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stringlengths 6
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stringlengths 16
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stringlengths 117
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A0A0R2HB58 | MIHQIPHLPPTLTFGTLAERVGIEIEEHRVQLPTAHLSQHPHDSALGDRRTEPNFQTDFSESQEELVTDPQPTVRKALTQLTQLQNRLMDHLKADEIIWPLSMPPYMADSDVDYLATHFERPWYADYRQILIEHYGYYQHIMTGIHVNFSLSDTISGPLLASGAYPNRNALYFQILKQVSKYRWLITYLFGASPVTENPIDDRMLARRSDITQPVRSWRSSTAGFANHRTIQLDFTNLDTFLASLDARIDAGDLYDLSEYYGPVRVKATDAYHSQHRHSVEYLEFRIFDLNPFTPSGINQNALTVLELLILDALYFPENIDNEMMQESIKINDAIALQHPDAPLPEAQQVAFKQLLAHFKLLQAQAEDGAEWQTTLDDLANNIDQPRSTISQQLVPHIHNDSLQAFATAQGEYWKTTYQNQRQ | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 423
Sequence Mass (Da): 48583
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A0A0M3J718 | MRNAARIILESTFTESSTMFLLQINGTLKGLTPGKHGFHVHERGDIGNGCIDAGGHYNPRGQPHGGPDDLQKHVGDLGNIIANLDVTFKRLSLIRFHSIVGRAIVIHEGTDDLGRGGDEGSRIAGNAGARVACGVIGIVVSFGILCR | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 147
Sequence Mass (Da): 15548
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A0A0J9XIE8 | MSYPRKPVLKSSPYHNPENYVMTPAALRARKPFFWKNIVLAGGLFALTGGIYWYTLKALIQDDFGDVPVPPVSEEELTRLRAKRDAEK | Function: Required for assembly of cytochrome c oxidase (complex IV).
Subcellular Location: Membrane
Sequence Length: 88
Sequence Mass (Da): 10039
Location Topology: Single-pass membrane protein
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Q45ZT6 | MEIVELHRKALSQTCRVCGSYVKNKKSLSSKEKYEELILSVYGIDFKLDDEDVHPPRICVSCRLWMTRSDSRNAEGPTYPTSGKTLANFSAHPELEPCSICEAYQATKSTKRKAVGTDGLPPPKIPSAAVSGTDEQQASCSFTAPSPPTARIYQPIKPQTRSDSRNAEGPTYHLCSVCAATTLTKEKAVGTDDLPPPEIPSAAVSGLDEQQASCSFTAPLPPTATAPLTPTATAPLTPTATAPLTPTATAPLTPTATAPLTPTATALLTPTATASLTPTATAPLPPTATALLTPTATRYRPIVTKDRAPFTRALFSPVLTVPARKSPARAKGSLHYVRRDCAKNRARGALDFMTSHSAAKNENETDLWFFGLHNRLRNEEDERAKMVMELWTERKKSTDLSVDDCLAMRVGTLCTKGMYAEKYSFLKSKGDKTFRPPGQLTKRESCYMPGNVRFGLMEGGKCVYHTPEKSLEEFDDHSMYEPIRINVRSKLTEFALPNCIGVAWSYPEAVAKTLEELDENIREGMLKVGLNPDGPSIIIDTTLKDGADGMGEIAVHKMKSDTFLPDKAFRASFVVLKCEVKRDDGTRDLVFEEPKPNSVIVNRPLLEAIGDENSASTSAVLMRKMEKERLILQNSIMTIHAGTYTRLHRFTIYNSMIDEKLARSSGGLQGSGSNFICTLCHATKTSAKTQLGSFKIDRTLTETQQTLTYITTNPDNLTPDELTTEAGGVKRKPLLTSEPKQQLMDATHADIDLGQFFKKIIVREMAGVHKWEASENVKQYIVDAERRLNINVRELLGTAPSLMMPGNYARALFKEKNEDVFLELIRNEERKELLRSVLQKFRALRKIYREHHPNKREVQGFKKKAVQIGRELLEHFEYVCWPNYLHKIFEHTQEAMLSEDGPGSIGILSSEGSEAANKLFRKLRNNFSRRGDVLDGLRDILWFHWLYTSPKLVRLRAVTRGTYTCSRCGAEGHNKKSCNVKAT | Cofactor: Binds 1 divalent metal cation per subunit. Mg(2+) or Mn(2+).
Function: Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T-lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. In the RAG complex, RAG1 mediates the DNA-binding to the conserved recombination signal sequences (RSS) and catalyzes the DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. RAG2 is not a catalytic component but is required for all known catalytic activities. DNA cleavage occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Subcellular Location: Nucleus
Sequence Length: 983
Sequence Mass (Da): 109119
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A0A2S9TD10 | MSFMPNIIYKKDDKEVVSDLLTKMLDDRVIMLMTPVNNISMTSVISQLLYLNVKDSKKPIHLYISSPGGSVLDGYGIIDTMNLIEAPVYTYTIGLAASMGALIFLNGTNRYMLPHSELMLHQPLGGVSGQASDIEITANRIIKMKKDINEMIATRCNLALEEVEKFTDRDRYFSATEAIEYGLADEIISKIEVKKMK | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
EC: 3.4.21.92
Subcellular Location: Cytoplasm
Sequence Length: 197
Sequence Mass (Da): 22077
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A0A1V0N1I6 | MTVNFSKKYGQVFLNDKNIAAKEVRLLGIEPGDHVLEIGPGHGILTGILLSEPVKLTAIEPDHRFYESLKISYHDHIASGKFNIIKESFLDTEPSYFDHIIGNIPYNISSPILFKILDFNFKSSILMVQKEFARRLVAKPGTKEYSRITINTSVRSTIKILFNVTRKVFSPVPDVDSAVISIIKKDVDIDLANFDKFIAKIFSMRRKKLSTILNYNGPLSEKRPEELDLSQLLTLYSRN | Function: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 239
Sequence Mass (Da): 27176
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W0LP28 | MPHCLHREPPWNEIYLLSALAALAIAIIVGLQPLFLDDVLKIPFEKSGTINANLTVVAEIVSLFVIAYLGATRHTLGRKWFVMGGFALLTIGALLAPFSLQIGGALGLGGLSVFYLARILSSLGANAAQSQLATLMGDAASHERRAGAIINIMLMMALGGGVIYAIILQIPHDIGGVLTVMLIPVGVGLAGAWLAWRRLREITSGHEELDRPMDRVWELVSGDPRMQLCFAASFYARADLIVISLFLSLWTINFADVVDQGRDYAVAHAALAVGFLGLVVILSMPLWRRFMQQRSRISAIGASVSLAGAGFIAMGFVVNPFDWMMVIPLLLIGVGQGGCLTAPKVLAAELAPPDILGAVQGIFYLVGGMGLVLLVQSGGYYFDAVGPRSPFILMGTGNLLIMLYAVYLMRTGMDENSEHTLPKKRRQLNLKPLIFLFSLLPLAWLVGRVLLSGYAPGSSLGQMPVGFINRYLGDWAFNFLLISLSLRPIYEITGVKTLAQYGRMVGLYAFFYALLHVLTYVWLEWVFKWGEMVDDIVKREFILLGVAAFVLLCALAATSFKQVVRKMGGKRWKQLHKLNYILTALVALHFIFAATHENGEPYVYALLVALLLGYRGRQYWKKRHDGASGPRPGRKRSAPHQPAKQDALVDDLA | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.
Subcellular Location: Cell membrane
Sequence Length: 653
Sequence Mass (Da): 71467
Location Topology: Multi-pass membrane protein
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A0A3P8V7E0 | MTKLLQWLLGVSLLVAVWALVTWDLLDLSLPDTYRDVAWPMPLYLLVSFGCYSLATVGYRVATFNDCEDAALELQQQIKEAKDDLKRKGLKM | Pathway: Protein modification; protein glycosylation.
Function: Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 92
Sequence Mass (Da): 10480
Location Topology: Multi-pass membrane protein
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A0A176TLZ6 | MKKSERQKIIKDLIANQLVAKQDDLMTLLKTHQVVATQATISRDMREMHIVKGTDHEGHQRYMIFETNDEDPAEALFKTFKQTAQQIDQIQFVNIIKTTPNDGNRLAAVFDDTQMPEIVGTLAGFDTIVVFSPDEALATQLHQKLAHYLSAEG | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 153
Sequence Mass (Da): 17296
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A0A6P4EP42 | MVYLNFVFGLGVVLAAAAAAVYFSWPNYPQAAPHRQTPRNRRDEDKEFDQGARLHRNFRDQRLRRSVPGDRCPVCLLNMEQRDMHHMKCGHALDNACFEDYRYLRRNCPLCNQTVNLSLPGDSCSICFDPLEKNNMVHLRCQHALHSECFQQFMNSGAKTCPLCREQL | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 168
Sequence Mass (Da): 19476
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V2YCE5 | MSSEFGKILKVSVFGQSHGTAIGVNIDGLPAGETIDLEALQHFLDRRRPGKSPLSTARKEGDVPEFLSGLENGKTCGAPLCAIIRNSDQHSGDYAELADKPRPGHADYTAWVKWKGHADMRGGGHFSGRLTAPLCIAGGIAKQILARRGIYVGAHLDSVGAACDEHFPLYPTKELFEEIAAKPFPALSDNDGARMQDVILAAKNALDSVGGVIECAAIGLPAGLGDPMFDGVENRLAAALFGIPAVKGVEFGAGFNAAARRGSENNDAFTVENGRISAGTNHAGGILGGITTGMPLVLRAAFKPTPSIAREQETVSLSKMENTKLQIHGRHDPCIAHRAVPVVEAVTATVLLDLLLEGNHGTF | Cofactor: Reduced FMN (FMNH(2)).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
Function: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 363
Sequence Mass (Da): 38109
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A0A4W2DGA4 | MAPPAPGPASGGSGEVDELFDVKNAFYIGSYQQCINEAQRVKPSSPERDVERDVFLYRAYLAQRKYGVVLDEIKPSSAPELQAVRMFAEYLASDSRRDAIVAELDREMSRSVDVTNTTFLLMAASIYFYDQNPDAALRTLHQGDSLECMAMTVQILLKLDRLDLARKELKKMQDQDEDATLTQLATAWVSLAADSGHPETLINLVVLSQHLGKPPEVTNRYLSQLKDAHRSHPFIKEYRAKENDFDRLVLQYAPSA | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated with ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors.
Subcellular Location: Membrane
Sequence Length: 256
Sequence Mass (Da): 28786
Location Topology: Peripheral membrane protein
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B0Z4B5 | KPEDWHSIAVILYVYGYNYLRSQCAYDVAPGGLLASVYHLTRIEYGIDQPEEVCIKVFALRRNPRIPSVFWIWKSADFQERESYDMLGISYDNHPRLKRILMPESWIGWPLR | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Subcellular Location: Plastid
Sequence Length: 112
Sequence Mass (Da): 13279
Location Topology: Peripheral membrane protein
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A0A0M3J4H9 | MGWLLVRKHPEVKRRGARLDLSDLYADEILMHYKLLALLCCFLIPTAVPVYFWRESALVAFLTAAVFRYCFCLHETWLINSAAHKFGFKPYEEQITPTDSFWLAVLAAGEGGHNYHHVFPQDYRTSEYSFVHNITKVVIDWMASAGLVYDRKVVSEERSRSSPNIATF | Subcellular Location: Membrane
Sequence Length: 168
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 19408
Location Topology: Multi-pass membrane protein
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A0A0M3IYU6 | MTTLPGQFSTSLIFNDHHRDLIHCVAFDFHGRRIATSSSDMIVCVWNQSSNGVWQKSASWKSHGGPVWRVIWAHPEFGQILATCSFDRSVIIWEETVRSEDETLSRNGMQSSMKAKSRTHWKRCCQLVDSRHNVTDIKFAPRHLGLMLATVSSQGMLRIYEAPDVINLSMWNLNTDITVFKYRCSALTWSSNRLKKPLIAISSDDREDVPKYIAIYEYHDSLRKWQLLNSSAIKVDEPIHDIAFAPSAGRSYHLLAIAAKNISIYKLNEDVRNDNPSQTTFYNIDLVEILENSSPSYVDMWRLSWNITGTILTAGSSDGNVRVWKANFLKKWPLIATIKSSESCKTDDPNKTTTISALPKQNHREWNKLLMILDAAENEGFHLLIVDSIGASVAMLSLTLWIVLAAVVILIAFLLYIYTRLPKKIPVQFRGKHAFITGGSKGIGKELAIGLIKRGCNVSISARDAKQLQLTCDELRTVAQSTAQANISARWYQLDVTDSFEKEFGNLYIQYHSVLKAFLEFTETLHLVEAVILKAEKECGKEIDILINNAGTCIQGAFDELSTEAFQQQFSLNCLSSIKTTHALVKRMKLARNGHIGFVCSAAGQFAMFGYSAYSMSKFALRGFAESLRMELLPFNIGVSLLYPPNTSTEGYQEELKTMPDEVREISGTAGLFTARHVAECYLNDMASGNISTSIGLEGWMLNAIASATSMENNFLRTLLESRPEFTLFSMFRELTSRKFTCQQKVTVSDQQMILLLLSVDITGADTHHNANLYERRQQNRRRMSFETSIL | Pathway: Lipid metabolism; sphingolipid metabolism.
EC: 1.1.1.102
Catalytic Activity: NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH
Sequence Length: 791
Sequence Mass (Da): 89163
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A0A0B0HCS8 | MNSRHSPGNESGFTLIEVLIALTIVAIALTSGLKMLGQYTSNLGSIQERTWADWTAMDNLVALQLSEQWSKTGEVKGTEKQTPYRFNWLRKVSETPYENVRRIEVEILNGADNQSLHRLSCYTGKESSW | PTM: Cleaved by prepilin peptidase.
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 129
Sequence Mass (Da): 14593
Location Topology: Single-pass membrane protein
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A0A538LCN4 | MYHRGQATLDVAPAAVRDAIAFLKDHADEPYELLMSVHGCDYFPEEPRLAVHYQLLAMQRTDRLGVRTRMGADDARVPSVVDLFPGADFQEREVFDMFGVVFDGHPDLRRILMPEDYEGYPQRRDFPMGGEPVLFTFNEHEMPRWYD | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 147
Sequence Mass (Da): 17066
Location Topology: Peripheral membrane protein
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A0A0U2ER12 | LYLVFGAWAGMVGTALSLLIRAELAQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFC | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 219
Sequence Mass (Da): 23340
Location Topology: Multi-pass membrane protein
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A0A0R2KC00 | MKWTKLYVRCSLQAQEAVSNLLLENGAGGIQIDDAPTTQQIVLATYFDNDEVTAPLIEKLTSALERLKEYGLDPGTYQIGTENLDDSQWSNEWKKYYHAQRISRYLAIAPSWESIQDFDDQTKVIRLDPGKSFGTGTHPTTILALHALEASVHGQKKMIDVGTGSGVLSIAAKYLGVEQVDAYDVDDESIKAAQENFNLNPLAKDITLKKNSLLDGVTGQVELIVANILAEIIVPLIPQAAAHLQDQGTLILSGIIADKLPLIEKTLQDNGFVVKETLKMKDWYGVIAVIPQDK | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 294
Sequence Mass (Da): 32348
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A0A4P6JCU2 | MIEKTYFTGSIEAIFFSNPSNFYKVLLIEIDETNAEYDDFEIVVNGTIGDVVEGDSYTFYGQLTQHPKYGEQLQVSQYEKAVPTSGAGLVKYFSSDKFPGIGKKTAEKIVETFPENTVDSILEAPEKLDGLLTLARKNSFIKRLRENHGMEKVLTKLAEYGLPSKITFQIYELYKEETIEKIEENPYQLVEDVKGVGFKTADKIASSLGIEADSPNRFRAALMHEVNTHSQSTGDTYIEAKNLLEMTIDLLEEARNVEVNPSAVAEEINGLIVDGKVQQEGTKIFENSLYFAEDGIRKSLTALTNRSGKDFADEKLLTVLAEVERDLEITYDDLQKQAIIGAMNQQFFILTGGPGTGKTTIINGFIETYARIHQLDLDPDHYNDDVFPILLAAPTGRASRRMNELTGLPAATIHRHLGLGQDEAEDALGNELSGALLIVDEFSMVDTWLANKLFQAIPGSMKVLLVGDADQLPSVGPGQIFADLLKIPEIPSVKLDKIFRQGDDSTITDLAHHIKDGQLPSDFTAKKPDRSYFEVSANFVPQMVEQIASAWQKRGNNPFELQILAPMYKGMAGINAMNVLLQNLFNPLNDRLEFALGDMKFREGDKVLHLVNDAEANVFNGDLGQIVELIAAKYTDSKQDELVMDFDGQELTYPRAEWYKITLAYAMSIHKSQGSEFSTVIVPMVSSYSRMLERNLLYTAITRAKQSLILLGEERAFAQAVAREGANRKTYLIERFMGENPAAKNLSVEMVSEKVTDKKERSDKEKKPAAPVELQGQIRSVSKKMPAQVEEISLFEDEEIETLDQGSLTEALILSGNFDPLIGLTQQDFAIFNK | Function: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase. Has no activity on blunt DNA or DNA with 3'-overhangs, requires at least 10 bases of 5'-ssDNA for helicase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 834
Sequence Mass (Da): 92992
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A0A0R2HAK1 | MTKALFPGSFDPITNGHVDIIERAGNLFDEIIIGVANNTSKTGMFTLAEREALVQASIASKSNVSVVAITGLTADYAQAHEVDTIIRGLRNAQDFSYEEPIAQMNVTLSGVETIFMPAKPQNMMLSSSMIKEVAKAGGDISNFVPTPVAEAMQQKLMR | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
EC: 2.7.7.3
Subcellular Location: Cytoplasm
Sequence Length: 158
Sequence Mass (Da): 17008
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A0A8T6TV03 | MTAEESVLVIGGGIAGFQAALDLAAAGVQVHLVEKTPSIGGRMAQLDKTFPTNDCSMCILAPKM | Pathway: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B heterodisulfide: step 1/1.
Function: Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B).
EC: 1.8.-.-
Sequence Length: 64
Sequence Mass (Da): 6576
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A0A0K2X6S0 | MKTNPPAMHVLLNAPALKNYPKDSLKSLATALFKAHQETPFTCTNLDEWVGLVKERYHAVMSPPLKPLYNATGVVLSTNLGRACLEPSHLKELELLSGYVNLEVDDTGKRANRCHLVQELLKMLFGAEDALILNNNASALVLVASVFAPKAQNKETLLSYGQLVEIGGHFRAHELLDCVTNLKFVGSTNKTYLQDYQHALSPQTTLITTIHLSNFLQQGFVASVGAKELFKLATAHKILFYEDLGSLQSVPQVQKFLKHAHLVSFSADKLLGSVQGGIVLGAKECVQALAKHPLYRAFRADKIQIYMLARSLQAHIQGQTNPTQRFLAQDQDALLNKALKLLQLLGGMPATLIETTALIGGGVVDTGLKSFGLLLTPKRDFKEFHNVLHQQGLACVLRSDGVLLDTFALFEKDLVGIARIVKSAL | Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1.
Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
EC: 2.9.1.1
Subcellular Location: Cytoplasm
Sequence Length: 425
Sequence Mass (Da): 46576
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A0A0B0HBU8 | MSLTIAVVAAEPSGDLLGAALMVALKSRHADIRFIGVGGPEMTAAGLDSRIPLEKLSIMGIFEVLPRLPELLKLRKQLRLWLIEQKPDIFIGIDAPDFNLGLARSLKETGIKTIQYVSPSVWAWKEKRVKKIRASVDRVLCLFPFEESFLHRHHVAATYVGHQMADQLPMSPNRREAREELGVPEDANILALLPGSRATEVERLARPFLQTAVEASAQLDNLHVVVPLVNATTRDLFEKLAEPFRSELNLVLVNRNATAVITAADVVLLASGTATLQGMLCKRPMVVGYKVSSLTAAYIRLFRMIKIPYLAIANLLCDEMLAPEFIQERCRAELMTPAVVQMFTDKEQTQNIVKRYTEIHEQLRCAAAASAAEAVLDQLRYTGGGANHA | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Length: 389
Sequence Mass (Da): 43022
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A0A0M3K0Q3 | MDENETKEERVSKMQEAENETNCDVIDVNENEIKIRKKTEPFGQANDGEQQQKQRSSTSTSSETGTDSQHDNKGFPRSWSPSSPSLSQRTDSSWIARVRNYVASTNLCTTNDEDNEFNDNLRRCNEAIQAGIDPLRIPSGSSVFSMRSIWLIFDEFVIHSFFXXXXXXXXXXXXXXXYPITDIYPKLVLHLSTKNLRFGRNEERIFLMTTQFQLNIVPKTRVVKLASPAFFYSRSCCKTQMPRLKAGSYQLFVHGFKSAAEVVPEWSRQGRACPLTPREICRFKMLFQKMCVLDYVIRNTDRHMDNWLIRYEKDEVLEIAAIDNGLAFPIKHPETTSRLRPFPFGWAHLMWAKMVCEFLLVHVPK | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+)
EC: 2.7.1.67
Subcellular Location: Membrane
Sequence Length: 365
Sequence Mass (Da): 42254
Location Topology: Peripheral membrane protein
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A0A085UCI9 | MVRILVLNLGSTSSKLAIYDDTKMSYSTTVVHDDALTRLDLLKQKAPRQMAIKQWLSKINVPSSTLDAIACRGGLLKPIVGGTYTVNRALYDDLKSFQYGIHASNLSGIIGYEMATHLNIPVFTSDPVVVDEFIDEVRMTGIPGIQRKSIFHALNHKATARQFAKDVQQRYEDLNLIVIHMGGGVSVAAHEKGLVIDVNEALYGEGPMALNRSGSIPNDALIEYQHAHQYDIQQMKRLFSAQTGLQAHVGSSDFKWIMERYHHDTHIHGVVDAFSVQIAKAIGERAALLKGNVDQIVFTGGMSHSTLFIDLLKPYIEWIAPVSVYPGEFEMQALAENAYQALGEHIPVKTYS | Catalytic Activity: ATP + butanoate = ADP + butanoyl phosphate
EC: 2.7.2.7
Subcellular Location: Cytoplasm
Sequence Length: 352
Sequence Mass (Da): 38991
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Q7TQ74 | MITAGLIHWILNTLNITVHIRDVCVFLAPTFSGLTSISTFLLTRELWNQGAGLLAACFIAIVPGYISRSVAGSFDNEGIAIFALQFTYYLWGHSGVVLCFPAHRSPGPFGSSGHSLTISLVAAALPSGALVHVARPELYRVSAWGGYVFIINLIPLHVFVLLLMQRYSKRVYIGVFALLQAYAFLQYLRDRLTKQEFQTLFFLGVSLAAGAVFLSVIYLTYTGMQKYTFQLLHQCLNISLRHGCLSSLIYIFLCVPSQQAYGSASKISTMKEYLAGKVRKHVTEQEKPEEGLGPNIKSIVTMLMLMLLMMFAVHCTWVTSNAYSSPSVVLASYNHDGTRNILDDFREAYFWLRQNTDEHARVMSWWDYGYQIAGMANRTTLVDNNTWNNSHIALVGKAMSSNETAAYKIMRSLDVDYVLVIFGGVIGYSGDDINKFLWMVRIAEGEHPKDIREGDYFTQQGEFRVDRAGSPTLLNCLMYKMSYYRFGEMQLDFRTPPGFDRTRNAEIGNKDIKFKHLEEAFTSEHWLVRIYKVKAPDNRETLGHKPRVTNIFPKQKYLSKKDLAASTEERGPHTQGLTVLSEEEQKKGWRLSVSGILGSEENVLPDCGQHHSTDHSNLHQEQGQMWTDNLGLGSEQVSAKGGHSPFCQDRAPFSDRDFNRLCPFSLHWDMSWQNCGNVRKNTESREQKGAQDYPGQPRRV | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein] = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-asparaginy-[protein]
EC: 2.4.99.18
Subcellular Location: Membrane
Sequence Length: 700
Sequence Mass (Da): 79138
Location Topology: Multi-pass membrane protein
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A0A0M3K648 | MDYKTEQKDRGPHTRHPSAPSYWRVTKLHRICDALYYFGTFPVGVATCVMFWVLYAIEPTLVMPLWAEKLIPRFVNHVTHTAPIPFVLVDTLLTCHHAPPKKLGSVVSVALVFGYYFIVLMVRLVDGYWLYPLFDHLNGVYFTGVFILSCIGFCALYVLGDFMNTVLWVPHHITFPASRCLCSEIEVMRLIRTSFSEGKTHEQEVDTFSVASSNEILIHLMLPT | Catalytic Activity: 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H(+)
Subcellular Location: Membrane
Sequence Length: 224
Sequence Mass (Da): 25631
Location Topology: Multi-pass membrane protein
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A0A8T6XCT6 | MKVLGGSASPLLATRLARELDVALGKVDTKRFPDGECYVRIHDDLEREDVILVQSTRNDEELVELLLLQDAIQEFRVRSLITVVPYFGYARQDKLFNKGEAISSRALIQAIQRNTDTVLLCDVHNLMILTYFDIPVENVSGMLQIAQYLKDAGVEMVLSPDEGSVSRARIVGQIIGTSVDYLEKTRIDGETVKITTKMLDVYRKRVAIVDDIIATGGTIVEAAKQLKDQGAKEVIAACTHGLFAQGALEKLEKVVDTIVSSDSIENETSAVSVAPELCKAIKNYQ | Cofactor: Binds 2 Mg(2+) ions per subunit.
Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
EC: 2.7.6.1
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)
Sequence Length: 285
Sequence Mass (Da): 31414
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A0A6V8EM17 | MVEEADLKQWRDAGHVARRTLEGIKDEIQEGKTWLEVIDSAERFIRRHGGQAAFPVTISVNEIAAHFTPSHQDLAPEGWDKPMTFEKGDLVKLDVGVHIKGALADNALTIEVGNQNKHTEQIKAAREARDAAIEKMHPGTPWHEIGQAAEQVTKDAGFEPIRNLCGHELERWNLHSGTSIPSYACGPNSGFKGKAETGSVYAIEPFNTTGKTGMIENIQPTGSSNILRVTGDVSIRKALSKGKLKPLGATMARYIEERYHTLPFASRWAYPLLEKPFPTEDAESLQKKWKAMIKKLTAIRFLEVYEALRDVDGGNVGQFEHTVIVTEGGPEVLTVL | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
EC: 3.4.11.18
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Length: 336
Sequence Mass (Da): 37182
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A0A6I3GG00 | MGHASRGQRSHGQARTGLSYSHPPPDLIRVRLDISYDGGAFKGFAENLGVTTVAGLLRAKLEKVYSQPIVLTCAGRTDAGVHARQQVVTFGVRGKKVEPIRLRNSLNALLAPSVVTSQVSIVETQFDARYAAMWRQYRYLVLNSEIPDPLLATTTWWVDKPLHLESMQEACEALIGLHDFTSFCKRPKDIPNATLVRRLLQAEWTVEPELNGRHELLRFEVAGSAFCHQMVRSLVGTLVDVGRGRFTAAQVGQILAAKDRSLSSNVAPPHALSLWKIGYPGDETPVWLSTPRP | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 293
Sequence Mass (Da): 32384
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A0A958J0I8 | MSTILHAESFGNAPDKVLFLHGFMGCASDWQPIISFLKNDHCCIAMDLPGHGKSVGVAQDLTWDFTFVANAVIETLVKMDAVPCDLVGYSMGGRLALYLALTFPKYFRRVVLESASPGLRTPDERDKRQQTDQTLALRLENEPFSGFLDDWYRQPLFATLRNHSNFELLFRRRNQNQPKLLAKSLRELGTGVQPSLWDALPELKNPMVLLVGEKDVKFRAIAEQMQSHNAQISIEIVQNTGHNIHAESPVVFANVVQRFLR | Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 3/7.
Function: Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC).
EC: 4.2.99.20
Catalytic Activity: 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate + pyruvate
Sequence Length: 261
Sequence Mass (Da): 29481
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A0A2G6DWD5 | MTLELPLTWLVGVLLAAVRIGGWLLIAPPFSHGAIPARVRVLLSVGLAFSVAPAIPADLLAGSAAPQTMRLILTGATEFLIGSGLGLMTMIIFAALQVAGTVIDLMAGFAMSQIFDPLTGSGAAVLGRMYHMTALVLLFATNAHLVVLGGLLRTYAEVPVGATVNLSGLAREGTDVFAGMFLAAIQIAAPILAVLFLTDIGLGLLTRVAPALNAFAMGFPIKILVTVVLIGLSYAGLGDLLRALTEQVLDVYGRLWP | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 257
Sequence Mass (Da): 26641
Location Topology: Multi-pass membrane protein
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A0A6A8MTV0 | MSDLKTWGYLRREAKDRLEAGGFVGGDQEAQWLVEEVSGMNSAELIASAKTFASVRATEQLDTLLERRLIGEPLQYVLGSWSFRGIDLMVDRRVLIPRPETETLVGLALIEAQRMGLKPGEVVVDLGTGSGAIAIGLAAQLFEVAIWATDVDSRALEVARANVAARGRMSAGIQIVQGSWFDALPHELSGRVRLVVSNPPYIAEDEIPELPPEVIDYEPFSALVSGPTGSEHIETILLAAQDWLADDGVVLIELDPRRAKKTHTYALSVGFAGAVIENDLTGQPRVLIARR | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Length: 291
Sequence Mass (Da): 31621
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V2XS52 | MQQDNYYEPGRRPPERRDHGERRPPERRDRGERRPSDRRDYGERRPSYREDREPPRRPRTNHRSAGRTAGFVLLYVAAVIGVSILLACVGWTAAGDVLALNKEYKEVTFTVSPGEDFDSVADRMKEEGLIEYKLLFNLFASVTHKKDSVAAGTYSLNTDMDYRALLAGVRANSANRSQVQVTIPEGYNIDQIFALLVEKGVANSVDELEEAAANHDYAFSFLEDIPLGNYRRLEGYLMPDTYTFYTPHDPVLALNKLMVYFDSQMTEDLMSQVEGSGYTLHEILTIASLIEREATSTDRTEVSAVIHNRLKNSKATQGLLQVDATLVYINGGKEPTEADKSIDSPYNTYKYPGLPPTPIANPGMEAIVAALHPADSKNYYYALGDDDVHHFFKTYDQLQKFIASQERYKG | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 410
Sequence Mass (Da): 46346
Location Topology: Single-pass membrane protein
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A0A958DKQ5 | MAKRKQTPQVEMPFLDHLEELRWRLIRAMIALGIGMILCFFVAPYILEFLKYPASQLDPPLIFQFLKVQAIFIVYIEIGFFGGLTLTLPYLLFQIWSFVSPGLMPTERKYFLPLVVFSTGLFLIGLTFAFLVILPIALEFFVGLAPDGIEANIAIDLYIGFAIRIMFLFGLIFELPMVCYFLAKIGLLTDELMRKYRRHGIVAIFIIAALLTPPDPVTQVFLGVPLVLLYEFSIYIVAMVVRKRKKREAVEEARYQALLEEERRLEEEKRTEQEGS | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Location: Cell membrane
Sequence Length: 276
Sequence Mass (Da): 31817
Location Topology: Multi-pass membrane protein
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A0A803TBY4 | MDLKRIKDSIHFWYFQYLLVTCCYGLLPWEQCIINSIIFIVVAMVVYTAYVFIPIHIRLAFEFLSQMLQFHCLLANAH | Pathway: Lipid metabolism; sphingolipid metabolism.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 78
Sequence Mass (Da): 9317
Location Topology: Multi-pass membrane protein
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A0A286MTP6 | DQVYNVLVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAMSQYQTPLFVWAVLVTAVLLLLSLPVLAAG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 155
Sequence Mass (Da): 16491
Location Topology: Multi-pass membrane protein
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A0A163WJ76 | MRKTKVERLDALRKLLSEKEVGDQIEITKLLKDLGFKVTQATISRDLLELGAARVSIRPGVHRYQIISEKNTADIRRRLEIAFRDSVESVNMSGNLMLIRTNPGAAAGVAHAFDQYGFQDVVGTVAGDDTILAVCSDEESCTVLRNKLLPILGNRF | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 156
Sequence Mass (Da): 17284
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A0A2A2MQS0 | MSVWTVLGGGAIGGFVAASLMRSGMSVSLCLSERYRNKPYHPLKFESAEGVHDEFSPDWVFAPVAQTKVLLVCLKSYHVVAALEKHQRHIDPECVIVLLHNGMGVSESVQQRFPHNPIVLGTTANAVVSVGDLSVKQMGYGDTWLGTLEAHDGLTNASLARWFQAIPRSYWTQNIAEKVWLKLAVNSAINPITALHQCRNGALMEEAHRPLFEQVVQEIYAVCTAERLPWSQQELRRKIVEVVELTAQNYSSMNRDVFYGRKTEIESILGHLINRAHLSGIMLPNCRRLYDGIKQMESHYLTQSDTDQHSATLVTL | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 316
Sequence Mass (Da): 35379
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A0A0B0HER2 | MKHDKIVALLAGAATSFSFAPYELWWLAILAPAFWLAITLDKTPEQAFRRGWLFGVGLMTPGLYWVHHSMSAYADTPYAIAVAVALLLALTMALYYGLAGHLSARWTLSHSSRARLLMMVALFGLGEWLRSWLFSGFPWLLLGYSQIDTPLGAYAPVGGVWLVSLLTMVCAALLVSMTRPGVTPRSISILLLLAIGAGGYQLSGVQWTHKKGDPIRVSMIQGNIPQDEKWLPENRLPTLAFYSDTTLELLDSELVIWPESAIPDFLFSVERELIEPLNAKLVESSTTLVTGVLTYPAEATYYNTILATGRERHFYHKRHLVPFGEYFPLGWLWKGWISGLATMGEDFSEGQAQRPLMQVGSHLAGVSICYEIIFPEEVRESLPDADFLINLSNDGWFGTTSGPLQHYQMARMRSLENGRMTLRSTNTGVTAVIGLDGQTIKQLPQFTRGVLTAEVQPYQGMTPYSRFGIYPAAALVLLLLLAARLSGRGN | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
EC: 2.3.1.269
Subcellular Location: Cell membrane
Sequence Length: 490
Sequence Mass (Da): 54253
Location Topology: Multi-pass membrane protein
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A0A6I3X4G0 | MIRLASAADLATIHGLEQILFPDDAWPLEKIDDDLHSPYARFVVADAEGQVAGYAIAQYLPGNDVADIQNIAVVESHRGRGVGAELLDNLIAWSVDQGASAIMLEVRDDNTVAQSLYASRGFAVIATRAQYYQPAGVDALVMRKEVSA | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 148
Sequence Mass (Da): 15942
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A0A0G3ZB58 | TLYFMFGMWSGMVGSAMSMIIRIELGLPGSFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIMSSITEMGAGTGWTVYPPLSSNLAHSGASVDMAIFSLHLAGVSSILGAVNFISTIFNMRPAGMTPEYTPLFVWSVGITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 219
Sequence Mass (Da): 23751
Location Topology: Multi-pass membrane protein
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A0A537VPD6 | MPKSRGRPKQRSSRYQLEPQRKKKVKASPRWYGPLMLVLMGIGVVAIVWNYTRGDQASNTVLMGGLGVIAIGFFGVTFWR | Function: Involved in cell division.
Subcellular Location: Cell membrane
Sequence Length: 80
Sequence Mass (Da): 9040
Location Topology: Multi-pass membrane protein
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B2RZ71 | MATAMYLEHYLDSIENLPCELQRNFQLMRELDQRTEDKKAEIDILAAEYISTVKTLSSAQRVEHLQKIQSAYSKCKEYSDDKVQLAMQTYEMVDKHIRRLDADLARFEADLKDRMDGSDFESTGSRSLKKGRSQKEKRSSRGRGRRTSEEDTPKKKKHKSGSEFNDSILSVHPSDVLDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCPIEWFHFACVDLTTKPKGKWFCPRCVQEKRKKK | Function: Component of an histone acetyltransferase complex.
Subcellular Location: Nucleus
Sequence Length: 240
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 27828
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A0A6A8MSP6 | MIAIDGPAGSGKSTVARALSDILGLSVLDTGAMYRSVALVALESGTSLEDFKECARIANEIEINLDHGVRLGSRDIEKEIRGPEVTAAVSKVAAIPEVRVALVARQRQWALNHGGGIVEGRDIGTVVFPNATLKVFLTARDSERARRRQSDEVAAQRSIAVDEVAQEIARRDHLDSTRAASPLVADPDALSVDTSDNTVNEVVAEILRHYSAKDEQ | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 216
Sequence Mass (Da): 23177
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A0A0M3JAQ6 | MFWGMVLVINLFKGNDWSRTGIFPRVTMCDFEVRELGNIHRWSVQCVLPLNMFSEKLYIILWFWLHIVLVVTFVNLTIWMFQILRDQSRMDFIKEMLDNAQVNGKL | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 106
Sequence Mass (Da): 12758
Location Topology: Multi-pass membrane protein
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A0A8B8ZVF7 | MDIFQRAFASQVFPPHLTNKLGIKHVNVVLLYESSSANKIFMACRIRKLLNGREQKVVQGLAEDAIDFAAETWHSVGPFLILYLLLIVRIA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
EC: 3.6.4.6
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 91
Sequence Mass (Da): 10296
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A0A7V1YJU6 | MKGRVDAERRLLHRVIDEIATNVDLDAVLRATVEVVTEATGGDACFLHLWDPAEERLVLRAATAGFEDVVGRITLRLGEGVAGWVAQHRQVVTIPEDKWADPRYKYIPELRGEEFTSMLSVPVVSRSGSLVGVFNVHSRERRDFSPDDVAFLRMTASLVAGAIERAHLFRALAEKEAELEALMRRTIEAQEEERRRVATEIHDGVTQQMVSVWYRLQAALRALRSDPDRAEAELARARELVDEALEEARAAIYDLRPSILDDLGLVPSLRTLAARQLEGLELELELPETISLPPHHEVALYRIAQESITNVRKHAEASRVRIALRQEGDDVVLVVEDDGRGFDATASSPGRISFGLTGMRERASLAGGTLEVASEPGRGTRLEVRIPCQPAEVRR | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 395
Sequence Mass (Da): 43947
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A0A4P2USK8 | TLYLLFALWSGLIGLALSLLIRAELGQPGSLLGDDQLYNVIVTAHAFMMIFFLVMPMMIGGFGNWLIPLMIGAPDMAFPRLNNLSFWLLVPALFLLLSSSLVESGVGTGWTVYPPLSGNVAHSGASVDLAIFSLHLAGASSILGAINFISTVGNMRSPGVVAERIPLFVWAVTVTAVLLVAALPVLAGAITMLLTDRNINTSFFDPVGGGDPILYMHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 219
Sequence Mass (Da): 23276
Location Topology: Multi-pass membrane protein
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A0A5K1VGX5 | MANSKFAYVKQLEEERRVLPCCYFVVRIDGGNFKAFTKTHGYTKPNDIRGLHLMNACAKEVMEKFDEIDLAYGHSDEYSFLFRKKTKVWNRRYDKILTNVVSCFSGSFPFLWKIFFPEQELLYVPSFDGRIVLLPTEREAKDYFRWRQVDCHINTQYNECFWNLINKDGYSHQQAYNTLITTQKKEKNELLFSKFGINYNDLPEIFRRGSILMRTEQILKGGHVAEQVDITQMESDKVAPPEEIPSDATIPCQRDALEKFTLSHENLVSDIFWEKYHFLFAK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage.
EC: 2.7.7.79
Catalytic Activity: a 5'-end ribonucleotide-tRNA(His) + ATP + GTP + H2O = a 5'-end phospho-guanosine-ribonucleotide-tRNA(His) + AMP + 2 diphosphate + H(+)
Sequence Length: 282
Sequence Mass (Da): 33331
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A0A7M7PM13 | MAADSSAVLPQHHGDTLGTYVEQYGGHEILDLSDASFQQKLEQIKDQIKKEIRKELKIKEGAENMRKVTTDKKSLANVNNLVKQANARLQELQQELNELNARIVVNTEDMAPSGGESDPLSPDQNDAPPPKPNPNSRIGALEKQLNIEMKVKQGAENMIHMYSSGPTKDRKLLAEAQQMLQDSKTKIEFIRMQILKTQQAQQSRQIPTGEKEAGEVSDMGFRRTSAVELQLTPIEFRVEEVRHHYKVELALVEGFKNVIKMYNNAKTSDKKGLAEAQKGLVEASHKLDILREGLEKRIQELPPDQTRFNQIKEELKSGKIKSDNPLPKPAALTGVLEVRIMGCQDLQEMIPYRARNSITSLNSPSESKGGILRGKASFHGRSSSRSSSTKEEISNEISAIMKLDSVLVGQTPFKPISNQCWDQKFLFNLDKARELEINVRWKDQRSLCAVKFLRLEDFLDNQRHGMCLNLEPEGLLFTEITFTTPVIERRTKLRRQRKIFPKHKGKNFLRAGQMNINVATWGRLMKRSIPSSLTPSGTSPPTAIRPRPPIQRLSFGEADSSESVGSNSQEGGAGSPSKDKMGGVEVQDALSSFDFLNNSSSSSPKVSSPLTPPAARSSPPPSPLSQTQGQHGAQEISAMDDGTLMTLENFRLISVLGRGHFGKVLLTEYKTTGEFFAIKALKKRDVVAREEVESLMCEKRIFEAANSIRHPFLVNLFACFQTEHHVCFVMEYAMGGDLMMHIHNDVFTEPRTVFYSACVVLGLQYLHENKIVYRDLKLDNLLLDQDGFLKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTEPYYTRAVDWWGLGVLIFEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAVAIMRRLLRRNPMRRLGSSQRDAEDIKMQGFFRNINWDDLLMRRVTPAFVPKIANSEDVSNFDEEFTAEHPVLTPAKDPRELTDEEQEHFKDFNYIADWC | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.13
Subcellular Location: Cleavage furrow
Sequence Length: 977
Sequence Mass (Da): 110193
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D8R9U9 | MELPDGAFQASDDDLSSVAADSWSVRSEYGSVLDADELVRQAESVIETTGAQDSYSSCKDEEESLQSVLGLQSHWNSTYADELNNFYAHGDRGEIWFGESVTDTVARWTARLCAATSTGTPFNPADGPLPAPSDLTGWSVLDVGTGNGVFLHAFYRLGFTDLTGIDYSEGAIELAIAIAQRNGLADIKFLVDDLLETNLKEQYRLVTDKGTLDAIGLHPEGQSRRLLYWKSISQLVAPGGILASRDLFFLVVTSCNKTKDELVNEATNAADDFKFEYMDHIRSYPTFRFAGVEGSRVSTVAFLRKA | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 306
Sequence Mass (Da): 33498
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S0DG72 | MSMYNMLLLQDMMSWVGIEASLFHDYSMVLLCLIGMGFCFFMGLMYVSGNFFLKGYSSSDYLEFTWTVVPAFLLYSLGVPSLYLMYFMEGASKYDLTLKVIGHQWYWSYELNDFDTDISFDSYMVNVTDLGLGEFRLLEVDSVVSLPFLSKIRVLVSSGDVLHSWALPSMGLKIDACPGRLNFMNISCMRPSVIFGQCSEICGVNHSFMPISIEFISWDDFLNCYVS | Cofactor: Binds a copper A center.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Membrane
Sequence Length: 227
Sequence Mass (Da): 25911
Location Topology: Multi-pass membrane protein
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A0A183G2S2 | MFLIGTGHMTESIRKEISTFKDILQVDVQDSYFNLVYKVTFEICNKLVPIEFRSFVWFQLLASYRWIAANHPDKHVLKIDSDVAVLLDEVESLLVDPSERLIQCSVNRYTMVERRVSHKWYIPESALPEFFLPNYCDGPMYLMTPAAMASILDVAWRAKVFEVEDVFFTGVLSRMAGVQLRSQRGMWHIWVSMNIAVRLDQAIA | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 204
Sequence Mass (Da): 23675
Location Topology: Single-pass type II membrane protein
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E2QC37 | MENQVRCYNDIVSEAFDSEDVKTDTSIDQIYVEKTILKLYKEFEKNSSIDPDLPLLIKEVHSKLLKKCLINLPKSYECLDASRTWIIYWILHSLWILNDMPDHETLSAVVKFLDQCQHEDGGYGGGPRQYPHLGTTYAAVNALSIIGTDEAYDSIDRSSLQRFLWTVRDVDGSFALHKDGEQDIRGAYCAISIAKMTNTYTEALFDKTAEWIVSCQTYEGGFAGCPGMEAHGGYAFCGIASLALLNRTQLCDIDSLLRWSVNRQMRIEGGFQGRTNKLVDGCYSFWQGAAFPIISAILSKDNKELIETVLFNQSALQEYILICCQNRDGGLIDKPGKPRDIYHTCYGLSGLSVAQHGTGVMDPYVVGSPSNELNRVHPLHNVAPHLVYNSVHYFIRHPPPVKDKN | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
EC: 2.5.1.58
Catalytic Activity: (2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]
Sequence Length: 405
Sequence Mass (Da): 45493
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A0A6I2W1M6 | MRAIAVVGSSNIDMVTYTSQIPDSGETVIGNSFSTNFGGKGANQAAMASRFNSTVYMVTGVGSDIFGDQIIENMKLAGINTEYLHKFSESTGVAPIWVDETGANRIIVVPGASNLLTAKDAVTAIQTIKHLGVVVGQLEILEEVTLAAFKAAKKLGLITILNPAPAKTLSNDFLENTDWLIPNAIEFESISNSEPNQASMSDFAKKHGVGLVVTLGESGAALIDRSGKYFKIESEKVEVVDTTGAGDCFVGTFAAGLNEGLRPEIAAKLGVICATRSVTRKGAQISYPDKITVTKYLNSLAF | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2.
Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
EC: 2.7.1.15
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+)
Sequence Length: 302
Sequence Mass (Da): 31903
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A0A0M3KAG2 | MFADPYKNPYHFVVEFPRHSEEGSVHRSDVLINFIDGNPNQVNADVNGKRINLRGDLNLARSVLHLTVNGKGIATQLASKKPGEFTLIYKGSPFKMKVMPSLANNMLKFMKEKPKLDMSSVVIAPMPGAIKNVAAKEGMMVTEGQELCVMEAMKMQNSLVAGKTGKVKKVNCKPGDTVDEGFVLVELE | Pathway: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3.
EC: 6.4.1.3
Catalytic Activity: ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-CoA + ADP + H(+) + phosphate
Sequence Length: 188
Sequence Mass (Da): 20665
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D8RF47 | PRSRRSLTVVEARGGGSVDAVDRLVAAVSYLLPLFDGIQYGRYLFMQFPVLEQALEPLFPLLRAYKSFPYASFVAFFVLYLTVVRNQSFSRYVRFNAMQAVVLDVLTIVPNLVERTFGPARGLGYSLLVSFYNTVFLFLVACFAYGVISCVLGRTPRLPFVADAADAQI | Function: Involved in protein precursor import into chloroplasts.
Subcellular Location: Membrane
Sequence Length: 169
Sequence Mass (Da): 18870
Location Topology: Multi-pass membrane protein
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A0A183F4Y1 | MHGRDVIAQAQSGTGKTATFSISILQRIDENEPSVQALVMAPTRELAQQIQKVMCALGDYMNIKVHACIGGTSIRDDQRKLESGVHVVVGTPGRVNDMINRSVLQTSRIKMFVLDEADEMLSRGFKDQIYEVFKTLPQEVQVGNEA | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 146
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 16148
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A0A3P8A9B0 | MAPVTTRRSKAAKRKSAVIHQEEPNRFMSSHIVRETNKPSKVACFFDESLLTCDICLEIMHNAMNVSPCNHKFCAGCIYEWNSLNAKCPKSGDSDAFEAQEEQLEGDDDDGSGLDYSSSERWSDDDMMGSYDDDEDEGDSDTQEEYMSRRNLEKARMEKLRREKEERERLKQMEAERTRRSNAASKKERAREPRCGNGGNGCFFMCTEWHEHSFFLEVKPRAELASLFVDCPPDDFPKAGVDEDGNDKEYGTLLANDGLNMVRVSEHAVELGTPPIIAESLDLQQRLPRYRANISSLTLYPQSLCAPTWADNQRLFMCKLHVEAEGMPFVPKTFHRLARDICDTEPLEEYCKDTAGANVSLLCCQCGNPIVDAKDGSISLSYLPSDDWLETSPSADYYCRDSCGAGCDPERYLLNDNCLLTVSETGVCRADRVLLCCGCNAELGSVVKNCHDIFIFHHSVCTLTANAKPFLKTRFNSMSVFFAQLVLSSCEAQSSLKLVVRSLNKTPHLLIWLLDSYVVAASGELRNDNNAETLNEVQPFPAVKMLYKVFDAQSAAT | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
EC: 2.3.2.26
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 557
Sequence Mass (Da): 62502
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A0A7K0V8F1 | MGTRERRERSNESDRLLNSLFTGVAGVALAAVGGYGRGELSPGSDLDILFLHNGRVDEKSLAELVNKILYPLWDKSFKVDHAVRTRAETRDAASEDLKVALGLLDIRLICGDPDLVAAVQNDAIDDWRGRSRERLPQLRASLSERHQRAGELAYLLEPDLKEARGGLRDITALRAIAMSGAVNVSLEHVSSAESTLMNAREALHQVTGRDKDRLLFQEQDKVAEVLKYHDADELMSAIAQAARSVDYLLESTWHRFDHRGKDGLGRFLKKPRTTQVSPGISIAHQEVSISDGFDLSADPVIGIRTAAIAAQVGLPIAPATLQRLVSAYRDGIAQLPSPWPRAARENLITLIGAGQPMVRIWEGLDQEEILFQWLPEWRAVRSLPQRNVLHRHTVDRHMVETAVYAAALTRRVHRPDLLLFAALFHDIGKGTQEDHSERGEKLIEPLAARIGFSDADVATLKLLVKHHLLLSATATRRDLDDPATIASVTSVIPDLQTLELLHALSIADGQATGSSAWSSWKESLLSELVSRVTSALTDNTIASQPIFTDEQLQFSRSGQLRVLIEDREPDYAIEIIAPDKPGLLSIVAGVLNLARFDVRSARTQTIENSAVMKWIVTPNQYAPTVDSKLIHQMISDALVDASELSARIAQRIADYASLPTIPVPSPIVETFMDAATDATIIEVRSHDRPALLFGIGEAITKCQIDIKSAIVTTLGAEAIDTLYVTEIGGGGLSQSRAQEVADRLSAALA | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Length: 749
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
Sequence Mass (Da): 81989
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A0A7M7RDG3 | MRCTLLQYSICALVVVLTLLQLIQLTMVSWLDNRNPNSILTGAREALPMSDKQNQNQNQTHQQRDKLIHITLPPAKLNTYGSYQIFYDFAKARSRLKSVKRRDITLITHCSMNNLHHVPDLVDRWKGPISLAVFGSLSDVKTIVSYIMSLKECILGVRRNVTFHLVHPVNSVSEEAEIFGSVNNKRSIRVPLIHCSKLMEAIKASYSSVSNYAADGILYPNNLLRNVGRANILTEFHFVLDIDMLPSVGLRENFLNFVKGSSSLWLDEDMVQQMVFVLPAFEMDDRAVSKVPGDKKELLSYLEKDRVRQFYVKACLYCQNHTDYRRWTSLQSFTGQLGVAYTVEWKPMWEPFYISRSDAPLYDERFRQYGYNRISQVCELYMAGFNFAVLDKAFVVHKGFKETTEFHQQKDEENRNNYYLFLQFHTALEYQYPETKRRCIK | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-[beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-alpha-D-glucuronate = 3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + H(+) + UDP
Subcellular Location: Golgi apparatus membrane
Sequence Length: 441
Sequence Mass (Da): 51301
Location Topology: Single-pass type II membrane protein
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A0A3N4CVT4 | MRPLRAFHSAVAMYTWLPVRKHDWADRDFPDGLLAFPWLGAVLGAAVGLLGWGAAAASGSRFLGALMAVGTVAYATGAMHLDGTADVADALGSRKPAEQARAIMKQSDIGPMGVASLLVVLLLEVASLGVAPPGTWPVLMALGMAAGRVVPLAATLPGRGEEPAPGTLSSLVAGKVGAAGLWISRGAVLAAGGALTWWLLGWPVAACWSGVVAVAWLLAACWQRHLLRRLGRLNGDCYGSLIELTQLAVWLGIALTVNLIGVA | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)
EC: 2.7.8.26
Subcellular Location: Cell membrane
Sequence Length: 263
Sequence Mass (Da): 27110
Location Topology: Multi-pass membrane protein
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A0A126QB68 | SSTLCKFFGNPEVYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGAQLTYSPAILWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 173
Sequence Mass (Da): 18870
Location Topology: Multi-pass membrane protein
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A0A346D690 | TIEPAITFQILYQFLIDQIGEKLAKTRTFVTTSIKSGELLEIAKSNELEIFEVIESIGGRFSVLSSVGFFPLLFAKINVDEIIQGAIEAHKKYSTSSISQNLAYKYALFRFLMYKNFNYKTEILISYEPFLIYFNEWWKQLFGESEGKNLKGLFPASAIFTTDLHSLGQFIQDGSKIFFQTIIYIKKPKFDLGIKKLVQFNTKINKLSGKTVSEINFQAFLATTLAHSSYGNNPNLVLEIADSSPKTFGHL | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 251
Sequence Mass (Da): 28510
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A0A174RIQ1 | MKRLLALVLSMLLFLCPSHAAWGQEPDIAVASDMVIRSEEAKAVNAEGGPSIQAPSALLMEASTGQVIYEKDADTKRSPASITKIMTLILIFDALDSGKIKMTDEVVTSAHAKSMGGSQVFLEEGETQTVETMIKCIVVASGNDASVAMAEYIAGTEEEFVKMMNERAAGLGMTNTHFEDCCGLTESPDHVTTARDIALMSRELINKYPQIHNYSTIWMENITHVTKQGTKEFGLSNTNKLLKMATNFQVTGLKTGSTSLAKYCLSATAEKDGVRLIASIMAAPDYKARFADAQTLLNYGYANCRLYEDKEMLPLPELAVDNGVTDSVPLKYGGTFSYLSLNGEDLAAIEKELVLPESIAAPVEEGQSAGVIQYSLAGKKLGEVPVLTAGAVKEAGFLDYFKRVLAGFAV | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Sequence Length: 410
Sequence Mass (Da): 44144
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G3B770 | MLYLSPTYKGNELLSVDVNPEIREFVTDSFTKPTAGDLNLKDFYNEVCNKPPASMENETEEDADPEIESELQFETMLEEQPLKSATEVVAGIERPKTYIQDFFNGLKSKTTISRYCMQQLLIRVYSRVVSTRSRELRRYKAFTAEVYGELLPSFVSEVMTKVDFKPNQKFYDLGSGVGNTSFQAAIEFGAAFSGGCELMEHASRLTAIQKLVLDKHLKIFGLKPLNLRFALAQSFVNNPVVKNDVLDCDVLIVNNYLFDMKLNFEVGRLLHGLRPGTKIISLKNFITPRYKSTGDNTVFDYLEVEKHEMSDFFSVSWTANKVPYYISTVMPTIRDQYL | Function: Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.
Catalytic Activity: L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.360
Subcellular Location: Nucleus
Sequence Length: 338
Sequence Mass (Da): 38582
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E4NQ61 | MALTPETLTRHELNGLRVEVVDAANPDLVGIAGRVVVETMQTLHVDVSDTSNGGTRVCQVPKQGATLQFEIPSRDTRPTHTDEAADAEKASGTTSKLRSETAGGLEASQSGRPAEDSSAASRTSSGNCEGVAYVTVDGTRLLSRPALRTEKAGDTTWR | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
EC: 3.1.26.5
Subcellular Location: Cytoplasm
Sequence Length: 158
Sequence Mass (Da): 16635
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A0A0M3JQS0 | MGNVIFRRKKVVTEELDEIQQKAQLLEEAINKTVNSKHSMRWLCSLTLFVLTGIGISMVLFYVSDKRRRTLYSVLASFAGLTLIYLTNRLMNAYYEWCIGKKRRTFLEMTKRKLAILEQVKETETFKVAKEILEKYGDPAALPSEPMHHSSRRVDAEQRLNSPRSCEQPQRPARGGFKVAEGHMQKETPMTAATADLAKSPSNSIFPVDRVDQRGAPRQEPQQRRLPPRPFLGQNRSLIERFVDFLLADGPNYRYALVCSSCYAHNGMARDDEYDHFSYYCWVCGAFNAARKPHQAQLQLRSQLRPPQRTGISPKIGSLKLQTVQSPIIRTRSESSTSVRSSDHQANVSNTHFFLISIMGKGK | Function: Plays a role in determining ER morphology.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 363
Domain: The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation.
Sequence Mass (Da): 41445
Location Topology: Multi-pass membrane protein
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A0A0M3KE73 | MAIRRRLSFTLHFVSDSTIPRDLHFITPENFFVAFQAMDLLIGQEFNFNLAQRWAGEMEWKVAQLAGVYVVAIFSIQYVMRERKAFDLQKPLYIWNAMLALFSIMGFVRLTPAFYGQLTTRGFVSTFTEVGPCFKDNVAGYWTFLWVFSKIPELVDTMFIVLRKRPLMLMHWYHHACTGYFSFVAYASGNAFLIWIVWLNYFIHSFMYR | Pathway: Lipid metabolism; fatty acid biosynthesis.
Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 209
Sequence Mass (Da): 24708
Location Topology: Multi-pass membrane protein
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A0A183F4Z5 | MNFLSSAVSSIKPRLDDYGTDRLNYYYSTMVIMVLSVTITAKQYVGSPLQCWVPAQKGSADPYSYLRGALCNVRAFIILLLVQ | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 83
Sequence Mass (Da): 9287
Location Topology: Multi-pass membrane protein
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A0A1Y1M241 | MIVVSSQLTAVTIITSKKFLKTITMAIPIKDIKLPEDSPKELLLDKHVEFIKRYGKSDDDYEFGMSDYLRMSGMYWGLTALELVDKLHILPENDVIDFIKRCQDPETGGISACIDHDPHLLYTLSAVQILCMYDRLDAVDASAVVNYVTSLQLPDGSFTGDKWGEVDTRFSFCAVATLALLNRLDAIDVEKAVSFVESCKNFDEGFGSRPFSESHAGMVYCCLGFLSITGRCGGFCFNSYCPLICRSFGYRGSRYVGVVALRTTATFGRSQRSAGEAARRLLQLVGAVFAYDAGSIALD | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
EC: 2.5.1.60
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Length: 299
Sequence Mass (Da): 33004
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A0A7C7LV40 | MGNEVGKADPTDSNDSDESTVEELEVEIKISDSERVKQLESEVARLRGGLAGAAEVIQEIENPPMPPIVGEDFVIPDHLVSDFVRLGRQLHREGLVKASQGAVAILDPDQPGLVHSTSKTCSLGQATELDIVSGRLGQDAPPGAPDEWRVIEILIAATSLHNGGPAACIHVQPPYATTVAMEKDRIVLQPIDHYGKENLGKAVIVDPDLEDMDEYLRQVAEALQQGNMKCVVIRGLGIFAVGRNFNEAWHWAATLEHSMQVLLLARQAGMKT | Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 4.1.2.17
Catalytic Activity: L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone phosphate
Sequence Length: 272
Sequence Mass (Da): 29459
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A0A7S3N9Q6 | RMLLNQVGRVKAVLVLDKEGNALIAKYYNLPELSDKNKRAFETRLHKASKASKSSTFENSFFTLEGQIAFFRIYDDISIFVIGNEDDSELVISEVLDTLHECFDEAFSHVIDRESLINNMTAVILIIDELIDGGIIMATESATILDRINVKLSDSKKAGKDKKSTKEDEKQPEPAPSSGYYSFTSVFSNAKSSFAKTLGL | Function: The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Subcellular Location: Cytoplasm
Sequence Length: 200
Sequence Mass (Da): 22285
Location Topology: Peripheral membrane protein
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A0A3P8D716 | MTLAQLKMKVIIHLGLLSESNLRIGEKSRSGGPLGELLQWSDLIACVFLLGHNLYISTEKASLIRHVDQFPVNSPCPSRRRQVDLVITDIIGLRSFKARKDFLLRNRCRIRLVDSFGTQTEFNYRSYFNAHKAALSAKGRQAFDNLILLDSLTNPWGGHGLQLLQHWTFFPHSPDNGFLGFAIHASNVKPLFERNSLGRPVSLVYGKEKYMWNGSEAVVELLKNLTEVHATVSDLNDTDHPMFSGVVNHGFLSAAEVAALLKSVNIFVGLGFPFEGPAPLEALASGAVFINPRFEPSKSRRNTPFLRDKPTLREFTSQSPYLERIGPPHVYTVDFNDISALESVIRKAVEEKPVPFIPEEFSPHGMLIRVNMLLYRDLCSSVSVWPPPNKLVPVISSPDESCEKSCESTGLVCEPSFFPLVNMAAVMSSVAGCSPAEVGNSTEPYAPFNCSHQASSLMFSCATRPPPGSGVVRLCPCRDYMPEQISFCKTCVS | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP
EC: 2.4.1.155
Subcellular Location: Golgi apparatus membrane
Sequence Length: 493
Sequence Mass (Da): 54590
Location Topology: Single-pass type II membrane protein
|
A0A3D3QBY4 | MNPAERRRLQSERLSRSIERLAGVDSAFWRSKLDGIAPGDIRGVDDLDALPFTNKPEMREEYPFGMLAVPIERTVRLHASSGTKGKPTVVAYTAGDIATFAEVNARAIAAAGGTPKDVLHVAYGYGLFTGGLGLHYGGERLGATVVPASGGNPGLQVSLMADLGANGLACTPSFALLLAERAASDGLLERIGERLRYAVCGAEPWSEGFRSKLEAAWGGIDACDIYGLSEVMGPGVAVECREGKGALHVFDDHFLPEIVDPATGAPVGPGGQGELVLTTLTKEALPVLRYRTGDVTSFVDDACSCGRTHPRIARFSGRVDDMLVVRGVNVFPSEIEAVLLGEPAVGGQYAIVVDRRGTLLELEVRAEMAGPGGSPEEVSVRLEKRLLERLRVRVRVHVGEPGTIPRQELGKAKRVFERTLDDDPFPEQPDG | Pathway: Aromatic compound metabolism; phenylacetate degradation.
Function: Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA).
EC: 6.2.1.30
Catalytic Activity: 2-phenylacetate + ATP + CoA = AMP + diphosphate + phenylacetyl-CoA
Sequence Length: 431
Sequence Mass (Da): 46017
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A0A0M3L8J1 | GAWSALVGSALSVLIRTELAQPGSLIGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLLPLMLGSPDMAFPRLNNLSFWMLPPALTLLLAGALVEAGAGTGWTVYPPLSAQLAHSGASVDLTIFALHLAGASSILGAINFITTVINMRMEGMTLPQVPLFVWSVLVTVILLLLSLPVLAGAITMLLTDRNLNTSFFDPTGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 213
Sequence Mass (Da): 22652
Location Topology: Multi-pass membrane protein
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A0A1Y1K9U3 | MTKSQISCGNFFNYFTIIVLLGKIHGGSAQCTTPNEKRGNCIPIRECPALLGILEKGVINPDEIQLLQQSQCGYIRNQPKVCCEVETSQPVNPDVQTSELLPAPGVCGKILAPRIVGGKVARLDEFQWMALIEYSKPTGRGFHCGGALISDRYVLTAAHCIKNIPRGWRLVSVRLGEHNLQSDIDCEEYCADPPQNVAVEESIPHELYDPKSIHRYNDVAVLRLQRPVAFTDYIFPICLPSTQNTAYAGLTMTVAGWGRTENRSQSVSKMKLDVPVRPQQECISTYQKAKVELREGQICAGGVKGKDSCTGDSGGPLMYVNQTEFDQIYFITGIVSFGPSNCGLQDWPGVYTKVVDYIPWIINKLKP | EC: 3.4.21.-
Subcellular Location: Secreted
Sequence Length: 367
Domain: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Sequence Mass (Da): 40589
|
A0A7C2HSI1 | MSATQIPRSAEPLGLLRRSSVPRWQRIGAAIVCLASLAATGLVVGRSPLFAVGRIRVVGEDRLRAAEIVRRSGIEPGTNILFLDAGAVERRLEADPWIRDARVTRQLPSTVTIRVVERTPVAVMERDGRPVLVAADGTELGPVARDLRLPVLAAERDALGGGVAVPAIEAPARALAALPPELRAQVREVAVLPGGSLRLLLASGTRVLFGAPGQAAEKGRVLRSILRWALAEGVRLATIDLRAPSAPSASTA | Function: Essential cell division protein.
Subcellular Location: Cell membrane
Sequence Length: 252
Sequence Mass (Da): 26551
Location Topology: Single-pass type II membrane protein
|
A0A163VUD5 | MTPAPEGYARGFTLAPMAGFTDSAFRTIARRHGATAVVTEMVSVQGLSRRNSGSCRLLAFREEEKPIGVQLYGAEPEAFERAASIVSRMGFDFIDINAGCPVRKVLASRSGAALLRDIPRLLDVVSATSAGAGGLPVTLKIRLGWDPENPVPDDIGALAASRGASALCVHGRFRSDMFDGPVRTAGITAIAGASPIPVVANGDSTSPSAALRMRDETGASGLLIGRGAIGRPWFFRELAGLGSIQPAAGEFRETVMEHLRLSMLDVPAPFVFHMFRGQLVRYLKGFKGAASLRSLAVGVESESDVAGVLEEASKIMETA | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
EC: 1.3.1.-
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Length: 319
Sequence Mass (Da): 33631
|
A0A0M3J6C4 | MNGITSARVFTSRPALYSLREDDLDYDVTNCFHRLLAVFAEALAAVRVKYNIEHRNNKGLAMLGIQDFTFTNLWQNHAFNFVEEIDYLTFPSPMSTDVVYIGSHCPIAKRLPDDLREFTEDASSKGTIYIAFGTAVQWHSAPEYVTNAFRYMIENLRDYRILFVYNGNSFGELPEHVNVLKWAPQFDVLSHNKTILFISHGGLKSVKEAICTSTPVVY | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 218
Sequence Mass (Da): 24888
Location Topology: Single-pass membrane protein
|
A0A8B7YLJ6 | MLPADDVSADVDGEDGSTGQNNDDDGKDSEKGFTVLGGERKKKKQKVARVLPDWLAHPTVIEHDLRKHSVTVEEMEQLDSRLVRSLLDEGIKSLFPVQRHVIPVILDSARLGIHAGDAGYRPRDLCVSAPTGSGKTLAFALPIIQALLDRVVPRIRALVVLPTRDLAQQVSKVFSSLCKATDLRPALIGGLKKFAQEQRMLVQTSTGETQCDIVVATPGRLVDHINKTQGFTLQYLRFLVIDEADRMMEQISQDWISQVEKCAFTGSRPAPGPITVESCRKISLPLQKLLFSATLSQNPEKLIQLNLFRPRLITSVVTSKSRRRDTQLGEGKMEERGEFVGKYTTPVGLKEYYIQCTPGQKPLLVLHLVQTLNLRQILCFANTVEATRRLYHLIKLVGGVAVAEFSSNQTAGQRRQILKKFKAGKIQLLICSDAMARGMDVENAKYVISYDMPPYIKTYIHRVGRTARAGKTGVAFTLLQPHEVPKLLKMLKHAGKTNIQKHGTDLRDLDHLVPAYKKALQQLPGVLKMEKFHSF | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 535
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 59617
|
A0A7M7N6A8 | MTSKAKPNPKHLVQGDPIPPLKKGVPRLFSFRFCPFAHRSRLVLAAKNVDYELVNISLSKKPEWYKTKNPFGTTPCFEHDEKIVRDSSIVCEYVNDAYPGVNLWPEDPYRKAQDKMLLDYFGSKISPPFFKATYHPPPSSTEDFLAVYQKELYVLEEELKKRGSAFFFGEKPGLVDFIMWPWFERWAVLGEDFHRENYPTLMGYCGRMKEDPAVIEAATPDEIYQNNFKKQMEGNPQDDY | Function: Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA).
EC: 1.20.4.2
Catalytic Activity: 2 glutathione + H(+) + methylarsonate = glutathione disulfide + H2O + methylarsonous acid
Sequence Length: 240
Sequence Mass (Da): 27939
|
A0A6I3HQS2 | MTQSAQSPHIALIGLMGTGKSTVGRRLAKRINYGFFDTDDELQLSTSRSVRDIFANDGEEIFRDLEAQTLSDAYARVDPLVIAVAGGGVLRQSNRLLISHMTHRIWLTADIDLIIHRVSSRALTKQGHRPLIDDDPRARLTQLYSERSSVYASLATSTVDVTDLKINEVVDVLTTIVTMEVAP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 183
Sequence Mass (Da): 20234
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A0A0B0HFU1 | MEVSNTLLVGLESAVNQVLEKDQVTRERLAKLHGRRIAIELVGWVTLHCVPDGRGALQIFSAPVEEAEAVISATPFNFAETAMADRREDQVFKGKIRLRGDIHLAEAFSNILADFDFDWEEALSKIAGDLVAHQLGNNLRGVAKWAWRGRRHLNAALGEYLTEEAQLLPTAFEVDEWRDAVDETRDAVERLQARIDLLASKIKQGGTA | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for ubiquinone (coenzyme Q) biosynthesis. Binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex. May constitute a docking platform where Ubi enzymes assemble and access their SCP2-bound polyprenyl substrates.
Subcellular Location: Cytoplasm
Sequence Length: 208
Sequence Mass (Da): 23169
|
Q2F694 | MGMEKNGNAEGKLSEYLYPPEILKRLDFSKSPAKFHPKISAVDPGEDWMIVRPLQRSDYDKGFLQLLSQLTSVGNITRKQYDDRFTKMKHSGGYYVTVIEDTRINKLIGAATLTIEQKFIHNCSLRGRLEDVVVNDTYRGKQLGKLIVVTVSLLAQELGCYKMSLDCKDKLIKFYETLGYKMEPGNSNAMNMRFDEPS | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Length: 198
Sequence Mass (Da): 22588
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A0A7N0ZTB3 | MSPLLGVEHVDPGVCVHVTREFLECIQENALCQRPALRVDAATVNVHCHTALLISDHSVFSQGAVKSRPCVCVEIKPKCGFLPFSNFITEENYIKKTTTRFKMHQEFKLHHQQEISHVSEYDPIDLFSGSEDMILRAMKSLFHTPQNNFRVFLDGALVFGGLGGGTADTDVPTAIALEDALQHFINVRDGLRTDSFLKLVAKTIFKSRILDKLLQVQKLEDIDIEGAIHTYYNVISQPCTVCKSVNRNMSHKLSSLHRLPFDECLRITRDHLISATAKDCSLMVAFRPERDGYGTVPYDNVYLDSTKQSFNYKMSFIDLDMKRLEKMEHYYELDQGIVGWYNQMIHDQESNHSKGAKLCKSRVDAASDRRLNSQASAQIFHSA | Function: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).
EC: 2.7.1.158
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Length: 383
Domain: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Sequence Mass (Da): 43447
|
G3B7U8 | MVEVYSYGPHELQSVKVFQQDPSTKDAIVFIHGGGWRDPSNSFDDFKPIMKDFSKCSLNVISINYRLSPSANTEAELKKMPYFRHPFHLLDVLKALVFLVKDRGLNIISVVGHSVGATLCLQLMNYKEVLEYGFKYIPANNKMLPTKQELDEIDTTLADSHFRRIYLIDGIFDVENLVQEYGDSYRTFVRCAFDSDDHFKDAVQTSNHQLGAPHLFIQDTTKVFLIHSLEDELLSPRQTKLLATYLTSVNINHEVVLQPWGLHEEVYRRSEVSAFIIKNLF | Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.
EC: 3.5.1.9
Catalytic Activity: H2O + N-formyl-L-kynurenine = formate + H(+) + L-kynurenine
Sequence Length: 281
Domain: The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence Mass (Da): 32324
|
A0A183F9T2 | MRHNRSVVDVLFVFIPQVFFLSCIFVYLCVMVVLKWIFFYVNPTFIFGQLYPGSNCAPSLLIGLINMFMLKARDVSNQFTRTDLLCYFSGFHKSHRLLKGFVKQLTSCVTSTVFSREH | Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Location: Membrane
Sequence Length: 118
Sequence Mass (Da): 13733
Location Topology: Multi-pass membrane protein
|
K4JA71 | MLSQQWLFSTNHLDIGTLYFNFGAWAGMVGTSFSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVLPIMIGGFGNWLVPIMLGAPDMAFPRMNNMSFWLLPPALTLHLVSSLVENGAGTGWTVYPPLSSYIAHGG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 140
Sequence Mass (Da): 15289
Location Topology: Multi-pass membrane protein
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A0A7M7NVM3 | MDELDIMERNKKKLTLPLSNDCVFSPCFSQTQASPVTALSMSMVTLSCMGGTPKRRLSMSSIGEASPVPPNLSRHSSHSSGVSVGTPSPCESPLILGTFQPINPSNDQPESSRHSTQFRRFNSMPLRLQQQHQESPSLQMFHRPRLIRQHGLEEPMKEEEKEDGLWMMKPAGKRKDSEEEKEEEKADSMQLDLPSPDIVEEATLPSEGFTFVMPKPLSARPASSRVSSLNFAPAGSRPISAPATLLDEEDDDDAIQLQEDRLTSFHDDEDDDADNDDGFSDIFDTDSQEGSSSAFSDGLAGLIHGALISPAGKAINSPPSHSIASESSQSGNIPNRGVDCNTLRTTPSGGPRCRKGIFKIPSQPVLARRNSSFLKRTERPQDTPSPVQNKRPRSSSVASPQVTSMEAEKTSPKNRMCLGRSLSMLSPNDPYFRRIDQALSIEGGQHNLTGDRTKACSVPLVTGKQKDLKCISPETMCRLLRSEYDQEIAECHVIDCRYPYEFNGGHIKGAINIYEEVELKKMFLENPLPPLPNNGRRVYIFHCEFSSQRGPKMLRLLRAQDRAANLENYPALYYPELYLLNEGYKAFFEYSTEFCEPKIYTPMNHDDHLEDLRYFRAKSKSWTERSRLVTRSKSLF | Function: Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle.
EC: 3.1.3.48
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Length: 636
Sequence Mass (Da): 71177
|
A0A8B7ZFD2 | MFFQSFPDDDRPTSRSPSYVFGHNAQGRRQLSTVRLRASSWSVSGACSRLLVALTTSPGRLNRRHVILGVLYTMVGISLISTFSIWSAVTRGGRNESMIVGRRTTEEQIRNTCGTTNATTNGTCSKQRPLGLKDMAKSLGGLADLFAIQPCNGKCETKKEGKEAPKKAGAKEKSYECPKKAVCPELDIPGLVEKRSLNMQDTPMNVSVIKVMGKDWQRVESAVETGNQEMQKLLGQTARYNTSVRTPITESLSWLGIRLGNYTYLPGGHWTPTNCLPRWKVAIIFPYRNRSYHLPIVLRYLTPMLQRQLLEFAFYSINQENNLAFNRAMLMNVGFVEALNFSRWDCFIFHDVDHLPLSDFNYYGCSGMPRHFLSGADRWKYKLPYANFFGAVTGFTTSNILKINGFPNVYWGWGGEDDEIWERVKEVGLPVSRPKGPHGYYDVIKHHHSSAPALKDRMQLLRNFKPRFRLDGLNNLRYRKPRFEFHALYTNISVDIQKLPVVPHQSPRSQSTKNDRHSKAVIASQNEKRAAAAKRALANGHVKTKLASDVNTNKRDKKPEVNIKPGDRQRPDGAKQANEGLREGDPKRALNASMVKTDQVPAKPQS | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 606
Sequence Mass (Da): 68393
Location Topology: Single-pass type II membrane protein
|
H8Z9N8 | MKCNKCQNRISLQDSIKSKIELLGEEDIFMFCEDCRICYICYTQTEEPTECCKMCGYSYHTHHFPETETAQRDGDAAEEDKSRCKKCADLYSEIGFGSLLGPEIPALERNYEEIDKEQIRKITEIVKKNRPGKNTEGIQKVFLGEVEMRPLFSSPYPEEYVKYPTLHICRKCMEYFSTKYSLERHQTKCKMQYPPGRLLYLDSEYIGVFEIEGDKESRYCQSLCLLAKMFLDHKTLYYDVESFLFYIIGEIKDEEFIVQGYFSKERGEGRNNLSCIVVFPPYRKLGIGSFLIDYSYYLTKSTASLPYTAGPEQPLSAEGERAYFSYWVNAILRYIADKKNFKPEDACFEKVSEHTGVSKENIRWAYKQLVKKFGKELTYQDFIANRDIAKKSRRIKKGAAVQKSVESKDENPEESE | Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
EC: 2.3.1.48
Subcellular Location: Nucleus
Sequence Length: 416
Sequence Mass (Da): 48517
|
A0A0G4N0K7 | MGSDNAPTGPATREEMREARLPLAYRDSCAHLLIPLNRCRTETWYLPWKCSDERHGYEKCQYEEFKKRVAKMDELRASKEGARSN | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Location: Membrane
Sequence Length: 85
Sequence Mass (Da): 9950
Location Topology: Peripheral membrane protein
|
B1PK28 | MIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPFSLTLLLTSGMVDSGVGTGWTVYPPLASAIAHAGASVDLGIFSLHLAGVSSILGSVNFMTTAINMRAAGMTMDRMPLFVWSVFITTVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPAFG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 179
Sequence Mass (Da): 19273
Location Topology: Multi-pass membrane protein
|
A0A2G6JUN0 | MWFMAAKSKLPDPDASVRSVRAFRLLPEALAVPVGLGLPVLELALAVLIGIGIFTRVSSVVTVLLMVAFTIGIASVWQRGLSIDCGCFGGGGQVDPGQTRYPQEIARDILFALFGAYLVWRPDTLWSMDRRLGLTGR | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 137
Sequence Mass (Da): 14834
Location Topology: Multi-pass membrane protein
|
A0A9F2IBY5 | GTSLSILIRAELGHPGALIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGSGTGWTVYPPLSSGIAHGGASVDLTIFSLHLAGISSILGAVNFITTVINMRATGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 199
Sequence Mass (Da): 21104
Location Topology: Multi-pass membrane protein
|
A0A0J6GZL5 | MKVMNIIHDSIVDGEGLRTVVFLAGCPHMCEGCHNKQSWNINNGFDMTIDEVFEEIMTNPLTNVTYSGGEPLLHTAELIELSKKIKRNSEKDIWLYSGYTYEQILNNDKHSALLEYCDVLVDGPFEIKKRDLTLLYRGSSNQRIIKLS | Function: Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.
EC: 1.97.1.-
Catalytic Activity: glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+) + L-methionine + semiquinone [flavodoxin]
Sequence Length: 148
Sequence Mass (Da): 16926
|
A0A9D5GF08 | MIYVRNTTRKHALPLRRIERMTRALLAATGHPQASLSLSFVGDAAMRRLNREHRGYDCSTDVLSFPLYEPFAVPAKALDREAELLLGDIIISVDVAARQAHAYEATLEAEITRLLVHGVAHLLGYDHEEPRERARMRQKERTLAAAVGLAWPYE | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 154
Sequence Mass (Da): 17385
|
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