALRLPRADGDADVDLRSRDWAETRPEWALAGCKAFIAAPRHRTAGKSLAGRAFLHDYDWKKDSDFSVLELIMTAPVVVASWISLQYYGSTVAPDVFGSGNKLLHNVTGGIGVVEGNGGTLRAGLPWQSVHEGEGYAHDPLRLSVCIEAPREAMTDILRRHDGVRALFDNRWLHLFALDASGQMAWRYTGDLEWSEMARDARISDDLDAAG | Function: Part of an energy-coupled inorganic carbon pump.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 86623
Sequence Length: 801
Subcellular Location: Cell inner membrane
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Q9HTQ0 | MRVLVLGSGVIGTASAYYLARAGFEVVVVDRQDGPALETSFANAGQVSPGYASPWAAPGIPLKAMKWLLEKHAPLAIKLTSDPSQYAWMLQMLRNCTAERYAVNKERMVRLSEYSRDCLDELRAETGIAYEGRTLGTTQLFRTQAQLDAAGKDIAVLERSGVPYEVLDRDGIARVEPALAKVADKLVGALRLPNDQTGDCQLFTTRLAEMAKGLGVEFRFGQNIERLDFAGDRINGVLVNGELLTADHYVLALGSYSPQLLKPLGIKAPVYPLKGYSLTVPITNPEMAPTSTILDETYKVAITRFDQRIRVGGMAEIAGFDLSLNPRRRETLEMITTDLYPEGGDISQATFWTGLRPATPDGTPIVGATRYRNLFLNTGHGTLGWTMACGSGRYLADLMAKKRPQISTEGLDISRYSNSPENAKNAHPAPAH | Function: Catalyzes the oxidative deamination of D-amino acids. Has very broad substrate specificity; all the D-amino acids tested can be used as the substrate except D-Glu and D-Gln. Participates in the utilization of several D-amino acids as the sole source of nitrogen, i.e. D-alanine, D-histidine, D-phenylalanine, D-serine, D-threonine, and D-valine.
Catalytic Activity: A + a D-alpha-amino acid + H2O = a 2-oxocarboxylate + AH2 + NH4(+)
Sequence Mass (Da): 47140
Sequence Length: 432
Pathway: Amino-acid degradation; D-alanine degradation; NH(3) and pyruvate from D-alanine: step 1/1.
EC: 1.4.99.-
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Q8TRA4 | MADIIIKNAYVLTMDPDAGDLKNGTVVIEDGKITEIGENTKENADTVIDAKGSVVMPGLANTHTHAAMTLFRGYADDLQLAEWLEKHIWPAEAQLKAEDVYKGSLLACLEMIKSGTTSFADMYFYMDETAKAVEASGLRASLSHGLIELWNEEKGEADLKEGKRFVRAWQGAADGRIKTMYGPHAPNTCSEEFLTKVKEEAHRDGAGLHIHVLETEAELNAMKERYGKCSVHLLEDIGFFGPDVLAAHCVWLSDGDIEILRQREVNVSHNPISNMKLASGIAPVYKMLEKGVNVTLGTDGCASNNNLDLFEEIKTAALLHKVSTGNPTALPARQVLEMATVNGAKALGTETGMLKVGKKADMIVVDMKKPHLTPCFDVPSHLVYSAKGCDVRTTIVDGKVLMDNYRVLVMDEEKVIEEARTAAEELVARANA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.
Catalytic Activity: 5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)
Sequence Mass (Da): 47157
Sequence Length: 432
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.
EC: 3.5.4.41
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Q2FRU6 | MADPKDISPCKNEDLFLKCRSTLITGVLLPDKTRSDIWYDETGTIRTCGPDIARNHRNEADIILDGSGFLAMPGLINTHTHAAMTLLRGYADDMHLQQWLSEKIWPLEAHLTGEHVYWGTKLACLEMIRSGTIAFNDMYFYMKDAARAVQESGIRAVLSHGIITFGDEAKMEAELKATEDLVHHVRSLNTSLITSAIAPHAPYTVPPQHLEVCADYSQKEKIIIHTHLAETKQEVDDCQKSYGMTPAALLDKTGCLTERTVAAHGCWLSEDDCRLLAERRVSVAHNPVSNMKLATGRAMPYHWLKDQGVNVCLGTDGCSSNNNLDMLEEMKTAALCQKFFWNSDTLLPAAEALSMGTSWGAKALGYQGGVIQEGMPADIVLISLSHPSMVPLHNPVSNIAYSAEGSVVDTVICQGKILMYNRYIPDEEKIIAGARESADDLLNRAGIMA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.
Catalytic Activity: 5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)
Sequence Mass (Da): 49429
Sequence Length: 449
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.
EC: 3.5.4.41
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Q58936 | MILIKNVFVNGKRQDILIEGNKIKKIGEVKKEEIENAEIIDGKNKIAIPGLINTHTHIPMTLFRGVADDLPLMEWLNNYIWPMEAKLNEEIVYWGTLLGCIEMIRSGTTTFNDMYFFLEGIAKAVDESGMRAVLAYGMIDLFDEERRERELKNAEKYINYINSLNNSRIMPALGPHAPYTCSKELLMEVNNLAKKYNVPIHIHLNETLDEIKMVKEKTGMEPFIYLNSFGFFDDVRAIAAHCVHLTDEEIKIMKQKNINVSHNPISNLKLASGVAPIPKLLAEGINVTLGTDGCGSNNNLNLFEEIKVSAILHKGVNLNPTVVKAEEAFNFATKNGAKALNIKAGEIREGYLADIVLINLDKPYLYPKENIMSHLVYAFNGFVDDVIIDGNIVMRDGEILTVDEEKVYEKAEEMYEILRS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated . Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions . May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens .
Catalytic Activity: 5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)
Sequence Mass (Da): 47468
Sequence Length: 420
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.
EC: 3.5.4.41
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Q8TYD4 | MRLAILGGIAVTPERVIEDAGILIDEDGRISFVDTREQLEECEDWEDEIELGEKDVIMPGLINTHTHGPMTLFRGVADDMPLMKWLREEIWPLEERLDAEKCRWGAALAAMEALKSGTTCLADMYFFMDAVAEAYAEVGIRAVISHGMIDLGEEDKREEELKESKRVYRKCQGMEGLIEFSLGPHAPYTCSEELLKEVRRLADEWGVKIQIHVAETEDEVKEVKRKHGKRPVEYLDEIGLLGDDVIAAHCVWLDDKEIEILSKRGVIVSHNPISNMKLASGISPVPEMLERGVNVTIGTDGCASNNNLDMLEEIKVAALLHKVNKMDPSATEMLEILRMATVRAGTVFSSEKIGAIEEGYAADLVVLDGSSPRLNPNHNPISNIVYSASGSDVKHVFVAGELVVKNGKLVKADEQEILENSTECAEQLTSS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.
Catalytic Activity: 5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)
Sequence Mass (Da): 47752
Sequence Length: 431
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.
EC: 3.5.4.41
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Q18T09 | MAQINENYLKLPGSYLFSEIARRVNEFKVQNPDADIIRLGIGDVTRPLAPVVVEAMKQAVEEMGRAETFRGYGPEQGYDFLIEKIIANDYAPRGVQLGMDEVFVSDGAKSDTANFQEIFGVDNIMAVTDPVYPVYVDSNVMAGRTGNYDTEKGQYGRIIYLPCTEEGDMKPELPTAPVDMIYLCFPNNPTGMTLTKEELKVWVDYARENKAIILFDSAYEAFIREEGVPRSIYEVEGAREVAVEFRSFSKTAGFTGTRCAYTVVPKDIMIYDSTGEGHSLNKLWLRRQTTKFNGVSYPVQAGAAAVYTEEGKKQIQATIDYYMENARIIREGLQEAGFKVFGGVNAPYIWMKTPGTMGSWEFFDKLMTEAHVVGTPGAGFGANGEGFFRLTAFGTRENTEKAIERIKARMK | Function: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate. Is also able to catalyze the reverse reaction in vitro, i.e. the transamination of LL-diaminopimelate with 2-oxoglutarate to produce tetrahydrodipicolinate and glutamate. Can also use m-DAP instead of LL-DAP as the amino-group donor, and oxaloacetate or pyruvate as the amino-group acceptor.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate
Sequence Mass (Da): 45914
Sequence Length: 411
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.
EC: 2.6.1.83
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Q6AL81 | MITINENYLKLQASYLFSDIAKRVATFQEENPEKEVIKLGIGDVTRGLTPSVIAAFHQAVDEMANDSTFHGYGPEQGYAFLREAIAENDFQSRGAGIVADEIFVSDGAKCDTSNIQEIFSAETKIAIPDPVYPVYLDTNVMAGRTGLFADGRYQNIVYLDSTKENNFVPELPTEKVDLIYLCFPNNPTGSTITKAGLKRWVDYAIENKALILFDAAYEAFIQDDTLPKSIYEIEGADKVAIEFRSFSKNAGFTGTRCAYTVVPKACMAYDSEGNSHSLHSMWNRRHCTKFNGVSYPIQRAAAATYTPEGKAECKELIDYYMANAKVVXSNHDKLGYSYVGGENSPYIWIDGKTDSWEFFDMLLSKAGVVCTPGAGFGTCCGNGYIRISAFNSPENIEKAMARITEALS | Function: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate
Sequence Mass (Da): 45078
Sequence Length: 408
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.
EC: 2.6.1.83
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B8DJJ6 | MADFKLADRLATLPPYLFAGIDKVKAEVAARGVDIISLGIGDPDMPTPDFIIEAMKKAVERPANHQYPSYVGMLEFRQEVANWYGRRFGVSLDPKTEVIGLIGSKEGIAHFPLAFVNPGDLVLVCTPNYPVYHIATGFVGGEVQFIPLVEENDYLPDLDAIPAATWDRAKMIFVNYPNNPTAATAPRAFYEKLIGICRKHNVIIAHDTAYTEVYYDENDKPMSILEVEGAKDVTIEFHSLSKTYNMTGWRVGMAVGNASLVAGLGKVKENVDSGIFQAVQEASIVALRDGDDFCRELRGIYRKRRDVVVAALNKVGIACRVPTAAFYIWAKVPAGYGSSAEFVTAVLEKTGVVLTPGNGFGTPGEGYFRISLTVDTDRLEEAVSRIANL | Function: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate
Sequence Mass (Da): 42564
Sequence Length: 389
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.
EC: 2.6.1.83
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Q7NDX4 | MKTAARLDRIPPYLFAEIDRRRDEAVARGVDIINMGIGDPDKPTPPVVLEAMHAAIDDPSTHNYPPYKGTKAYREAAAAWFERRFGVGGFHPDTEVISSIGSKEAIHNTFLAFVDPGDYTLIPDPAYPVYRTSTIFAGGEFFAMPLLPENQLLPDLEAVPETVARKAKLLWLNYPNNPTGAVASLEFFEKVVHFAKKHDILVCHDNAYSEMAYDGYKPPSILQVPGARDVAIEFLSCSKAYNMTGWRVGFVIGNRTGIAGLGQVKTNIDSGVFKAIQQAAIAAFGLDDERLHALMAVYQNRRNIIVEGLRSLGWPLEAPKATLYVWAPIPKSFGSSVEFVGALLDKCGIIVPPGNGYGEHGEGFFRIALTVPDERMREAIGRMEAAGIRFEG | Function: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate. Can also use m-DAP instead of LL-DAP as the amino-group donor.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate
Sequence Mass (Da): 43042
Sequence Length: 392
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.
EC: 2.6.1.83
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B8CX89 | MENADRIKNLPPYLFAEIDKMIARAKKEGVDVISFGIGDPDQPTPDNIINKMIEAVKDPSTHSYPSYEGMYEYRKTVADWYKNNYGRELDPDKEVVSLIGSKEGIAHLPFCYINPGDIALVPDPGYPVYKTSVLLAGGKPVQVPLVEENNFLPDLKAIDEDIARKAKLFFINYPNNPTGAIAPEEFYEELIDFADKYDIIIAHDAAYSEIGLDGYNPPSFMQFEGAKKVGIEFNSLSKPFNMTGWRVGWAVGRSDVIESLGRIKTNIDSGIFEAIQYAGIEALTGPEDNIEKMTELYSKRRDLLVEGLRELGWEVPVNKATFYIWAKVPEGYNSTEFSTHVFEKTGIFFTPGNGYGEFGEGYVRIALTVTEERIKEALERLKNSDIKFK | Function: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate
Sequence Mass (Da): 43768
Sequence Length: 389
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.
EC: 2.6.1.83
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Q8KC06 | MSNRLISGSAVALVTPFHQDGSIDFEAMRRLVRFHREAGTDIVLPCGTTGESPTLTNEEEAEIIRVVCEEAGESMMVAAGAGNNDTRHAIELARNAEKAGAQAILSVAPYYNKPSQEGYYQHFRHVAEAVSIPVIIYNVPGRTGSNVNAQTILRLARDIENVVAVKEASDNFEQIMTLIDERPENFSVMTGEDGLMLPFMALGGDGVISVAANQVPKVVKGLIDAMKAGNLEEARAINRKYRKLFRLNFIESNPVPVKYALSLMGMIEEVYRLPLVPMADANKAILRAELEKLSLV | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32386
Sequence Length: 296
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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Q0TP55 | MFKGSCVALITPFTEDGVNYEELRKLLEWHIKNHTDAILVCGTTGEGSTMTLEEKKEVIKFSVEVVNKRVPVIAGTGTNNTKASIELSKYAEEVGADMVLIITPYYNKTSQKGLYAHFNAINDAINIPIMLYNVPSRTGMNITPLMLDKLADLNNVVAIKEASGDLSQVAKMAELCGDRIAIYSGNDDQIVPILSLGGAGVVSVLANILPEETHNICEKYFLGEVIESRNLQLKYLSLANSLFIETNPIPVKTAMNLMNFNCGPLRLPLCEMEDSNLVILEENLKANGLIK | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31925
Sequence Length: 291
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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Q8RQM8 | MSTGLTAKTGVEHFGTVGVAMVTPFTESGDLDVAAGREIAAHLVDNGVDALILAGTTGESPTVTTAEKLTLLKAVREEVGDRAKLIAGAGTNNTRSSVELAEAFAEVGADGLLVVTPYYSKPSQEGLVRHFTEIAQATDLPICLYDIPGRSGIPIESDTIRRLSELPTILAMKDAKGDVVAAAPLIEETGLAWYSGDDPLNLVWLALGGSGFISVIGHAAPNALRELYTSFEEGDLARAREINATLSPLVAAQGRLGGVSMAKAALRLQGINVGDPRLPIVAPNEQELEDLRADMKKAGVL | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31451
Sequence Length: 301
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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A9KFS0 | MFNGSLVALVTPMQENGEIDYSNLKELVEWHLENDTDGLVILGTTGESPTITAEERHKIIRQVVDQVNKKIPIIVGTGANSTVHTIEMTQQAMELGADAALIVTPYYNKPTQEGLFQYFKTIAEAVPIAQILYNVPSRTACDLLPETVIRIAKCSNVVGLKEATGDIQRVKQLKAEDLDLLSGDDKTAMDFMLAGGKGVISVVANVVPKPYHAFCITAVSGNVELAKKENDQLSPLYDSLFVESNPIPVKWALSQMGVIPKGIRLPLTPLSERYHAKVRESLQQVGIKC | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31613
Sequence Length: 289
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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C0QT41 | MFKGSIVALITPFKDGAIDRKSLKRLIDFHVEKGTDGIVIAGTTGESATLTFSEHEDLIKMAVEFADKRIPIIAGTGANATHEAIALTKSAEKAGADGSLQIVPYYNKPTQEGIYQHFKAIAEETSIPLILYNIPSRTGVDMLPETFARLYSDFPNVIGIKEATGNVARVSEMISLTNPDVVILSGDDALTLPMMAVGAKGVISVANNLVPEDIATMCRLALEGRFEEARQIHDRYWKLFKTLFIETNPIPVKTAAYLMGLIDDIEMRLPLYYMKPENEEKLKSVLKDYGLIR | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32295
Sequence Length: 293
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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A6L5G7 | MIQTRLKGMGVALITPFKEDDSVDYDALLRLVDYQLQNGTDFLCVLGTTAETPTLTKEEKDKIKRLIIERVNGRIPILLGVSSNCTRAVVETLKNDDMTGVDAVLVAVPYYNKPSQEGIYQHYKAIAEATDLPVVLYNVPGRTGVNMTAETTLRLARDFKNIIAIKEASGNITQMDDIIKNKPANFDVISGDDGITFPLITLGAVGVISVIGNAFPREFSRMTRLALQGDFANALTIHHKFTELFSLLFVDGNPAGVKAMLNVMGLIENKLRLPLVPTRITTFEKMRAILNELKIKC | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32787
Sequence Length: 297
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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A4SX51 | MTNKAHSQGSKKTIQGSMPAIVTPMFEDGSLDYPGLRALLDWHVSEGSDGIVIVGTSGESPTVSVEEHCELIRVTVEQIAGRIPVIAGTGGNSTQEAIELTHFAKKVGADASLQVVPYYNKPTQEGMYAHFKKIAESVDLPVILYNVPGRTVADMAGDTVVRLAGVPGIIGIKDATGSLERGTLLINDLKRAGHHEFSVFSGDDLTAAMLMLMGGHGNISVTANVAPRLMHELCVAAMSDDVKRTREIQYQLIAVHKAMFIEANPIPVKWALHEMGKITAGIRLPLTPLSSSLREPLKAALKQANLL | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32877
Sequence Length: 307
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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B2RMB9 | MDRAQLRGMGVALITPFDEKGEVDHESLRLLADYQVAGGADYIVALGTTGESPTIEEAERSAILQTVREAVAGRCPIIVGAGGNYTERLVNRIQAMDKTGVDAILSVAPYYNKPTQEGIYRHYRTLAESTDTSIILYNVPGRTGVNIKSETTLRLATDCPNIIGIKEASGNVDQVRAIVLEKPDPFIVLSGDDHLSLSFIKEGAEGVISVIGNAYPELFSRLIHLCLENRFEEAETIQQRLEGMCYLMFVDGNPAGIKELLYQKGLIRHNILRLPLVSASDSTSTLIARVRNQIEQR | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32617
Sequence Length: 297
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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A2BZ39 | MIPNNTQFSNPIFGRILTAMVTPFKENGGVDYELAIKLANHLCENGSDGIVLCGTTGESPTLSWDEQHNLFVAVKSSLNSRSKVIVGTGSNCTSEAIEATKKAYEFGADGALVVVPYYNKPPQEGLYNHFSSIATAASDLPLMLYNIPGRTGCNLLPTTVNKLMNFPNILSIKAASGRIEEVTELRAACGPKLFIYSGDDSLLLPMLSVGAVGVVSVASHIVGLQLKMMIESFQKGEFSIALDIHEKLQPLFKALFETTNPIPIKAALELTGWQVGSPRNPLTPLIKEKKDNLFQIIQNLSL | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32683
Sequence Length: 302
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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P49423 | MSTVPEISSAPFGRLLTAMVTPFDTAGAVDFALAARLARYLVDQGSDGLIVCGTTGESPTLSWEEQYQLLETVRNAVNGSAKVLAGTGSNSTSEAIHATAKAAEAGADGALVVVPYYNKPPQAGLESHFRAVAQAAPDLPLMLYNIPGRTGCSISPITVQRLMNCSNIVSFKAASGTTNEVTDLRIRCGSRLAIYSGDDGLLLPMLSVGAVGVVSVASHIVGMRLKAMIEAYFAGENSLALSHHEQLQPLFKALFATTNPIPVKAALELIGWPVGAPRSPLLPLENQMKNELMKTISALLQT | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31764
Sequence Length: 302
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Subcellular Location: Cytoplasm
EC: 4.3.3.7
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B9JYQ3 | MKLVVVGVSGRMGQALVRIICETQGAVLHAAVGRPGSASIGRDAGDLAGVGPLGVPVTDDALAAFVNADGVIDFTRPETSVEFSALAAQARIVHIIGTTGCSPADEARFEAAARHARIVKSGNMSLGVNLLSVLVAQAAKALEASGWDIEVLEMHHKHKVDAPSGTALLLGEAAAKGRGIDLTEKAVKVRDGHTGPREPGSIGFATLRGGSVIGEHSVLLAGEGEIVTLSHSAGDRSIFARGAVKAALWAQDKKPGLYSMLDVLGLSSPH | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 27636
Sequence Length: 270
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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Q5PA93 | MKIGIVGCLGRMGRIIVQEVVGTGGVELSGGVVRRGNGLVGEDMGAVLGCGHGAKITDSKEFLFDCSDVVIDFSSPECMLECVGIASEKRVPLVSGTTGVDERDFRTHAEKVPLLWSCNMSLGVTLLLELVKMAAAGFRGYDVEIRELHHRAKKDAPSGTSLMLGKAVAQGMGVELESQQHTFGSGCRRSGAVGFSVARGGGVIGDHAVMFLGDDEIVELQHRAIDRRVFARGAIKAACWLVGKPAGLYTMSDVLRA | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 27190
Sequence Length: 257
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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O67061 | MSVRVVVCGALGRMGRRIIELALQDKDVEVVGGVEHPDCVPSIDLGEALGKEELKGKPLTSRLEELLPYTDVVIEFSGNPTAAVGHAELTTLEKKAIVIGTTGFTKQEIEQIKEFSKNAPVLLSPNMSLGVNLLFKLAEIAAKVLKDKNFDAEIMEIHHRFKKDAPSGTAMKLAEILSETLEKKNLVFGRKGEAPRKEDEIGVMALRGGDVVGDHTVYFLGFGERIELTHRATSRDTFAKGAVEAAKWIKGKEPGFYTMFDVLGL | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 28961
Sequence Length: 265
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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O29353 | MRVAVSGAAGRMGRLVVKNAVAEGLKVVQAFDINEVGKDAGELAGVGKIGVPIEDDISKLDADVLIDFTTAEAAMKNAEVAAEKGVRVVMGTTGFTDEDRKRLAELAEKVPMIVSPNFSLGVNIFWKIVEYAAKMLYEWDAEIVELHHRHKRDSPSGTALKLAEIIRKVKEEKGIEADLKTCREGISPRESEIGVFGIRGGDVVGEHTVFFFGSGERIELTHRAMSRECFAIGAVRAAKWIAKVDKPGFYTMDDFLE | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 28096
Sequence Length: 257
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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Q96VT7 | MSSPRPSTSSTSSDSGLSVDTTAYPEESKYTSTAPGAGGLSDENRYRDVEEGEAGADEPFLPSAKKQAASGSRTSRLIWGLVILCVAGWLWGLVLFVTQNRSAQQSVSEALQSHESGAISGSSSSGKPVTLEQVLTGQWLPRSHAVSWIAGPNGEDGLLVEQGEDQGKGYLRVDDIRSRKGDATSQESRVLMEKAIVQVDGRTIFPVSTWPSPNLNKVLLLSEREKNWRHSFTGKYWIFDVATQTAQPLDPSNPDGRVQLAIWSPTSDMVAFVRDNNLYLRRLSSKEVVPITKDGGADLFYGIPDWVYEEEVFSGNSVTWWSGDGKYVAFLRTNETAVPEFPVQYYLSRPSGKRPPPGLEDYPEVREIKYPKAGAPNPVVSLQFYDVEKQEVFSIEAPDDFEDDDRIVIEIVWGTEGKILVRATNRESDVLKVFLFDTKARTSKLVRTENVADIDGGWVEPTQYTWFIPADPSNGRPHDGYLDTVIHEGYEHLGYFTPLDNSEPILLTQGEWEVVDAPTAVDLRKGIVYFISTKESPTERHLYQVNLDGSNLKPLTDTSKPGYYDVSFSHGTGYALLSYRGPSIPWQAIVNTETDELKYEETIEDNAGLARMVDSYALPTEIYQNVTIDGFTLQVVERRPPHFNPAKKYPVLFYLYNGPRSQTVDRKFSIDFQSYVASSLGYIVVTVDGRGTGFSGRKTRCIVRGNLGYYEAYDQITTANLWGEKPYVDETRMSIWGWSYGGFMTLKTLEQDAGQTFQYGMAVAPVTDWRHYDSIYTERYMHTPAHNPNGYDNTSITDMTALQQTVRFLVIHGASDDNVHIQNTLVLVDKLDLAGVQNYDLHFYPDSDHSINFHNAHRMVYERLSSWLVNAFNDEWHRIADPVPDDSMWEKVKRSLPMLVN | Function: Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Catalytic Activity: Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 101256
Sequence Length: 901
Subcellular Location: Vacuole membrane
EC: 3.4.14.5
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Q3Z7V5 | MTPIKVVVHGASGKMGQEVLKTLCQENNLLPVGAVDIRAKSPALPLPDGSGSIPYSADLSSVLSQTKPDVMVDFTIAKASMPAIRIAAAHKVNLVIGTTGFSPEEISEIEQLAKTNDIGIIVAPNFALGAIIMVHLAQEASRFLASAEVIELHHDKKLDSPSGTALATAAAMLKTRGEAFNKPAKENMSDARGQEHDGIRVHSVRLPGLLAHQEVIFGAAGQSLTIRHDAFSRECYMPGVVLAIKEIVQTKGFVFGLDKLLKL | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 27943
Sequence Length: 263
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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Q6AR64 | MTKVIIAGASGRMGQRVAHMVEAHPELEYAAAFEAAGNPAIGKDIGRIVFGEENGVIVGEGLESVIADGDVIIDFTFHTATMEFARIAAKHGKAMVIGTTGLSVDELAELKDLSASFPCVQAPNMSVCVNVLFKLAKKTAAILGDDYDIEILEAHHNKKKDAPSGTALKLAEMAAEGVGRNLAEVGVYERNGIIGERDPKEIGIQTLRAADIVGEHTIYFAGAGERLEISHRAHSRDHFAKGAATAAAWLVGRENGIYDMFDVLGLQDL | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 28623
Sequence Length: 269
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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Q72BM6 | MSTPIIVMGAGGRMGSTICRLVQEEPQLCLAAVLERPDRASGVARDGCIAGSDPDVVFPQVPGGVIIDFTAPEASMATARAAARHGNAVVIGTTGFNEEQKAELAELARQIRLFWAPNMSVGVNVLLKVLPELVRLLGEKYDLEMVELHHNRKKDSPSGTALRLAECLAEARDWNLPDVACYHREGIIGERPQKEIGVQTIRGGDVVGVHTVYCLGPGERIEVTHQAHSRETFAQGALRAAAWLATQKPGKLYNMADIF | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 27984
Sequence Length: 259
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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B8E2S7 | MIKTVLFGACGKMGKVIGKALIDATDIELVGAIDPYFKGEKYEKIIGIDKISLEVVESIDELQEDFDVAIDFTNAEAAYQNIKKVLQKGKRMVVGTTGLTQEMMEEFKDLAVKNKTAILIAPNFALGAVLMIQLAKQVVKYFPDVEIIELHHNEKADAPSGTAILTAEVLREEMKKYNLTHKDATKIEKLPGARGGKLDSINIHSVRLPGLVAHQEVIFGGLGQTLSIRHDALSRECYIPGVLMAVREIVKREGFFYGLESFLNREEA | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 29649
Sequence Length: 268
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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Q3IKQ7 | MTKNKIGVFGANGRMGSALLEAASTKEHSELAAAYVRSSSPLLGINVNQLNSAADKTVTFSDEANITNVDVLIDFTLPAGMRTHLQTAVKQGVPMVIGTTGLNEADMTLLHEAANHIPIVFARNYSVGVNVLLNLVQTAATKFGDDMDIEIFEAHHRHKIDAPSGTALAIGEAIADAKGWDHDKVAVYDRSKVEQAKSQNEIGYSVLRGGDIVGEHTAYFATMGERLELTHKASSRMTFALGAIRAAGWLINKPAGLYDMQDVLDLK | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 28675
Sequence Length: 267
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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Q7UJD7 | MADSTGPISLTVHGAAGRMGRRVVALGLADPNFQLVGAIDHAKSDHLGQDSGAVAGEAPSGIEISSHWPVLDDAATNQAVIDFSLPEAIDGCVEHCVKVGSPLVVATTGLSDEQKQNLSEAAASIPVVWAPSMSLAVNLSMKIAEQITAALKDVAGGLDVEILERHHRFKADAPSGTALKFGELIAGQLGESTSHVHGREGHTGARTREEIGYHAIRVGDNPGEHTIVFGMLGEKIELNVAASNRDCYASGALAAAKWLIHQKKGPGLYSMFDVLGMSDN | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 29223
Sequence Length: 280
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular Location: Cytoplasm
EC: 1.17.1.8
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Q9X9V6 | MTDTTAPRTSGAVAAGLATIAADGTVLDTWFPAPELSDEPGPSGTERLTAEQAAELLGGGATAAVGPDARRGVEVVAVRTVISSLDEKPVDTHDVYLRLHLLSHRLVKPHGQSLDGIFAHLANVAWTSLGPVAVDDIEKVRLNARAEGLHLQVTSIDKFPRMTDYVAPKGVRIADADRVRLGAHLSAGTTVMHEGFVNFNAGTLGTSMVEGRISAGVVVGDGSDIGGGASTMGTLSGGGNVRIVIGERCLVGAEAGVGIALGDECVVEAGLYVTAGTRVTMPDGQVVKARELSGASNILFRRNSVTGTVEARPNNAVWGGLNEILHSHN | Function: Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-2-succinylamino-6-oxoheptanedioate + CoA
Sequence Mass (Da): 33932
Sequence Length: 329
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3.
Subcellular Location: Cytoplasm
EC: 2.3.1.117
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Q30RL0 | MEIIQTTEAFKALVQDIKTSINGYKEPLAFGVCRVDMGQLNLEKTLQATYPVINWNENFGSAAIFIKALQEQGVEIDFTQSEVICNINKAFLKSCLNAFSPYSEEAYGDAHKNIQVISALYNQIATSGSKDGEFKVTFIFADEPLKSVEATYLKLYALSQAKVEIRSINLNGAFGALPNVAWSNGKPLELDYLREFEIELKLANEYPHIEFVDKFPRFLQHIIPADNTRILDTSKVRFGAQLAAGTTVMPGASYVNFNAGTTGAVMVEGRISSSAVVGAGSDIGGGASILGVLSGTDGNPITIGKNTLLGANSTCGIPLGDGCIIDGGLAVFAGTKFHINDAELIELKKVNPNTKFDNYMKGWELAGLHGLHFRQNSLNGQYVVQRSTREIKLNTDLH | Function: Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-2-succinylamino-6-oxoheptanedioate + CoA
Sequence Mass (Da): 43231
Sequence Length: 398
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3.
Subcellular Location: Cytoplasm
EC: 2.3.1.117
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P56220 | MQQLQNVIESAFERRADITPANVDTVTREAVNQVIGLLDSGALRVAEKIDGQWVTHQWLKKAVLLSFRINDNKVMDGAETRYYDKVPMKFADYDEARFQKEGFRVVPPATVRQGAFIARNTVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVIVEEGSVISMGVYLGQSTRIYDRETGEIHYGRVPAGSVVVSGNLPSKDGSYSLYCAVIVKKVDAKTRGKVGINELLRTID | Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-2-succinylamino-6-oxoheptanedioate + CoA
Sequence Mass (Da): 29887
Sequence Length: 274
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3.
Subcellular Location: Cytoplasm
EC: 2.3.1.117
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B6J929 | MSETLNLLKQLIERPSITPNDAGCQTILIDRLKSVGFQCEHLPFGEVHNFWAWHGHQSPFIIFAGHTDVVPPGDETQWHSPPFTPTEKNGYIYGRGAADMKSGLAAMVVAAENFVKQNPDHNGTIGFIVTSDEEGPAENGTQKVVDYLQQKNIKLDYCIVGEASSNEKLGDAIKIGRRGSMHGELTIIGKQGHIAYPHLADNPIHRSFQAFEALAKTKWDEGNEHFTPTSFQFYNVEAGAGAANVIPATLKAKFNFRFAPIHTTQQLQQKVERILNYYQLNYDIQWNVSSQPFFSGNGRLATFVRQAIQEICHLNTEPNTYGGTSDGRFIATTGCEVIELGPVNKTAHHVNENICIADLEKLTDIYFRTLQLLT | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Function: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Sequence Mass (Da): 41644
Sequence Length: 374
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
EC: 3.5.1.18
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A5G1F7 | MAAARPFLKMHGAGNDFVVLDARAHPLDLAPAAAARIADRHRGVGCDQIILIERDDGAAAFMRILNADGSESGACGNATRCVAALLAGETGARRLTIRTNAGLLPAEIKGPTLVEVDMGAPKLGWEDIPLAEPADTLSLRLALGPVQNPAACSMGNPHATFFVDDLTHLQIETIGPKLEHARLFPERANIGFARIDAPDRIRLRVWERGAGLTLACGSGACAALVNAHRRGLAARRAEIEMDGGTLTLTWRDDGHVLMEGPVALVFEGELDAAMLAP | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 29251
Sequence Length: 277
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
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Subsets and Splits