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stringlengths 6
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stringlengths 16
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stringlengths 117
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A0A2E8PSW1 | MYEEAVFLRNLRFCVFRDLATNILAKVRLGLVKHLNAHPLDYGFRKMEAHTLVEDTPARLYAMLSSAELDAALISSVECLRNEHRFGYCKSVGVCCDGALRSILYFEARKDRAHIDLANHAPSRIYADSGSRSSVALLQVLYHSATGQLPHLESAEPEKIPEAVLRGEHAGGLLIGDAALRFSQSPQADRFLIRDLGQWWKEQESLPFVFALWAYPGEKPVESALFEESLQEGLQHLPQIASESEFSFAEEYITDLLHYRLGKQELLALQRFRERLLALDLL | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Function: Catalyzes the dehydration of chorismate into 3-[(1-carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone (MK, vitamin K2).
EC: 4.2.1.151
Catalytic Activity: chorismate = 3-[(1-carboxyvinyl)-oxy]benzoate + H2O
Sequence Length: 282
Sequence Mass (Da): 31927
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A0A6P5AF33 | MLALRKLLFGTGNYTFNIEWKRTRFTFRDVKSNFPYGLFMEKLGSRGMTIHGSRGMTMCVQAYILKHLLYKDDCLLEEKGNSSNLLVERFNIGFFEDQREDALIHALADILWKAGEGKYAAVTIVGEKMCISPSPELRFDNYTEKILIYEFTDFEALLKFLRRNLDQFQGDFSPGGILMVYSAMLSRTFPKLVADMDEHKTPTILTAAEACTTALINLFLTGRAVSYLFNGKVVYDKKKKPLPYPLLGQKERAELGFLFWDKTEFEVQDRTEVGSMLKTPKLPIWLTSVNDVFGVLFCTVPDLLSHWRKEHRFCLFYFTGQTTQIQGTKLTIDNRSGRADPGGEEEEQKIPSLERCILTKWPDAVVNWNGTSPFV | Function: Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins.
EC: 3.4.19.12
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Length: 375
Sequence Mass (Da): 43001
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A0A370U8U1 | MAKEKYFDLTGKRVYVAGHTGLVGKALVRALEQRNITLITATKAELDLRDQARTHDFIATQKPDVVLLAAAKVGGIEANRTLPVDFLYDNLMIASNVIRASAEYGVARLMNLASNCYYPREAAQPLREDSLLTGPFEPTNEAYATAKLAAMRLTQYYATQHGKGFFTLVPTSLYGPGDHFDDERGHVIPALINRFHQAKQQGLSDVTLWGTGSPTREFLYIDDAVQGMLHFVEQYQRVEAINLAGGQSISIRELGETIANVVGYQGKLNWDTHKPDGMPHKALDSERCFSHDWRPETSFNKGLEQTYRYYLDYVAAT | Pathway: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 2/2.
Function: Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.
EC: 1.1.1.271
Catalytic Activity: GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADPH
Sequence Length: 317
Sequence Mass (Da): 35440
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A0A651E4I1 | MSERCFPRFPDRDIVKLIVETRTETPLDTAPISVSRVLVFANGEKPQAVELADRISETLTAENISVFRMSLGQNVAEEISLDTIDMVVSLGGDGTVLTCARAIAEYDIPILAVNLGQFGFITEIRQDEWYDAFHAFLSGNVGVSRRLMIEVRLFRDEVCIATCTGLNEMVVAATGISKIVNLTASTSRGRLGSYRADGLLVATPTGSTAYSAAAGGPILHPDLDAMILNPICPFTLSNRTLVMPGHEVVRIQVDHSQRTDVVMTVDGQEAHALKADDVIEVRRSHHRAGIIESDRRSFYEVLRSKLHWSGGR | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Location: Cytoplasm
Sequence Length: 312
Sequence Mass (Da): 34196
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A0A7X9WHJ0 | MDLNQNYLTQLHQKLDTNIENLRPYAEDNQVPIVDKLTLDMIKQLIRMNHTKNILEIGTAIGYSSMQFSSVANDIHVTTIERNEDMIALARNYFHQYGYNEQIRLIEGNALETYQQVNDREYDMIFIDAAKAQSKKFFELYTPLLRKGGIVVTDNVLYHGFVSNIDIVRSRNVRQMVKKVQQYNQWLMEQSGYTTNFLNIDDGLAISIKGE | Function: Catalyzes the methylation of 5-hydroxyuridine (ho5U) to form 5-methoxyuridine (mo5U) at position 34 in tRNAs.
EC: 2.1.1.-
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + S-adenosyl-L-methionine = 5-methoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 211
Sequence Mass (Da): 24550
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A0A137P2P7 | MSFDINWDKIKENYTKSIENFLNKKFQSLQNLPKFLGPMSVTEFNLGTIPPNIVLKDMMEPFPYFYMGQAPWDNNSFEDEDETLDGNSQMDFSLDQANTLLNRHLLNTQLEVEMDVDSDLENELEDDLNNLDLNRSHNIGNGHTSHNNATYNNNPYSPTHLRSPSGNNFPHRPHDDLMSTNSTSHPHNQLPSKSDEDLQLLFSLEYDGNISFTISSSIQLSLPFGSFMHLPMKFKISGFQFNTNFLIIYLKQTQQVKFTLFDEILISNYYSSQFNLGSGDELLNWSTSVNLGKTNLNSQLLKNLKIESEIGDPNKQVLKNVDKVEKFILEQTRKIILNHFTYPKFFDFNLNRKTSDEDGEASSGNNGEDGDIEDILDVDDSF | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM12 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Subcellular Location: Mitochondrion outer membrane
Sequence Length: 382
Sequence Mass (Da): 43819
Location Topology: Peripheral membrane protein
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A0A7S0I4S1 | LMRAQWQTLRALARRAREGFVKPNSARFAPLVLNGRTFASKVAFAGGMAIIAGHGVQTYGACSVASCSFQHDVHAEKKAGEKRLSKQIIDAVYTGTDSYGSISEEEEEEILESGGHWAYGEIEMDGFQALIEYMSMDSNSVFCDLGSGLGKSVAFAFMSSECKCAIGVELSATRHNQAKAAAERLVKVINLLRQDDAASAWLQEQQGCNTPTMMMRWGSKEMQLVHADCNKISMERTTHVYMANLTWPEAIVDEIGHKLDSNPSVKMVASLKRISEKRLRRLRQCDVLYLPMSWQDRNTVSYGVPVYIYSV | 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: 311
Sequence Mass (Da): 34553
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A0A4R1BR78 | MYEIYVAARFEAAHRLVGDFGPATRLHGHTYRLEVLVRGERLDGSGVLFDIGELRGAVDELAAGLHYRNLDDVPGLEGRNTTAEVVADHAWEKLAPGLRGRGLDSLLVRVWESPDVYAAREDAL | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.-.-.-
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 124
Sequence Mass (Da): 13681
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A0A1Y3BLH6 | MATCEFLLPKHHVDRLVRQFSDEIDKPLNGGGDDPYGFPMFNTFVTKFPSNQENGNFLGLDIGGTNLRIASVHLEPGHTDSGKEITMENFPVPIECRQGESRKVNVHFTSTNNHKLLIKCSPCFQFFDHLAKSIDHFLRRHFPQQTETIALGFTFSFGFEQLSISRGRCVQFGIQTNLPDALGKCPLELLQNSIDSAGLPVKVVVLANDSTTTLVYGRFVDPQTRASLILGS | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 2.7.1.-
Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Length: 232
Sequence Mass (Da): 25828
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A0A1V6GPT1 | MNDRADSRQTVFHDRRIQVLVTMVRLVLGTVFLSAGITKIVDPAGFALAVYNYHILPAWLVNLAAVTLPWIEVVAGVCLVLGLWVPGSALVVSVLLLAFTTALGFNMYRGLDITCGCFSTSPGSGKITWWYVLRDGSLFLSGLLVLFADRGRFSLSSALQGTDRNHHS | 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: 168
Sequence Mass (Da): 18298
Location Topology: Multi-pass membrane protein
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K6V4T2 | MIKKTLLLAADSKRLERTISRNRLTKPLVARYVAGTTLDEAVAATRELNAKGIDVSLDLLGETVSDLSESAAATAAYVDTIHALATQSPGSTVSVKLSQLGIGLDPIVCEGHLKQLLDVGAEAGITVEVDMEHSSVGPQTLEAYRSLLPGHPNTRVAIQAAMRRTPDDLASFTDIKPRIRLVKGAFLETIDKAIVDPAEVTAEYHYLSEWALKNLPDPAFGTHDDTCIDIVKAAAERLGIDKRDFEFQMLYGVRRELQEQLAADGYRVRIYVPFGSQWYPYLMRRMAERPANLMLFLRSVISD | Cofactor: Binds 1 FAD per subunit.
Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.
EC: 1.5.5.2
Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)
Sequence Length: 303
Sequence Mass (Da): 33396
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A0A3B5L7S8 | VRLVRNRQREGLIRGRMIGAAHATGEVLVFLDSHCEVNEAWLQPLLAPVQADRRTVVCPVIDIVSADTLAYFASPIVRGGFNWGLHFKWDPVPPAELGGPDGAAGPFRSPTMAGGLFAMDRKYFFELGQYDGGMDIWGGENLEISFRIWMCGGQLLIVPCSRVGHIFRKRRPYGSPGGQDTMAHNSLRLAHVWMDEFKEQYLSLRPELRNRGYGDISERVALRKRLQCRSFRWYLDAVYPEMRAVANGNKQPPPFDWSYDEDGQLVLAGLLCLDVSEVRTSDPPRLMKCHGSGGSQQWSLGVRF | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 304
Sequence Mass (Da): 34196
Location Topology: Single-pass type II membrane protein
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A0A3C1C780 | MLTYVLVGFALAADAFAVSVSAAACANALPLLIGLRAAFMFGLFQFLMPLAGWSLGSAFSALIQNYDHWIAFGLLAIVGSKMLYEALHARRKSACVDPENGTTEKATTTAGIDHGLNSAANGIMKLNTLLVLSFATSIDAMAVGLSYNLLGMPIMLPSFIIGTITFIVCIIGIEFGRRLRKLIQKGAEIVGGSILIIIGFRILIDHIIKGT | Function: Probably functions as a manganese efflux pump.
Subcellular Location: Cell membrane
Sequence Length: 211
Sequence Mass (Da): 22394
Location Topology: Multi-pass membrane protein
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A0A067NAR1 | MAESSRPVRRSARAAATRTEHRPIYAEVGLSDTEEKPTAASSDLSNLSASDGETSGPVRATKRSRSPSDDDEAFSEIDSPPPPKSRRTRKPKTSVPKSDLVASTSKSEHHASLHSVERVLPLRAPLLAWYDSVKSLRPMPWRKDYDSSLDAEARAQRAYEVLVSEIMLQQTQCATVVPYYEKWLLKFPTISALAESDIETVNGAWKGLGYYRRAKMLFAAAKKVVQDFSGRIPDDVRTLEKDIPGVGRYTAGAVASIVYNVRTPAVDGNVQRLLSRLLALHAPLKSKGPSEMIWDAGSALVRDVGTPGAFNQALIELGSTVCKPTNPDCAKCPLKDGCGAYSLSKGKNPGPVLSDIEDACTVCEAFPDASSVSVTRFPMKIEKKRAREEDSAVCVVEWRSPADERWFLIVRRPDKGLLGGLWEFPTHDFCTPPSTSALDTAPRTILSSILASSLHGLGSSPTSESKSESRSRYFKASAESDSNGDSLRITQVNQAGSVLHIFSHIRKTYHGVWVVLEGGPSGGSDAHDLPLLVDRKETGKKGETAKWIRESEVDSANMGTGTLKVWKLVQPLWGAKEVVEEKKPAKRRRATKRRDA | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs.
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Sequence Length: 596
Sequence Mass (Da): 65153
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A0A0E3UZX7 | MMKLSRSLRYVFVSAMSAILLGACASADRPSLLSTPTTARPRPIQETSANMGSLYPANSGGPYINAVSHRPLFEDRRARNVGDTLTVVLNETTSAAKNSGMTAARKANGTSTFGNNSPTFNGAMFSLANAANFSGTGDIKSEGAGTSAASNTFAGTITVTVVEILSNGNLVVAGEKQVAVSNEEEIIRFGGIVNPNTLVFNQVSSQQVADARIEYRGRGATDDTQGTGWFTRLMLKLAPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Subcellular Location: Cell outer membrane
Sequence Length: 240
Sequence Mass (Da): 25223
Location Topology: Lipid-anchor
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A0A6J0X0C7 | MSASQDSRSRDNGPDGMEPEGVIESNWNEIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQKLRERLKIH | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 210
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): 23462
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A0A6P5AI64 | MMASSGLSFENPVFAAYASYASLVVLKMFFVALYTTHTRFRVGVFANSEDVKGNKGAVARLDNPDVERVRRLHRNDLENIPAFLVVGLLYVLTGPSPGVAVWHFRVFAASRCLHTVSYLASRQPHRVLCFSAGLLTTISMAVHVLMVGTL | EC: 2.5.1.18
Subcellular Location: Membrane
Sequence Length: 150
Sequence Mass (Da): 16501
Location Topology: Multi-pass membrane protein
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A0A1X7FT95 | MRVAAEPIVAPENVPRVPYSESRGLALRSEQTAGASPETPVRFDIKVDVEALLKFGANQPLRPLDPGWAEYLPCAGLPLPGKADAIVPHPRRYDEGPALDSLVLTASIPSGEGALMPGQDYEAGTTLVRTGERITPEAQAILIAAGIRTLRVVKRPRIIVAVASCDLLPIDHAREAWQRPDSNGPYIRSLLQRWGYEVPAVEYLPLVNSWLPEPVSHSTFRQYVQELKRLVASYDLIIGTGMPERSIGGVSGLASCPGFLSPIPVQVAQRPGGLFSFGRSQDRSPPRSELRKHYRADGSAAALQRILYEDQAVLVNLPGFTSNVGVLMHMFVRRIVDELEHVSHPRPYWRTGKLSHEIGRDANTHRVLWGNAIVTSGGQITLCAPYPQPVEGLAALAKANALIAAPSGQGPLCAGTPVHYLSL | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 423
Sequence Mass (Da): 45849
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A0A137NX23 | MFRPIKSSPLNTLRSASRQTNQLVLKRLESTATEAPKPKKGYFFKVLGLTVATSFVYSGIVYQAAHDEEFRKTYLKYAPGGQDTLDFVEELERQTKDPNPERMNQLVKDQLDNATNSIKNLLGMSTEPKEVAPKNILQETSTSAPVAEEQSKKLAASPVPEPTNLTTSIPNTSVSTKNLDQIEKDVAQLQKEITKKTEKVTEKVAEKAQEAKQAVSEKVTETLSHVESAATKFHETVEKKVEQVKNEITYDVANILQSKSGNYTLANPAPKKVAAKSAPKKEEPTKDIVYKIPHHLDQLKSDDSSVDSVYRSIEGFLNSINAAGGARQDIIDQYNKLAARLSTLNNRLVDLKANSQASLESLKKESDVKLQDSLFAERQQNEVARSQLIEDLRSQFSQEKARIEKEFLSHLEDQLSHQASVLERWWRRESKLLVDRERNGRLSKLDDALKQLKLLEHATIDNTSSLETSRQLKQWTLAVESFIDRVEDSARAPFVPEFKLIQSLAANFPVAKAVVGSLDASVSRKGLDTLNDLKDRFKAVREEVSRVSLVEEDSGLFGHTLSYVLSLFMFKKEGLVQGDDVEAVLARTQTYLDRNDLESATREANQLKGWPKKIAVDWIKSAVAKLEYEQAAKVLKAELRLLNLEA | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway.
Subcellular Location: Membrane
Sequence Length: 646
Sequence Mass (Da): 72480
Location Topology: Single-pass membrane protein
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A0A1Y3BCJ6 | MYEELFMFYHKRQCEMCNNVPKDPSLCLICGQLICIRESCCRNGNSFEGVHHSRKCGAGTALYLAVNSSTIILIRGRKACAWGSVYLDEFGEEDRDLKRGKPLFLCNERYRILEQQWLTHSFLNINKKWIYHTNMI | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
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.
Sequence Length: 136
Sequence Mass (Da): 15932
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A0A229T891 | MRTLLGEATVRDAIDAIAAGNPVVVKDDLYDADATLVFAACRATANLVGFTVRHTSGFIRAALTDENCERLNLPRMHRFGDSPYRVTVDLLGAGTGISGADRARTIAALASPDFSAADFSRPGHVVPVSVSPGGVVNNPTPAEAAVDLAVLAGLPPAAALGELVSRENPLHMADQAEASRFAAEHSLPVLALSELVAHRYQASSPTGRAEHMEVGMVANNEHAWETAGVVVRGRQLGRRLGYPTANVDQPAGAALPGDGVYAGIVRLDDGRLRAAAISVGTNPTFDRDERTLEAHLLDFDDDIYGMRVTVTSVRRLRGMTKFNGETELIDAIADDIARTNALVAHLVPSSVQR | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: ATP + riboflavin = ADP + FMN + H(+)
Sequence Length: 353
Sequence Mass (Da): 37325
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A0A6P4YAI1 | MKHSTSVTVVIVAFFVAIILLSVVGNALVCAVVCRNQNLRSATSYFIVNLALSDLMVTVLCMPVTLVNHIFTGWRLGELICKLTSLQGVAVAASAFTLVVIAVDRYRAVMDAMAPKLNGRQSLAILGFIWVLSFAVMVPHALVLGTAERYHGRENDTMVICKEWWQSDGHRQANTLTVFITCYLVPLLIIAILYIRIIIRIGLRQKSFGTEPRTERQRQKQLGYSDKKVTMIRMLILVVVLFALSWLPYHVVILMVDFKHFTSAEIQSMYLYAYPVVHWLGYCNSTMNPILYGYCNRNFRKEFQALLGNFAHDFLTTETPNELPMKNKRDGTCVSSRRTETLRSGTMGKSPTVVTAGGNNKPTVVVMMTTTV | Function: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Subcellular Location: Cell membrane
Sequence Length: 372
Sequence Mass (Da): 41743
Location Topology: Multi-pass membrane protein
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A0A7S3XS70 | MDPKITACISAASIVLTAVYFFGIVPWTKLIALCLCTGYIPWYFDGGPMRTDRSWPAFQKAGFWKAIGRYFPSRIVCPYKLDPKKQHIFACHPHGVGSINHGLTLTDACGFISEVFPVPRLDLSASVIFRIPLWREICLWLGCVDASRSMANKVLRAGFSTLILVGGEQEQVRARPGPGGHAAFLRARKGFCRLALAHGCTLVPVYAWGENELYATSRALLGPRLAVVRALRVALPLFWGRAWCPILPKKHPLTLVFGKPIDVEKVSGEPSKAQIDALHTRYIQALQHLFEETKEEYGKQPTATLKII | EC: 2.3.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 308
Sequence Mass (Da): 34227
Location Topology: Multi-pass membrane protein
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A0A640VUQ5 | MHLALIGYGSIGKRIVAWLADHPVQQLTIMVRSGAIGQTLGDPALAQAAKAAQVTDDIGTLMEGKPDLVVECAGQAVVAAHGPVILTAGLDLVVVSVGALADNDLRQRLAAASEAGRAELILPPGAIGGLDLLSTLALAGDVQVTYRGTKPPQAWRGTPAEDLCDLSYLRQPTTFFDDSARDAARLYPKNANVAATLALAAGSFDRTRVQLIADPDATGNAHSFDVRSPAGSFSMQIESSPSADNAKTSVTTAFSVISEIIRKRAALAE | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.
Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
EC: 1.4.1.21
Catalytic Activity: H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate
Sequence Length: 269
Sequence Mass (Da): 27908
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A0A6C1RPQ3 | MRRMIIVLTLVTVLSGLVLAATFASLSPRIELNRERALQASLAALFSDVDEPQFEQLEIEEMDIYRGEDAEGRLIGYAVAVTASGYNGPISMLLGLTPDLQQIEGLQVVENLETPGLGGRITEEQFREQFIGLDPMQSITTIRHVEPDPAANEVQAISGATISTDAVVDAINRRAEKAIDAIRDAEDR | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 188
Sequence Mass (Da): 20507
Location Topology: Single-pass membrane protein
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A0A2S6UUF2 | MTNTNRDISFLPKGATSFFKKRTVEVLAIILLILSLFLLISLVSFSKNDPSLNNLTDSKVSNWFGLPGAIIADISIQIFGFSIYLLIPILMSWSWRLISHKGVKKFWLKICTLILTLGVFSFNHELLLNFYNKFSLTELSGLVGSLIYKYSIGLISTNINIFYLISSLFFILGCVSFIYTLSLGIEEWKKIGQFFKLLLKKIFYTILWFSRTGEKLAFKPSPKKGSTEISDNTKLKTYRFKFVSKIFSAKFFKKLFFNQSAKFKHKIEPTLSNEIRKTNSISANQESNIEKKGRISKNNQKIIKGKREGIEAQAKLGLDKNIIELPPLHLLSINTNKKRTVSEEALEQNARMLESVLSDFGISGEIIKVRPGPVVTLYELEPARGIKASRVISLADDIARSMSAISARVAVIPGQNVIGIELPNSNRETVYLRELLSSKDSENSGGKLTLALGKDIGGEPIFADLTRMPHLLVAGT | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Translocation stops specifically at Xer-dif sites, where FtsK interacts with the Xer recombinase, allowing activation of chromosome unlinking by recombination. FtsK orienting polar sequences (KOPS) guide the direction of DNA translocation. FtsK can remove proteins from DNA as it translocates, but translocation stops specifically at XerCD-dif site, thereby preventing removal of XerC and XerD from dif.
Subcellular Location: Membrane
Sequence Length: 476
Sequence Mass (Da): 53382
Location Topology: Multi-pass membrane protein
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A0A7S4DL53 | VFGPATGLGTNPSGVLTITPLRRPDGSLILVNRGWTPKSNLSSRSQTNDEVTLCVVSMKGEQKAKFTPDNDEAAGLFFWIDHDFLSQRVSHLAPKEQAGKKLAILEEVKTGQREEWPASRTLEEFEQFHVMPETHFVYAVTWYSLAIFGTVATWLRFRKRPGSSAFPKKTFSPPSST | Function: Probably involved in the biogenesis of the COX complex.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 177
Sequence Mass (Da): 19770
Location Topology: Multi-pass membrane protein
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A0A194SBM7 | MPASVAPLHPPSPIASSSLSTPLSLPSPPSAGTPHPHAMPTPAAHAVHAPRAGLPQGALLAPRPAQAHPAPTQSSAPFFSFTQGVLLGQASMIILAALFLKYVVFEDPDAAKRAREERKRLRAAARGEGGGEEDEAGGKGKRGQKNGKVGKGGGKAKASSRTPPDFPAATLSAAALLGALSYDLSTHPPESLDWLNVLSAQLISSYRALAASHASGGARALIEEALNRRTGGTEEGAEAAQGMVGLDFVEVDEVELGEGFPALSDARRVELDLDYIDTVVLSVSTRVVLNFPRPRFAVLPISLSLTLERFSGTLTVELPPPAPAPAPAPSSSSTEPHHHHHPGHPSVHLSLHPDFELQLATSSLLGSRAKLQDVPKIEQLLVARIRAAIQDRVVWPGRVEVSLPSLSRDKSRHHHHHHHSHSHSEAHVHDAAAVPPLADDLAASPLRTTPLSPLASPLDPSPSTPPSSSSTSPSPHFDRPLRNPLLSRTATSSTTASASGADTPSVDLSGPDGPSIALHPRVRPPPAHLAHESAREAAAAAAMPSPNPSESLPGYFPPMSGRSGLSGAASKGFGAAGAQGMRYRAAAGGAGVGIGLGR | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 598
Sequence Mass (Da): 61809
Location Topology: Single-pass type I membrane protein
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A0A1Z1MML5 | MSIFISYIVFIIFFTVLAISLYFSLQAIKLI | 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. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.
Subcellular Location: Membrane
Sequence Length: 31
Sequence Mass (Da): 3616
Location Topology: Single-pass membrane protein
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A0A067ME71 | MSHAHVQAGPSSTAAHPFNEATYYDDYSGDEDNAGAANSEPEGSDIVDSDESDDFLPPRPAPPPAVEPTNKKRKLSPREDPNRLRQNEPLPEPQILEPSIINAEPLDEFMREVADWILQHTRGRQNIEIEAKVGLLIDTRTRARLHIPVQVETIIAPDYPSVRFEADMSAAQHAHINQLLNNLHANTMKPGYPHARITYAHTRQLDSFYPMPGGDGSNVRVTTDEKTGEVKACVNKIRVAHLNVYSPKRRVDWRISISAEMPAPRPSGPPTHTRRKDRITYTHQAFQVDLTQVKPSQANSSQPPSVLHELELEFRDPHELLRAAAMRENDSTFDELVRVFINNTRILVRNA | Function: First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
Catalytic Activity: a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate
EC: 3.6.1.74
Subcellular Location: Nucleus
Sequence Length: 351
Sequence Mass (Da): 39517
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A0A1Y2ELL2 | MNSATSSPLYSSMPAPSLPRYRPRPARTVRRALLFAAVFAGGYASHGWLRRSSSPTQGDFSRPSTPIRLHHLNAPEKNDRRPLFSPQDCPLTVIFTEDEYAADCLIMDSDQFSTERLVDRESQRRVRPWQSQAILAWESAPNRPLLEEHHRLIAEGRRHETFDFELGYRLTSDVPQVYAYSYMQFERPPVLWELKRQDKLASAFMSNCEAKNARNIILDELIRLLPGQIDSFGACSHNADVVQELQHMGLLDGMEKTDWNIKVAATSAYKFAFAMENSNELDYVTEKYFQALEHGSIPLVLGAPNFNDFLPTPNAAINIADYLPPSYSASSTSNSTAPTELTAEAKEGLARLAERLRYLGLLRGEEWAKPSWIPRRSS | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 378
Sequence Mass (Da): 42798
Location Topology: Single-pass type II membrane protein
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A0A8H4TVB6 | MSTTISVTAPIPLSAKAQKKKALSKQYGGIHAGSWVDFLPKSWIPYVQLSRLSPPVGLILIYFPHLFGVIHAASIQSSSMTEMLYVSGILVVGSFFCNNGSHAWNDLVDAPIDAQIERTKMRPIPRGAISRQAAFVFALSQAILAAGCLLPLGFGTALATIPTIIATLYYPFAKRHTHFAQVVLGFCLTWGVMVGSSAMGVQAPWRHESSVSLLLASNLWVILFDTVYAHQDLEDDLRVGVKSLAVLCNGHARPLLWTLFAGKCACLYWCGVSGQLGLPYFIIALGGCAVSVGSMVALVDLKDPESCWGWFATGFWFTALSIVAGLFANYLFA | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate.
Catalytic Activity: 4-hydroxybenzoate + an all-trans-polyprenyl diphosphate = a 4-hydroxy-3-all-trans-polyprenylbenzoate + diphosphate
EC: 2.5.1.39
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 333
Sequence Mass (Da): 35965
Location Topology: Multi-pass membrane protein
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A0A151UDM8 | GRFEILCLSGSYLVADSGGPRNRIGGLTVSLASPDGRVICGGVGGVLIAARVLFR | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular Location: Nucleus
Sequence Length: 55
Domain: The PPC domain mediates interactions between AHL proteins.
Sequence Mass (Da): 5575
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A0A7Y6FHI4 | MWEDEAPRGSSALARLAHEGVSLWLDGVGRRSLADGTLTRWAAHAPVNGVLLSLGVLAHEVRAGHAGPSRERGAGGPGGRPADDAVQALYYAGARRACDALWTRFARTRGAEGRVTVELDPRVADDARATVDRARAAAREVNRPSLLVGVSATAAGLTAISDCVAEGIGVNARHITSPARYAEVAEACFEGLERAVALGRPVAGYHAVATFEAARMEAAVDRFLDSAGGDGAPLAGRTAQALARAAYQLYDGQLGSARWRRLRSFGASPQRLVWAAGDAPGSALAVRQVEDLVAWSTVHVLPAPTLDALTRSGRLRGDTLSGESGAAQLVLSGLRRAGVDIERTGAELARTLRERGLESRLEAAAAVRDCWDATGGDRLSARPAEDAGRRVRRPDRGAGPGVR | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
EC: 2.2.1.2
Subcellular Location: Cytoplasm
Sequence Length: 403
Sequence Mass (Da): 42212
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A0A6C0X6A6 | MELKFFYIFSILALLSAGCVIIAKNPIHSILFLVFVFFFVSGLLILLNVEFLAMLLIIVYVGAVAVLFLFVIMMLNVKIYSTYENISRYLPIGFVLSLVFLFEFYLIIKKDLIAYDLLGFDLLNNLVGWLGTIVFTSNTTAIGTILYTYYSFYFILCGYILLISMIGAIILTLFRRGDLRRQEVYKQVKTNFRNSVNFSKR | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion membrane
Sequence Length: 201
Sequence Mass (Da): 23175
Location Topology: Multi-pass membrane protein
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A0A6P4Z1J1 | MARERHVAPAERPQAYSDAIFSIVATIMIVPLSGEAVSEIAENENLLAGLGEIWFKLLVYAISFGLVSSTWDMHAWVFRMIEKVNETIVLLNLGVLMVATFLPYAFLMFAEHPREQLAVLLFSGCIILQGIFMLAILWHAYSRPNLLKTELVQKGEEEMKFQRTRATVKLLIRPIIVIIAIPVSYGSIEVAWALLVLMTLKPIIFIAVDAIMTCVRGNVQAGTKLLKLSRLYSETSDVIRTNAYSDGVYAIVATLIILDICVNNVPHTGLVDIHGTLAEALSRDANVFLSYSGTFVTICLLWYLHHSIFYHIQAQNSLLLNFNKLALMFAGYLPIVFKLTGEFGGHLVHNDNSSVAVQLNSGTVFLASIWLLVIWITAWCKKSELLQPSAHDVRDCVFMCLNLLIYPIVSLVIFCVCFVVPVSSAVINGVQIGLILVFILLKLLRNWTQRFVKAEEPRKSPEIDEEVANVKTEPEEPSKEDQEGIDNPVEIESTSL | Catalytic Activity: H(+)(in) = H(+)(out)
Subcellular Location: Membrane
Sequence Length: 496
Sequence Mass (Da): 55392
Location Topology: Multi-pass membrane protein
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A0A6I7NYP6 | MTTASSPRARGPVRRVLDGLYLASGILGACFILGIAGLITAKVVGRLLGRNIPGSDDLTAWFVAASAFLALAYTFRHGSHIRVTLLVQRFTGRWRRGFELASLVVATLAVGGLAAGLVDLVLDSWRWNDIAQGLLRVPMWIPQSATALGAVILFIALVDDLVTTLRGGEASYLKGDGAADRFDGH | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 185
Sequence Mass (Da): 19672
Location Topology: Multi-pass membrane protein
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A0A0F7ZSB2 | MQATEAVAYVHSKRILHCDIRHDNLLLDANLELKLADFQGQHFSTNGEILLDALSVEFTKSYLPRKPADHASVRTDLFALGSTIYFIMMGYEVFPDLDKFEDEDEIGCRFRSGEFPTDPHVCAAITAKCWKQLYSSAWQALSDLEEVQAAIARGETPDFVAKDVLPLPSGDAPSVEKKVRSRL | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 183
Sequence Mass (Da): 20506
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R4YKK8 | MPHSSYSFGLYIGFFCAYLIVGHLLSNFAFQSQIVPIWLPAGIALVGCYLWWWRFIPAVFIASFAFNYSVQTSIDDITLSTEQGIGLSLISMGASLQAFVGSALLRYWLGHPLRQASNIKILYFIFVVGIFVNLISSSIGTFSLTVFSPAYSMKNYWNNFLYWWLGDSLGVLLVAPFLLSFFSTKESEINLKRSRVLIVSTSSFLFLSILVLTGFFIDFSNENTKKSTVREVRSIENGLYRELNNSTVQLQNLASYIQNTDSISRIDFAQVVSKLTDNQPTIAAMSWNPVILQEEKIKHQVELKNIYDKDVIIRGESLLSSDPVVYVRLIFPEESNDKAIGFNVFSNQDRKKTLIDAEMNFQAKATPIIQLVQSKYNKPAYLMFFPIFKGNKNLRGYVAGVFLAEDMILKALDFSETKRFNYELYEAGKDHWFSANNDGGVLKGSGDAEKLEFKLSGQIWHLYLQANTEYLSQQKSQSYLLLFFLEFVIVAFIMLFILMVNSRQIYLNEQVAEKTQSLNRAVEDANLANSAKSRFLANMSHEIRTPMNAVIGFSRLAKESGDLSVVQDYLEKIEISSDFLLNIVDDILDISKIEADKLVLSHENFDIHQSLHRLNSLFYSQAESKGLTWSLINNIPKTLMFKGDQVRLDQVLVNLCSNALKFTQSGSINIVADVNIINKNKNQIIVRVQDSGIGISDGNKDKVFSAFTQADESTSRQFGGTGLGLALSKELSRLMVGDISIVDNKGGGTEFIFQCLMDTADAYFDFQKIVKDQLDIIEEKENSNTTILSDSKGSLQQGAVQSSEHEVMPIAAKHLLVAEDNEINRLVIEAILENEGITADIVNNGQLAVDKIQERAYDAVLMDCQMPVMDGYTATAAIRSIPGYENIPIFALTADATTESKVRAKKVGFTGHLSKPIRVEDLMNALNHM | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 929
Sequence Mass (Da): 104195
Location Topology: Multi-pass membrane protein
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A0A851P773 | RSPQLLLCGHRLCAGCLRTMVALGGTASPLRLRCPFCRRQSPVPGGDAHRPRDGSEGPEPLRCHERGRERGPPEVLLSPSVLQPWAESGDDCLVLTILEVPAAVAPPEGLGGLRVVRLQHPRRSPAPKSRARGWRALLGTLCLLCCGSLPLGTYLLLARHHGLGLALLCLLPAALLLCASCSLCQCLC | 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: Cytoplasm
Sequence Length: 188
Sequence Mass (Da): 20037
Location Topology: Multi-pass membrane protein
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A0A2A5Y227 | NIRKKGEDLKENQIVFRKGRQIRTVDIAQLLSIGQKKIKVYKQVTVGVLSTGSEINQTKKKQNHLIFDANKLTLISMLKKIGCNTVDLGTIKDDFQDTKKKILNNIPNCDLLISSGGVSDSDTDMIGKVLISHGKINFWKLAIKPGRPFAFGEIKKTPFIGLPGNPVATIVTFLMLVVDYIKVLSGNREFPDRSRYISSGFSMKKKLNRREWIRGSIINKGKKQLLEKYKTTGSGIISSISQSEGIIEVEENVDYIKKGMKLKFLTFEDILS | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 272
Sequence Mass (Da): 30567
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A0A6P4YWJ6 | MWTTPYGLQLQFDWRADGDNSRGMKLYIHLKDKLAVKKKKRWSQIMYMSYILDYAAYYKPLGMESEVIKNEHIRPGIGDSQDNSLRLHAEKPWRGTTGGEQEITIELGETAVSVTGIILQAGVKGERVEKIKVNEGEEIEVPWSTTPPSTPHANSTVTCLLEPSILTKELTVTLLDWTGKDDTPPQQPCLRMEILGHIDASNKPLGMENGDIKDKQIKATPKCCEDNSLRLGATKPWKGNIASSNSEQKISIDLKEKSLVTGIILQAAGENEGRVTKIRVANQVDDDIDRDTYILATDADVKFTPKSANKLLDRAQWDTDVGAVCGRTHCLGNGAMFWLQLFDYAVGHWFQKAANSTFGTVLCCPGCFSVYRCSAIRKCVSTYATKAEKAEDFLMKDMGEDRWLCTLMIERGYRLVYTSIAENSTFVPVSFNDFFNQRRRWGPSTIANQVELMRKWCKVVRNPHVSHLFLLYQTLLFLSFLIGPATAILIAAGGLDFYVSGSFPLEATIAIMSILTFMFGYVCLKCKQETQLKWAKALGAMFGVVMIMTTVALVEKIVITIRTITGSSEGVSPVEVLTQLDTYYFIATIGMFLVAGLIHFRESYCLLHGVLYFFALPTTFIFLNIYGICNITDKSWGTREGKTTDGVKESNKNLFDTIGQKFRNVLGNVQESGGGASFDTEDGRAQNVAAGRNGEATHGRAENSPLLTIKEEKDPGQEESIGGANADTEDGRAQKAADTRNDGAIRRRKNTQMVDPGIKIQNWLQEVVFNGDEYLTVRLSLVLQIMTNRFGTYVVLPHAL | Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP
EC: 2.4.1.16
Subcellular Location: Membrane
Sequence Length: 800
Sequence Mass (Da): 89084
Location Topology: Multi-pass membrane protein
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R6P5U4 | MSEIVSAYLPEFIITIFIVINLIASLFFSTYLYKLSKWVTLLGIVLAIASTFFLQIEPEVFAFNNTFLTNIYTVFYKILILISGFFLTLLSRNMIREKRDRAFEYFSVFLSGILFAMCTVSAVDFISLFVSLEALGLSCYLLLALNKNPNAKQLTFGYLVQGAVVSSLFLMGLSLIYGMCAHFDFEQISLYFANLSSVMGQPQVLLTFALILMMCTFLFKLGLVPFSSWLPDTFEGASYPIGAYMSSIPVLACFGIFSRILMIFLNYTFTMKIVLACIAVVTIIFGSLSAIRQESLKRLMAYSMSVQSGIMLLGMCVFSVYSLSSVLFYLFCYVFANIGAWSAIILLYNSAKLENLNDLKGIIYHRPYYVIAFTVVLIALAGLAPTCGFVAKMYIFSAVARSGFIFLPFLLIALVSSVIMIYGYWRIIRAMFRRIETKIEVDNQVISSKFILYACAFATVGICFLADKIIQLCQLAAYYM | 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: 480
Sequence Mass (Da): 53959
Location Topology: Multi-pass membrane protein
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A0A3B5M813 | SYIGLWPFLLTDNRSMFNPFSFGLQCMEMERFVDEADVVIVGGGPAGLSAAIRLKQLANEQEKELRVCLHSVGWPLDRHTYGGSFLYHLNEGEPLVALGFVVSAFTSCVYEN | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
EC: 1.5.5.1
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Length: 112
Sequence Mass (Da): 12475
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A0A8H4XJT4 | MHSYTFTELASGGDLMSLLFRHGTVKEFDARYILRQVVHGLCYLHEKGIVHRDLKPENILLAYSPKIAYQRVMLSDFGFSAVPRRSRMTTNVGTSIYQAPEFTISGQTHTAAVDIWSLGVIALLLVSDSHGPELNRMDQEEIGEYLCQLFPSLPRKPSTNGIDFVWSCLQTNPSDRPTAQETGKHAWLCTPEKHLQFFKLLENRMMSSWEPQDKLKPMPWELPNIVKTSPPTSGSSSQYFTASIETPVRTGRSVANKESDKAHESAEKKSDGHGEKATSPLMAPPPQPTRTKSFSPSGTKQRDQQKQPHSPWHEYIGPNQTAQPEPRSKRKRVPKFKGQDTALLPLPGLDRHLRPPVNYRHRQNILWELERSRSKFLLDPLPILPSTPLEAVEVEAPASPKKRRSTYDVVSRPRGRDRPSVPSIELR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Subcellular Location: Membrane
Sequence Length: 427
Sequence Mass (Da): 48334
Location Topology: Peripheral membrane protein
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A0A3S9P8P4 | MDHKSDEEELNKSFLGSAEQVYTDKINFHRINIKRELNAFEKRKYFNSFDFTFINGNHYIAEKQLLVIDSRKPLLKKVAKITNPVAVVFSATDKEIPPELLKELPELKTLPQFSIEEIDKIGVFITTSVLDKPKLKGLVLVGGKSTRMGSDKAVLDYHGKPQWEYAKELLAPYCDEVFISVAEEAKSYKGTPQITDKFLGLGPMGGILSAFQEDPNSGWLVIACDLPLLSEKSLDHLVTKRNTHKMATSFKSPTLEFPEPLICIWEPKAYGTLLEYLSWGYSCPRKALINSDIELLISEHEEEMTNANTKEEFIEIKNTL | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytoplasm
Sequence Length: 320
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 36322
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A7TL63 | MIYLIISLLAFTQYSLSFSHFIQEPFPIEKYSIDYIPLNHWESEILANSTALNLGKIISLGKDSDCYIPNYSFAALQKIGYFQNYNIEKKDDENLDSFLRDNLNDAIEILRKQFSNNDHEGSSCINYPNGFWTYQFCSGNSINQIHFGDIIKNDEKLNFTLGNTNEEFEKRDHKLLYDTVDGYYISESISNGDICDLTGMPRSTEVHYSCGPSTDKVSIELVQEQKTCNYILKVSVNELCSLDIYKEQNQELSDPHFNSPISSSALTSNSGNIKSMVCVVKHEKPKLGILDVIEDSKPIFLGYGFYFLTDKNENSNNRLIYTGSSENLQKNLGFAVDYLVTEKYIKISNDDNDEFTWNCDIINIKHELIDKISLVLNDDALIGFKNLGLN | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 390
Sequence Mass (Da): 44532
Location Topology: Peripheral membrane protein
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A0A1Y3AY69 | MSEIKAWFMSIPVITRYWFGLSLAIPVLGRFGLLNPYHMFMTKDALWHLELWRPFTGTFYYPIGPGTGFHYLINLYFLYQYSKNLETSEFQGKPADYLFMLIFNWSALVVSICRILFFEYL | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 121
Sequence Mass (Da): 14437
Location Topology: Multi-pass membrane protein
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A0A6C1PEN2 | MTFRQFLLVVEIRTKVISVSTFVLATLYAASRGATISAADTVLLAVAVLCVDMGTTAFNSFYDYLRGVDTPLYTAEPDKVLVHEAVAPGYALIVSVALYALAAVAGIAVAATTVWWIVPVGIGGMLVGFLYNGGPLPLSRTPFGELFAGGFLGTVLFLVVYAVHARALTTDALIASIPSSLMIAAVLTVNNTCDYDGDRAAGRRTLSIVAGRSFGEAIVYASGLIAYAILFAGALATVDALPRLRPGGVVAAAVGLLVTAAFYLRMHRRGYSHATKRPQMVAIIRVVSIYTAVYAAMLVYAAV | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Membrane
Sequence Length: 303
Sequence Mass (Da): 31808
Location Topology: Multi-pass membrane protein
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A7TIM1 | MQFSKVLVIFIALFYQSLAFSISNGKINFPGSGKSAISIDKFDTKINSKGLSHKVTVKDLEEIIEFGFSIPSNSDNAIKSHLLLGFPRDGLETVIEPLVQKKDDKLVYLFNIRLNALSKALLSRAVENQESLEATLLLANEDNKNNNIFGRVFQLTLSPDLEVQYTKPSRFGFKDEIHHIFRSPPKAAPAFIAQVFSLAIAGCVVLLIGTWLSTGVLSNMCIPGGMNSIYFIVMISSIVGFEYIFTNYYLGVSIFETLHAGLYLIIPSLIIGTKFLRNIGKQI | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 283
Sequence Mass (Da): 31394
Location Topology: Multi-pass membrane protein
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A7TNH4 | MNHYSNIKSPGASWSLDTFGPVKPSPNNNYRFMLVMIDNVSRYVIISTHLTKDMNTYTNQIENSIHFIKTQFGRTVQELIMDRGSGFNNSQLKELCDEFGIHRVFTAVQDHSANARAERGIRTIISDARTLLIQARIRLKFWHYAAKAAVNVRN | Function: Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence Length: 154
Sequence Mass (Da): 17675
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A0A0B5HL16 | MREIIYVSKNAVTTGNFKDLMQAGRMDIVCHAVIMTLFTSNKLRDNVKLHLFFYGRPDPPKHLELMPRIDEKFQISKKDIAGLIKRMLYKYKKERKKEVFPGCHVEKLSLVKFINSLKNRGVYVLDKNGDDIRNAEIQENPIFILGDHEGIPKEDLKIIKKTAKKVSLGKTTYFSSQAITILNNELDRREL | Function: Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs.
Catalytic Activity: pseudouridine(54) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylpseudouridine(54) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.257
Subcellular Location: Cytoplasm
Sequence Length: 191
Sequence Mass (Da): 22152
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A0A2T2TFM1 | LVHVTGGGLPGNLQRVIPDGCEAAVDYDAWERPALFSLIQSMGEVPEAGMRRTFNLGIGLVAIVRDAEVEEAVERLEAVGEAPVRIGQVERAGEDSGTVE | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
EC: 6.3.3.1
Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Length: 100
Sequence Mass (Da): 10614
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A0A6P5ACA8 | MFFLLCYFVPIFIMSLVAHHEPRYISPCLVPLVLAYHSKFTWKGGKKLLFVGFVVGNVLGGVLFGVLHQGGVVPSLLHLHNLVHQKQSTETVHITYFHTYIPPGHLLGINGNQTANQNFRMSHKVTNDRVEPQVHLHDLAGAPTTVLFDKLRILYQEKQASNNTHVYIVSPSSLHSIFSKHETDMKIVLQEVFFPHLSMEDPPRVQDIVHTRLDELNTLLEELRLMFGLNLYEVL | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 235
Sequence Mass (Da): 26821
Location Topology: Multi-pass membrane protein
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A0A067N533 | SSHLIKLNTLFQIHDIYLTPGSGPLLALVLEEIVPSVRKHGLLYGICSKGAWTLISCLPRLKFYYIINHYIKYVELLESLESRTDCEKFEHPVCAITDVFHHSATAVLCYVQLQGHTSVVLILALALAPAVLPDHLTSWVPIALDLTVHVFMYYHYYATAGGRRIWWKKHLTTMQITQLVIDIDNLFIVLCADYSYIAATYFPHLPHQGNCYGKENATVIGSTLLTSYLFLFINFTPVHTSPLRRHHKK | 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: 249
Sequence Mass (Da): 28350
Location Topology: Multi-pass membrane protein
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L8HBZ7 | MADETTALWMQAFSWLGLGYVIYRALFVDNGPTFEDDPSPARNHLLRLTTAAFYVPFVIVSAVYVPNVIHIFMTIMVTKGLGEFIECLIPARASKEEGAKKKYKFSRMDRLVQLLGGLQVVLCHFLSELGLSLGLALAFVIILCFFLFKTVQEGHNPLPPNTVRNLAFYLFGWVWIAWTISHCPAIYHTSPYGGSILVMLLLTGWIGDGAAYYVGKNFGRHKAMPNVSPNKSWEGIIAEIVFAVLLCYGFKQMQLSGVTDKHALLATKPIALTSSARLPPYDTIHYIGLALLTSCLGIFGDAIESLIKRMGNIKDSGVFFPGHGGILDRFDAFFVSGPFIYHYLIHVVGAGHL | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 353
Sequence Mass (Da): 39060
Location Topology: Multi-pass membrane protein
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A0A0F7ZQG3 | MRHDTLITVTLLACLTHAVPSIEKRKSDFLVDTAGIGKRDLSNGLVGGFDKREPLPQLGSKLIEGITRIPDAADAPSTAGSKALNAFKRTVGKYAFGQTHVKRARVGEDCNAKGDFVQQSLKTCSERAGLAAQEASKPDSRLLQQFFKNNDQGTASQVSGLYNKIKQECDAVGGGSLNLVCPDDNACGKFDAFANPNAPGGPQIMLCRGFFEISDGPSGGRRCGGLDAGSLMIHEMSHLLGGTSDFGTAYGLAAVQSLSAAQNLQHADTYGLFAHAVALGCSDGDLQTGGAPSGSGNTGAGGDKNSPIGGGQANGVNRGNQGQNALGGDARGAAGNGIPQRTNQDNGGQGRNRAGPGQQVGNNDNGNICKAGNKAGAATKQSTQSLGKGQNGLAGGTSKQLDQSKGVGNTQQQGKSNTKPGKQASQTGKGTVPQNGIKGNKGKTLSGGKNSTAGDDGGSARKGTKQNGSSGKLTGGQSKGGSNAKNKPKNGNAGNVIDSTGGAKTQPGGKKKSTSGQNSAGNAGQGTRAGSSPQGVQSGRGSNEPSADLTPPPLPGSAADGAQSNVGQGQTSFDGSVGPAFGRF | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.39
Catalytic Activity: Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.
Sequence Length: 584
Sequence Mass (Da): 58460
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A0A6P5AQP1 | MGKPSWLNNVTSSTIKKARVYTTKKNRKKVEYNTRVVDNTWEQVCKFNLGDISPFSLDSPESVPEKRPGVVPWRKERLGGSPEWPSDRGTGLCRKEDVNDAPCEDVTSLWSSRNRAVSTSPCSNKENSSLKNSQPLRSKRVSSKKKSLRVQSSNKFDLDHDSDSDFVPSQPKKRKAPTRQKKACSKKGKTLKGKKSKKRNESCTKAPVENGQYFSDFEVHSSAHASNLSGLNHFTSQESMNFGNSENVTNPSYSNFIGDTSPQNDKSSLYLSSHNHNSSYFDELVRHRLDQFVTRDRKANTPLSFTSPFEANSNYETPPSQVQQKSPGAKRMQPVVMLSNISKGELMESSDVVLAEVSPSSSEMSRSPKEACALDVTSSDFVVPESPIEQDSSKQGTDLSPEATVFRTSTPFAEKGKYNLRKQASETKASGTRKRPARGAKESNRDRDTPPPKRHRAKSRNAEDNSQKIRKTRTLRTRQKKSSNSVTPCSVLVPRLSEKDIQRLSSGNKLSRKKQQSGNVRESKNKSKKQNTKKKTPPKKRYTKNKTPPKKRNTKNKTQVQQRQKSSTESFFKTPDSRAVYTPDACEHLSPAGFLAFTPGSRGNKMGTSHRAKSPGSGVKQTPLRGAMGLPSRHGSMMSPLFKKAVQNRVRISPKEKLLLHCDKERILTFQECIPGAMMERCVKIGEGVFGEVFRTRRDDGSSVALKIIPIEGDFPVNDEPQKTFEEILPEIVISRELSELKDGTCNQTGGFIHLHRVCLVQGAWPDHLLAMWDQWHQEKAGGSENDKPDMFPDSQLFVVLEFADGGCDLEHFQFHSLSQAKAVLHQITIALAVAEAALQFEHRDLHWGNVLVRKVEEQSSTHHLAGEEVCVATSGLDVNIIDFTLSRMQKDGQPLYCDLSADPTLFEGKGDYQFDIYREMKKENQDNWKRHHPYTNVLWLHYLADKLLNKKYRAIKKSQRQWQQKFRTFLKQVLACRTVAQVLEDCQLLKEK | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 993
Sequence Mass (Da): 112070
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A0A8R1TKQ5 | MAKQQIYSDFNYLEFEVWQGPVLQVLYAPYNYTRNYDLEMKYWNPETIQLFFYKHWSTSVYIALIYICLIHALQRYQRTRKDWNLRLLLCLWNAALSIFSFIATIRFGEEFYTILTTRPFVHSVCYSISPLQPAAVWAFAFAISKVVELGDTIFLLMPIEVTAPGRWFIMMNFSVHSIMYAYYSITAWGIRLPKLFSMCVTVLQTSQMIVGVLISIVVLKQKLKNAVCQQSMDNLALGFAIYSSFALLFVRYFYVAYMRPKKFLRKKIE | 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: 269
Sequence Mass (Da): 31716
Location Topology: Multi-pass membrane protein
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A0A7S4D5R4 | GGYRPHIVSHWNLSEFLPPACQEYFLLAAGELAYRPREEARRLRAQLRQGRLALSQAATQGQAAPSMAAAAAGTAAVTCEADVAREVERYMKGFVAGRFTKKMLEMTSEIMRYNTGPECFPVLPGSHLKLSNPALEFAKSVCRVFALDPALAQEVQLLRRQLLAHIGAAREFDAAAVWRDPCASFVLPDVTCGFCNLCRDLDLCRDPAVLGEKEDRWRCLGCGHSLDKRGVEARLVAHAEALQARYQLQDLRCAQCRAVADRRLAPTCPCAGAFAGDLRPGDLRA | Function: DNA polymerase II participates in chromosomal DNA replication.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 285
Sequence Mass (Da): 31272
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A0A7S4D863 | RTRGAAAAAAGARRRWDVYFGIDVFGRNTYGGGGMQCDKALEKIAEAGVSAALFAPGWVMQNQMENGGSFTGNDPKEWDRTEEEFVKLSTEFWDKIKSFFEQRGPWISGSAFCTFFSQGVGKHFSIAGEAHEHDTFW | Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
EC: 3.2.1.96
Subcellular Location: Cytoplasm
Sequence Length: 137
Sequence Mass (Da): 15216
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A0A0F7ZW12 | MSITPEAAQPTQPSRAIQDALKSQTLTRDSIIDDSGASNHTFNDLKWFKDIKELPQELSFTSANGGDLVAKAIGTAYIRAKRSDGLVTEMNLGRSVYCPTAPINLLSSGQLRADGAIRDGFKDCIIHKDSKTEMAMIDWINNVAVIRSETPTTRQQIQGNMLLAVSYQVMHERLMHASPEIVLKACEQAGIKIPNREAKEHHCRTCHLAKSALIVSRTPPVRPARPLSLVRIDLIENKPLGHRQFRYTWHAEDAHCGYHWVRFLRHKDELFQATKDFDAYIQRTTGYQVQEYGMDNDVSFNWTTELIPWARANGISLKPTVPGTPRQNGLTERAGSKITQLARCIMIHSKLPEFLWPYAQESVVKVLNLLPCKSNQGLSPHEVFASFLRVNEELHKPYIRHLRTFGCVAYVHIKKERRVQARKMAPRAEEGKLVGWEGIHGKIYHIYVPARNRIVRACDVRFYEKLLQEPQKSASAEEVDTIEYEATLLDEVQEEEAGATIVERISDSLSTIEPGGGTTDKGPSIEETQDHHLPTPEITQELDESHDSSVKLVAHRRITTIAEMREGLEFPNAHRFRDEAVHFEDPPSATASANTSGHKRKSSSDTTSDNASGSKRWRSNSQKSKLVQEFNDQLPIGKAKPSLYTPGEDPWENRIYSCLVVSPAGRAISDFKTIKKLLESMRDAIRAHQSLYVTGNILHRDISSNNIIIADAKEPGAFKGMLIDLDLAKVRDSGPSGARHQTGTMQFMAVEVLRKADHTYRHDLESFFYVLLWSNGFDGEEKPPKESDLRNWEIGSFRDIAKAKEGDMTMNGLERIMSEFPERLDIVKPLCLMIRSIMFGDTARLSFGTPAGDPD | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 855
Sequence Mass (Da): 96234
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A0A146KBF7 | AKMTDLLIPTLIGVDIGCGVSTVKIPFKIQKSHQLFEQFDAFLRAKVPSGPDMRDKAIPMQLQQKIFSKTNLSQKMKFPEFQKLLHQKQEHFRDDFGTAMGTMGGGNHFIEVNEDS | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.8
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+)
Sequence Length: 116
Sequence Mass (Da): 13125
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A0A6I7P2P6 | MTLLVVGNAAVDRFFGLRALPRPGETVLAKAKPWEPGGKGLNQAVMARRAGAEVRFAATVGDDAMGRELRAFLAVEGLGLELVRTVPLPTDESAVFVDRTGANMIVSTADAMHAFPAELVDEAIDGLGVGGRVLIQGNPRDEITERLVRRAHGRGLWIAFNPSPVAACHPALLPLVDLVVVNEIEAASLDVGAVAMVLVSLGAAGARLRVGTVEIVVPAPPVVAVDTTGAGDVLCGVFVAGLAKGVEPAAALAVAVRAASLKCTRHGTTGGFPAAWELRELGG | 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: 283
Sequence Mass (Da): 29078
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A0A5B8UBK9 | MGAHVRGRAHRGRDVQGLRRPRRHGPLRGRGQGRPGPARRVRARHHEHVPGLGSPPALRRPAWRGRVRGLGEQLTETLRQATGHDRLVLLCSFQKEESVILDELAAVAGGLDGIRVVTIDTGVLFAETLATWKRFEDHFGVRIEVQDAASPSEPWTGPEHCCTPLKVAGLERALGDADAWVTGVRREQAATRADAELVEVDPRRGIAKYNPLAFWTEKDIWNRILERGLPYHPLHDQGYASIGCACCTQPGDGREGRWAGTDKTECGLHVV | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate.
Function: Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
EC: 1.8.4.10
Subcellular Location: Cytoplasm
Catalytic Activity: [thioredoxin]-disulfide + AMP + 2 H(+) + sulfite = [thioredoxin]-dithiol + adenosine 5'-phosphosulfate
Sequence Length: 271
Sequence Mass (Da): 29938
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A0A6J0Y2X1 | MSPQGDGNLSEMPLQEFVLEGFAGGLQAQALLFTLFLALYVVAVLGNLTMIVLITLDARLHSPMYFFLKNLSFLDLCYSSVIAPKALADFLSSLSSKFITFEGCTIQFFFFSLLGTTEAFLLAVMAYDRFVAICSPLRYPISMRPSVCARLVLGSYCGGCLNSILQTSFTFSLPFCSSKHINHFFCDVPPLLKLACADTTINELVMFAICGLIIVGTTLVVLMHLHSH | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 228
Sequence Mass (Da): 25030
Location Topology: Multi-pass membrane protein
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A0A1Y3APD2 | MRDRQALNLRTPLMLWNVILAIFSIIGTYRCLPEFIHIIRTEGIQSSYTKSTYYADFRLSLWYLFFTVSKAFELIDTLFIVLRKSKLIPLHWIHHILTLNFSWFVFTDVPATARWMVCMNFFVHSLMYTYYALKALKFNIPK | 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: 142
Sequence Mass (Da): 17029
Location Topology: Multi-pass membrane protein
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A3VLN7 | MLLLLMAFHVTADVVSRSFFNAPIAATLEFGTYYYMVAASFLALGYAQMRDHNVSVDILVHGAGSRVRMIVECVALIITLFYGVAFTWASTLSALEKTRVGAYTLTQFFNLATWPSNWILVVAGVVFCLVLLAQILRLFVALSRGEDRSVAQLIGQNRESV | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 161
Sequence Mass (Da): 17775
Location Topology: Multi-pass membrane protein
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A0A137P628 | MSSVRSYPVFTLFDSFWKTIFGTSANDFVYKQGETFLSNPEQVLALCIGYLVVIFGGQKLMKSYKPIQFTILFQIHNVFLTFVSGLLLALFAEELYYINREIGPLKTLCSAQAYTSRMDLFYYLNYLTKYYEFIDTFFLVMKKKDLQFLHWYHHSMTAALCYINITSRTSATWVVVTLNLFVHVFMYYYYFLTTLNVRVWWKKYITVMQITQFVIDLVVVFSGTYSFFAFNYYPNLPNFGHCSTTPFSSLFSCGLLTSYLLLFIQFFFKSYSKKASVPKEKKAQ | 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: 284
Sequence Mass (Da): 33433
Location Topology: Multi-pass membrane protein
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A0A151UD11 | MASKTGKRFTISLFLFYSIFCIQIEFIFETQNINVFAGAIIVVMGVSGAGKSTIGRRLEKEMKYKYLDADDFHSESNKEKMRMGTPLTDEDRKPWLESLRDTIKEYLNNKKGLILGCSALKIEYREMLRSAAEGKHYMPASLLQSQLDLLKIDDAEGVLRVDATLRPQAIVTTILNMHQFQGYL | Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 184
Sequence Mass (Da): 20983
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A0A7S0HH04 | MALAVLSVVIRSLVSFFPYSGQGNIDGRVREDGTKMYGDYEAQRHWMEITLHLPAQDWYRETKDNDLMYWGLDYPPLTAWHSKLCGMVMHLFDPPSVELHKSRGYETASSKMRMRMIVMLFDLLVFYTGVFSATRTLYKQSVSAKKVCMLLCLFSPGLILIDHGHFQFNSICLGLTAW | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 178
Sequence Mass (Da): 20502
Location Topology: Multi-pass membrane protein
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A0A137NVF6 | MSNQGWTVEDAQPANFNNKNKGKKQLKNKLNSKPKAFDKSKPSDNKLKGKKSKMIQLFSGNSDDEEEELVRRKSEVIKFNKDQLLNVANYDTINGDEDNRTTKNNTGSTLTKSQKRKQNKKNKKNAVSDEEWMKLSTSAPPPMPKMKNILGKEINWESVESNELVDDGLEDGLEGFLGLEVADGIDCNWEEIDGAGKMLKFTSVGNIKKRKLDDDLDDTYALPLGEDEMKGFIHLDDFKEDGVENSDEEDDDEEDDKDDENDEDIEDEEEKDEEEEEIEAEVEDEEEVEDEEDDDEEVPTLVDIPEEELEEIKDKLGDWIHYELHDNIMKSLYESKFFTPTQVQKDTLLKSLQQKRDIVASAETGSGKTLAFGLPILQRISEVDLTDAESKKVYGLILAPTRELALQITQHLKQMGKYIPKFYCGTVVGGLSAQKQNRVLRKVPHILVATPGRLWDLVSTNSDYLKLIRQVEFLVFDEADRMLQTGRFKEVQQLLPVLDKHIDNMPKPASRQTFIFSATLPPSLKAEPTKSKKDKKPKEVGIQELLKSINFRDSKPFYLNLTKEDQGLASKLIESRIDCLLADKFLYLYYILLRYPGRTICFVNSIDTIRRLTPQLELLGIKAYPLHAEMQQKQRLKNVDRFKTLDNVVLVASDVAARGLDIPLVDHVIHYQLPRTVDLYIHRSGRTARGSQSGISIMLTCPEELKSYTMICRHLEKERVDHFNIDNLLVKKLKPRVALAQEIDKLMHSGRKEKANRNWIEQQAEKLDIILDEDFIGKVKKSEDHQEVQAITQRKIHKLKEQLNRMLNDKIIQVGHSTKYLTKFYGSNSDLLQNLKQQKTEAFDVNEKRSAITDAKKRKLKK | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 862
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): 98983
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A0A6I7P9Y0 | MEPNELMHSIHQDRCPYLPNRRWLASAFAAGRIPAAAYESLINAGWRRSGSLFYRNSCPGCSLCIPIRTHVQQFRPSRSQRRVRRTNSDLLVTVHEPEPDTDLFALWVDYQRRRHGDDLPEDEAWSAFARFLCYSPVPSLVMRYRLQGRLVGAGWIDLLPNGVSSVYFVFDPCHASRSLGVYSALREIEFAAQLDKRWLYLGFFVPGCSAMSYKARYHPYDLLIDGQWRAWRR | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-aspartyl-[protein] = H(+) + N-terminal L-leucyl-L-aspartyl-[protein] + tRNA(Leu)
EC: 2.3.2.29
Subcellular Location: Cytoplasm
Sequence Length: 233
Sequence Mass (Da): 27062
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A0A1V4YX11 | MSVTPRDNAAFEAGIKLGALYHQFVGTPVSMSTVESLERAIAASIGVQPYVRSITVHIDRKMIEDSLSSFGYTELKGPMLKVDGVIRYDRYETHVGIQYKDGYPLMFIKDIREV | Pathway: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin biosynthesis.
Function: Catalyzes the conversion of 7,8-dihydroneopterin (H2Neo) to 6-hydroxymethyl-7,8-dihydropterin (6-HMD).
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 114
Sequence Mass (Da): 12788
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A0A7S3Y2V7 | MESATGSVSADKLVPDGEIGAGNETLPSNLPPPPLQASASPPPQNGASTQEENNDNDSRASNSGTEPDLSTPKKGHVPARSSLSDVEFQIPGRAIYNIQDLQHFSKSRTYSELMMFIRICNEKVKGLKVSDIQEHSEIIGGLLGLLDTLEGWVGEHPPLQQPMRFGNKAFRAWHAQLVEESPALVRALLPAKVAGASLELSPYLCTSFGNETRIDYGTGHETNFVVFLCCLFKLKVLPRADLPAAVLRVFARYLRLCHRLQAAYVMEPAGSHGVWGLDDYHCLPFLWGAAQLVGHPSIEPSSIHDDSIIRENKDEYLYLSGIDFVKQLKKGAPFAESSPMLNDISAIPQWRKVNTGMFRLYEGEVLGKFPVIQHFLFGNILPASWVPAAVPGFELPFPPESPGSSMPGSPGSPFLAHPGLAPLFRGRSASSMSAHSGDEMPPLGPMAHAPWAPEPEPLLPSPGGSVRASRTNSFSLDDVHHQAHAFRTGV | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 490
Sequence Mass (Da): 53137
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A0A067MW90 | MSNIRQSTRPPRSGNNQNRAQDTPEVRMSKALSYILRHGAQKEGLAIRADGYIKVDDLFKRPKLRGLDFPTLEKLVKNNEKQRFQLLFESSATSSSAPATAALAPGVNTSGTWWIRANQGHTLKVEDLDLTEVLDASQLPVAVHGTTRQAWESISRQGLSKMARNHIHLATGRPGDPGVKSMRASSTVLIFIDVPKAVKDGFKFFISANGVVLTEGNKDGFIPPQYFKSVESRDGTAIV | Function: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
EC: 2.7.1.160
Catalytic Activity: 2'-phospho-[ligated tRNA] + NAD(+) = ADP-alpha-D-ribose 1'',2''-cyclic phosphate + mature tRNA + nicotinamide
Sequence Length: 239
Sequence Mass (Da): 26241
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A0A0B4XKS0 | MAGWPARELRMFHIQTLNQIAVCGLERFPRERYEVASEFSQPDAILLRSHRLGAEALHPGLKAVARAGAGVNNITVPAFTAAGVPVFNTPGANANAVKELVLAALLLGSRGILPGIDWVRSLTALDEQAMHATIEAEKKRFRGQELTGRTLGVVGLGAIGSRVAEMALGLGMQVIGFDPALSVDAAWRLPHQVRRMESLPALMARADYVTLHLPLLESTRHLLGREAFSQARPGMRLLNFARDGIVDDAAALEALRAGRLAAYLTDFPSPALMREPGVVALPHLGASTGESEENCARMAADQLIDFLEHGNIVNAVNFPTLVLERSGGHRLAVSNRNVPKMLGQLLSVLADANLNVLDMLNRSREDIAYNLLDLETAPDATVLTRLAAIEGVVGVRRLPPV | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
EC: 1.1.1.399
Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Length: 401
Sequence Mass (Da): 43149
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F2IHY8 | MPVFQFKHFQIQQKHAALKVGTDSMILGSLCGWENPKRLLDIGTGTGVLALMCAQRFPFQEIIGLEISEEAIIDAQINAQNNPFDTKITIVNQAIQDYKPKEKFDAIISNPPFFENSSKNPNDQKSLARHTESLSFSELLQSITRLLTAEGKAWIIIPFESTENIIQLANANELFIADLITLFGKPKKPTRTILCLIKQISEIQESSLCIRTESGSYTEEYKILTKEFHDREL | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
EC: 2.1.1.223
Subcellular Location: Cytoplasm
Sequence Length: 233
Sequence Mass (Da): 26346
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A0A8R1TLS4 | MAQTIEPSRSDVKQDYSEQSLNSTRIYSQPFCLYCERVIIAAHKKSLRFEVINVDNLEDIPDWFYSKNPEGVVPVLEHNGKLVNGSQMIIEYLDDVYPEISIVSKEPLLRAKQRYDAFKLESVCNAIRKISYSKRLTGNIDALAMELAKAEELLQSSFYSGETLGLPDIVLFPFIQRLFMIRKIIKDNFLDKVFPIHFSKLENWFTRMRTLPEVIIN | 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: 217
Sequence Mass (Da): 25204
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A0A651EFS7 | MARIALFASGTASNAQCILEHFGYLQKAPFPGGAVSDPSIRSCEIACTISDRSSSGIHQLAASAGLPGFLVSYRSGREHAEQRIRAVLAEQKVDLLVLAGYMRLLGAELVDTYAGRILNIHPSLLPEFPGMHAIERSFHSGNARAGITIHLVDAGMDTGPVIAQASFDRTTIASIVDFEKQIHRLEHILYPKVVEQVAKYIDNGQWPGANLYASGLRESLPDCYRLEDTHT | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
EC: 2.1.2.2
Catalytic Activity: (6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide
Sequence Length: 231
Sequence Mass (Da): 25113
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A0A0F7ZXI4 | MSAKSITDVYPIDGLCAVNVDFGGKEYRICWSGNWRNLPDLSTFPDLTGATITEIAQSLAMRQVWTQSEVIAHGADSHIRELRTCSDDFPICKVANDWRQRQAIRDEFFILRRFSELDANIVVPRTHPDPLRDDEGIFGFRMERLQKIPWGHSLSCLPALRKAVQQLHQARVIHFDLSPNNCMVNKYGNLIIIDFGRGGLIDNPVPLHKQKGPKRNSEMRYSIEQDLEGIERLKGTLNTWQQENRRVAKYEVAIWTKEALQRSPSLLLNPLHSQRDGGKTSRGNLHRGSFQYI | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 293
Sequence Mass (Da): 33576
|
A0A146KI99 | MLQYIIYSLAEQISVSVIVLHYKHEFGVEQTINSISSQNLENIELLVVDDGSTDKSLDNIYKLSQKFKNKKIIPNKNRIGFAKARVQAINLAQGSYVLFMYSGSVFATQNSLRLMFETGINNQNAQIVHGKANNNVNAPLIFDLVTPPQSQIQTIKNFLTEGKLFNIALIKDIAKNYQPEKMLECPDDLGFMTFAANAVRSYIGIDQVVFIPFFQNNWNKQSFNYQEELLLMTKSVTRSINAESGLAKHFFSQLKSNIQIDKLTPEQQKIICSNYQLIDSRGKTYNLVELADLRQCNIEDGLEDELEFQRLLNKQIEEERLKNQNTANQKPVKFDAKQVVQQEMLKQAKSKLTVLILPAQQQKMDQSIQNIQKFAQVDFRIMDQPNKIKAERVKDIQSEYLIIVDAGEEVDYQMLLDEIQFGHPDLILFKKGDGQTIYSYNKKEQMLSVKGKAFATTLINQEYELTAKSEELILKDLQTNTKLIASIEINLKQ | Function: Dolichyl-phosphate beta-glucosyltransferase involved in the glycosylation of glycoproteins through the synthesis of dolichyl beta-D-glucosyl phosphate which serves as a sugar donor for transfer of three glucose residues to the Man-9-GlcNAc-2-PP-dolichol precursor to N-glycans.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 493
Sequence Mass (Da): 56494
Location Topology: Single-pass type II membrane protein
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E5D487 | QHFIWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLHGTQISYSPATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGLVQWFPLFTGLTLNNKYLKTQFMTMFVGVNLTFFPQHFLGLSGMPRRYSDYPDAFLLWNVVSSIGSLISLVAVIFMLFTLWEAFIVQRKSLGTLSMVTSIEWLQKLPPAEHSYSELPILTGHF | 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: 284
Sequence Mass (Da): 31798
Location Topology: Multi-pass membrane protein
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A0A1R1YDE9 | MSDELVEQKPLADSGPIEQPTNEEIDSLIKVVKTQGLTDDIIDGVYLGILTISLILILFVTAIGPSLADFIPALQPLFSFIANVWPFITNMSENLKTLPQNYSIFIQSLPKSFLDFQSIYFNLIAYMSNCLTTLPYKRLILIFSWGAYVWDAYLDVRQRDMLHGVNRPIPIRSIVTRKAFLEANSYGLDKSSLKLTQSLIDQIKTTLVLCYDVLPAFWNMTGEFMQTRLGFGPEYEITHSILFFIATSFVNSVTNIPFDLYGTFVVEQKHGFNKQTVSLYITDFIKTLALTASFGSLILSGLLYTISKTGDNFYFYVMLFMMLIQIIGITIFPTFIQPLFNKFTPLEDGELKVKIEELAARLDFPLKKLYVIDGSKRSGHSNAYMYGFFKNKRIVLYDTLIKQTNLEEVCAILAHELGHWKMNHVVKMLVISQIQIFVIFYLFSLVIVQQKLYSDFGFSTMPVFIGFTLYQYLYQPVDSVVTYYFNKLSRKHEFEADAFSCSLGYNEHLKQGLIKIHVENKGNLNPDKLYSAYHYSHPPLVERLDAITSSSNSKKSI | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.84
Catalytic Activity: The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids.
Sequence Length: 557
Sequence Mass (Da): 63734
|
Q158A5 | PPSIFFLLMSSMIESGAGTGWTVYPPLSSNIAHSGASVDLTIFSLHLAGISSILGAINFISTIMNMRPQGMNMEKSTLFSWAVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIGQESGKKETFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWVATYYGVSLGLNPITMWSLGFVFLFTVGGLTGIILANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFSQWFPLITGLTLNEKFMKIQFMIMFLGVNLTFFPQHFLGLSVMPRRYSDYPDSFYLWNMISSMGSMISLMSIFYLMFIIWESLSTKRKNLSPLSLPTSIEWMHKFPPAEHSFSELPMISIKF | 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: 410
Sequence Mass (Da): 45622
Location Topology: Multi-pass membrane protein
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A0A1R1YH33 | MSPSKSKTDSSSSGQKRQKRGKPYPQAQVVHAEGHISVLDANAPSTNYNGLVNFFLLLFGGMMVRLILENYLKYGILVTLPGFNFDSSDYFMSIVILLFLLFNFFFAFFIEKFAAFKAKEIFESSATSNTSEKNSPSKLNKKSSIIDHESAQLSESESSIAVKNSTNNNNSNRSTTSPPVDKKEADAINKRNQIEYEKSFSKVDSAAKFKFKEMVNRDFVTLILQSLNIFFALAVPSFLVFNHVSNPLLGTANMMASVVLSLKLFSYYATNLDLRRAYLYNDDKFNKDLLLETKFSKKDILSINSSCEATVYIGRPISYDIPYPQNIKLSNLIYFMAVPTLCYQPSYPKSSHNIRPSFVAKRLLEIVFLTSLMYIVVHQYAFPTLFNSVTAIESKNQAWVSERVLKLSVAVSLLWLVGFYTFFHSTLNLFAELLNFSDRRFYLDWWNSTDLGTYWRLWNLPIHNFCKRHIMIPLTSPPFNLSPFIGGSITFFISAVLHELVFGIPTKSTRLYSFFGMLLQIPLVSLTQTVSSYRRPNSNIGNALFWISFCIIGQPLLVLLYYYDWIKLNKSFIS | Function: Sterol O-acyltransferase that catalyzes the formation of stery esters.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 574
Sequence Mass (Da): 65524
Location Topology: Multi-pass membrane protein
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A0A2E9QA75 | MRILGLDPGFGITGWGFVSFRGSSLNQPTLHSYGALTTPGGRPLSLRLADLQNQFIELLDRLEPDRVAMERLFFGKNITTAEGVYQARGVLLAAMGQKGIVPIELTPNQIKQSITGSGKARKPEMMRMVQMLLNIDEPIRPDDAADALGCAIVASAFSHLEYEQLQQTQSKHDSGEDSPTSELQGEVDMGTGIGFEADAEYLRSKTSPGPARSPSGEAPDEVMDASALLEGEIPGQLGAGSEIRFLRHGKGKATASKGAKSAKKEPRPKATSPGKAPRKDLKSAGKAGMKDRATGRKKSDGEGED | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
EC: 3.1.21.10
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Subcellular Location: Cytoplasm
Sequence Length: 305
Sequence Mass (Da): 32518
|
A0A0G1FL78 | MKKIVAFNWKENPDNLSRVGGIVRAVLRSVPKKRLTIVIIPPALFIEKVRKLIGVRKEEVFLGVQNVSHLEKGAFTGEFSAAMLGSLKVTHAIVGHSERRYLFGETDKIISLKIKSCLKNKIKPILCVGEKKKMPQEKSWSFIRRQLETDLPKIPDPKLRTLIVAYEPVWSIGGNRKVNPSHAAYMIDKIKSFLYSVYGRRYSVLYGGSVGCKNIKNFLKYHQIDGFLVGSASLRPAEIRCLLKLI | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 246
Sequence Mass (Da): 27834
|
A0A963P000 | MTALAVISIVLICQVVLRYVFHAALPWPEELAQFLLVLLTLLGGYRALEMDMHIRLQVLDDFRWPRLVMLLRLAGYAASAAFMLYVAYGGWDLTMRSMHTPSTALRMPMGVVYATLPIAFGLMTILLVVIMVRLVRGRDVVLDRPE | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 146
Sequence Mass (Da): 16506
Location Topology: Multi-pass membrane protein
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A0A151UFV6 | LLLQMNPVHKKIPVLIHNGKPVCESLIAVQYIEEVWNDRNPLLSSDPYQRAQARFWVDYVEKMVPSCVSLLLSLLIII | Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 78
Sequence Mass (Da): 9000
|
A0A963PBD7 | MQDLADRLPPRLGRTVRRMVAVKLTYSAIATLILPLTFLMVVIFRYVLHRDLFAYEEWLLPISFWLYFMASAVATYQDTQIRADVLESLFRTPRSIWIRRICLTAIEIVITLAIVYWGWLMIVNDISAYPFWQKTIALKIPFFVPHLGIFIGL | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 153
Sequence Mass (Da): 17941
Location Topology: Multi-pass membrane protein
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A0A4S8PUX8 | MSNSSQPTFQFPTAAIEVERAVAELRYGRPVLLAEGSRKLAVVALDCVAPSLYDQFAAVTEDRHSLLLTAPRAARLGIAADSDVITPLAGLAFDDASRLAYALGAEKPAIWQPADDLAIQSTELARLALLLPAMVLADVTEIADRFAGCCEIAASRLKGADVARQRFEKVVRTRVPLKDLGDADFVVFRGGLAQKDQVAIVVGKPDMSKTVPIRIHSSCITGDLCGSLKCDCGDQLRNGLALLKQAGGGVLLYLDQEGRGTGIGAKMRAYGYQHLGLDTIDADAELGLAEEHRRYEAAVAMLRQLGISKVAVYTNNPTKIAGLELGGIEVEARSPVTGRVTAENQNYLRTKTLRAGHMLDLETLVAAE | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
EC: 3.5.4.25
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Length: 368
Sequence Mass (Da): 39309
|
A0A6G7GEG6 | GMVGTSLKMLIRTELGQPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLTSSTVESGVGTGWTVYPPLASGIAHAGASVDLAIFSLHLAGVSSILGAV | 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: 136
Sequence Mass (Da): 14309
Location Topology: Multi-pass membrane protein
|
A0A0F7ZWZ2 | MASKSSSVSVSLPKLAGLIDHALLHPTLTDADLAAGCALARDLGVAAVCVPSYAMAETAEALRGGASEIDVVVNVAKVLGGAWHYVEHEIDAVNRLVSAAGGALKVIFENDYLDDHHIVRLCEICTRLRVAFVKTSTGFGFVKQPDGSLASRGATLRHVELMRLHAGPDVQIKASGGIRNLDQILQLMSMGVTRVGASATQAIMDEARARGIGEEEMLVEVGHVKGQ | Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
EC: 4.1.2.4
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Length: 227
Sequence Mass (Da): 23903
|
A0A6P5AH34 | MGIKGLLPALSPSTRPININDLTGSVVGVDASCWLHRGSYSCAKELVLGQPTDGYVNFFMSSIERLLQNDVTPLVVFDGPRTLPAKAKEAAERRRKREVAKLQARTAIDQQRARSYYLQAVSITPEMVDRVIEALEVRGVDYVVAPYEADAQLAFFSMNGAVRFIISEDSDLLAFGAKEVVYKWDPVRLTGQLISQNSLHLSFPDFRDFSHDKFQTICILAGCDYLTSIFGIGVVKAAKFVNAIGDRNIFQVRFDPLPDVPAANLTRTWTTEQMLNTTDQSDFTFVCTDESEEGSSSSSTKPKRNLRSDPLTQANVVNIGTTFKWTIPCFPVMSLTFRQATVSIDGQLKPAVFDAADQRVLLYPSPFDIVLRETCSISVDNKELLVIWTWDFASLATTSSEDILSQVPHSTLSSASIHTVQEYDYMSDSDSDSDKRQHDREGKDDDEVGEPRENRRRETRLSDEDPDEDSDDDSFDTHELPFKVMGVTYHKRYQDVLEEAYNAINDNNNTPKADIIPEPDNSFDPNAIAVRIYTDNGPEKVGYIQQALTQHVHQAINTQRLGGVRIGRIAFRTTWYHPGWYLKLLITKLGKWEGAVVQKALRVK | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair.
EC: 3.1.-.-
Subcellular Location: Nucleus
Sequence Length: 604
Sequence Mass (Da): 67835
|
L8GPJ9 | MQTRSSWEHEEGEDGHGWDHAGWSYDGPTGPQYWGTLTPDYAQCSSGGRQSPIDIIEFRTSRRFLGDLKFTYPTNASGTLWNNGHTIEFHSETNLWSHISGGPLYEDQYHIVSMHLHAPSEHQLNGKYYPLELHIVHQARGTMDLVVVAVFFEEGPYSEFLAEYEYPIHDIETPDAHSPVGGIDVMSVIPRNASYYYYRGSLTIPDCDERVTWLVLSHTMTALPEQIQEFTKIYPHINRPVQPLNSRVVYFHAEGDPSLLPPNFHIPAPVECPPNVTITVPERDDPPEHHVLGISLVFFCLIALMVSLRAVRPK | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 314
Sequence Mass (Da): 35675
|
A0A0F2T6J7 | MRILVLGASGLLGGAVHRATAPGVQVVGLTRAGCDVTSAHQVARAIERHGADVVVNAAALADNATCNADPARAMAVNVGAARTVARAAQRQGTTLVHVSGNIVFTATEAPVGRREFEPADNHHGGILAQAKAEAEQAVLDDCTRVLLIRTACLFGTRPGGAWGGLPGRVRRAVTAGETLRMVNNSFTSAAYAPDVADALLTLLRHGQRGIFHLVNEGSTTPYTLTHRLRELTGAHPAQIEETFAEHTEYRLLADDKTTAAGAPMRGLEDALRAWLREDQHARP | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 283
Sequence Mass (Da): 29872
|
A0A6P4YIB0 | MTHGVMKDILRNLVGKLCSIQHLKTSQDLKPRVLILACVEAGRFLSSCLQSDVHTAVLCSPGNLIPHSKLYGKEVLGSEVASLEWACSQGSLKHVIVCGHSNCQILDVLGRSQMQSASNSRSSPFLSWLTQHGNSTLTRFERYEMDRLQPVTFQGVSPKELWDAYVDPQCYWTDQDQLSQVNVLQQLQNVSSHGFLKPQLKSGALQLHGMWLDSRHLPYLFSKEHQQFVQVKDDNIDSLLK | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 241
Sequence Mass (Da): 27129
|
A0A7S4D870 | RSGDIAEIQPKAAGSSLLHNLTRHFVKDALRIAGLDLDSLPLILPVATGMSITLTLLCLKSQFPERNMVVWPRIDQKSCLKAIYAAGCEPVVVENRLEGDSLVTDLEAVEQALLWPDERGAGGVAEEEGRESAGPEEAGPPPPPPPPLA | Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route): step 2/2.
Function: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
EC: 2.9.1.2
Catalytic Activity: H2O + O-phospho-L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + 2 phosphate
Sequence Length: 149
Sequence Mass (Da): 15879
|
A0A6P4Z4M7 | MLPKKAFKTGSTAPDPPAPGVLRLISSRFCPYAHRTRLVLAAKGIDYETVNVCLYKKPEWFFSINPLAKVPTLQHDGKVVYESLVCNEYLDRVFPGRKLLPEEPLEKARIGMLQAVWDAKCQPNLMKVSMSEGEERQKVFDALKEGLSFLEKHLATQSGKSFFGGDQPGILDYSIWPWFELIDLLLTDDDVKLQEVEFPELLAWRAAMFDRPEVQTCAFDMSVFAKYVATMRAGNPDPDIGLEDSN | 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: 246
Sequence Mass (Da): 27808
|
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