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stringlengths 6
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stringlengths 16
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A0A4Z2CN81 | MQLSRVRWCTAFCYRLNVVSLNKISNSFNIYFNRKSVYWLHLIWNFFVLCHIKCLLFFLSPLVIAYRKIKGVDLSENFVFVTSDATKMPSHLVKYAFGPTLTVEIKPKFGAIPLWPATGVVNLAKNSASLFCLRQEHSSKRSRWKDLSTYCPCDLFSGDRDRLVHGLNALLTTPQNNFRVYLDSHPIYSHDIDKLGYGLYRFFHLEHDSISLNKQQNEPPNCFDHQNVCGHSNECQFSNDRDRLIRGTLLEALLHKFDSTNDDLITRVPLNSSDRQPFSMCCALHLNGKFHSTQCGNCHNLGKKYTLPEGCILQRILSVQLLITTDIAFIFPHYKRVCTFLASHGWTWEMWLKLARNGEPLKYLKTQELAESFEIVEKYLIALIARDCSIMITIQRARPDCPSSSPVISSACCCIPRMLISCAVIDLDPKPLDKLRDRLDLETAVTKEAINRQYELLIPESLS | 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: 463
Domain: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Sequence Mass (Da): 53215
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A0A7S2WEQ9 | MFLWRGGFRVGSKEKTSDGKLHTSRWLVLGYIVPMLATLSFFTMADHKEERFLSMTYPMICFCAALSIDIMDRTVQYFVGGAFLTLERLLIVLGVFACCVLSVSRSTGLHMNFYAPIEVFEHVNQLDQLDADLAGATVCLGKEWYRFPSSFFLPQGVSVHWTKSAFDGQLPQPFSPWPEGTKKVHSYFNDENRGDPTRFFDVSKCDYAVDLNVGTDFGAIGRWDEMWSRKHCASFLDANLSPAFIRSFYIPFGYSAKKNVYAEYCLLEKNSRV | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 273
Sequence Mass (Da): 31111
Location Topology: Multi-pass membrane protein
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A0A0G1WR53 | MSKNIVKSMRPSSSPMSFKKSTTKDKKRQSIHFIGVGGIGVSALAKYFLARGVSVSGSDIKETEIVNELVKLGVRIKIGPHKAQNIPFGTARVIYTAAVRKENPEYREAKQRRLPTQSYAEAIGELTKKYETITISGAHGKSTTTALCALVLEEGYCDPTVIIGTKVKEFGDSNFRGGYGPYLVLEADEWNKSFLNYSPKIAIITNIDAEHLDTYKNLDDVKKTFLQYLKKIPSDGMVVANWDDRNVKDVVWQSKKRVIWYSQKDRDAEEIKKHLKIPGEHNLSNALAAARLGSLLGIPYVHILQALSGFRGVWRRFEFKGMDKNGAYVISDYGHHPKEIMATIAGARERYPMRRVWGVYQPHQYQRLQYLWNDFTTAFDMADRVLLLPVYDVAGRETKLARDAVNSKKLAKELVERGKLATYHPSFGATKRVIADESKKGDIILVMGAGDIYTIADDLVR | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 461
Sequence Mass (Da): 51858
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A0A7S0SQZ1 | GGGGGGGGGGGVISNSSGGDEGDGVAAGVDAPSASGAADAGGGGRGSGSTPEELGLGSVDAGVSGLNGRPVEWHETLDAVPPGPTILVAHEFFDAMPVHQFTRTKRGWCERLVAIRGQAPRPTSSAKSTAKPGSGGANLVEGSAAAAIWSSRRVDNAQPANGTDILIDTTDTADT | Function: Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
EC: 2.1.1.320
Subcellular Location: Mitochondrion
Sequence Length: 175
Sequence Mass (Da): 16960
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A0A6V7XXD2 | MSIFVPIVFVLLQLLQGCQSFGPAAKKTITLQSKLVVTKNFDCGFTRYIPDPKKMGDGGANEYQQPVIEVRNGATLSNCIIGAKEGFKAADGVHCEGSCTLKNVWHEKVGEDAVTFLGKFSDKPPSILMIGKIVLRFVIKCKYSYSFT | Function: Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.
EC: 4.2.2.2
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Length: 148
Sequence Mass (Da): 16229
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A0A142CDA0 | NHSYFMQDGFKISFYYFLFSELMFFFSLFWFFFDSSLIPMEEIGESWLPKGVEMVQPFSIPFLNSLILLSSAITLTWVYYNFLMLKKKMLFYFFTLLLGLMFLMLQFFEYKMMIFSM | 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.
Subcellular Location: Membrane
Sequence Length: 117
Sequence Mass (Da): 14313
Location Topology: Multi-pass membrane protein
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A0A6V7VIE9 | MFEQPQHSSSLTPSLSDNSISGMTNNSMLNSQTLEEYCWYWGAASKEEISAAMENQQNGTFAVRDASTKGQYTLTLRIDGTNKLIKILVENGRCGFTQDSMDFDSMASLVQFYQTCSLRDFNEKLDTCLLYPLNSPQSLTCQNSMKSDSTIDPSYRVSLLKCTFEAIHAEYDRVSRRYDQLFNQQLALNEEYNRKQRTESAYADVLKIFERKIAELKTTISGEKDLNDRDRESLTINIELQEERMEEIGKAQNLMRAAIQNIGLSLQKINEELGRLKPLLLKLHKKCEKYRDKLLEMSKQKVTHAQLDRVVQSVSLALDSEPSTLSTFLLRISLPMSNWCCECWLWHQATKDESIALIRSLMNDFDNSNASTDGIFLIRPSSSRIGFYALEISKDGNVHSCLIEYRDPRTTIDHSGGYGFAQTQMLFASLMDFVRYYSAVPLKEHNSVLDTPLITPALSQLKQRKEKNNSNTSNTDHQRDKAKLKRIEAIDDATELSTSRDDERSKEKILDTLLSFCGCANLLKIGMMQLVEINRGSARFKQLNYCLNDIRVRVSLFAYLLPNCFIPIFERYNSNIFISFILIAILGFICVVLIKTSRQRWMYSSQAFLLGTVNAWAIKFSVDAFEKGRTDVITFCLYVILFGLFHFSEFLMTAYSNPDSLRPDSFLLNHSWAYWTAAMCSWIEFWTRLWILPTFYSPFVSLAGLILCILGEIFRKLAMCHASVGFTHQISFRRSRNHSLCTDGVYAIIFLGYVGWMMWSIGTQLVLCNPICVISYAIVSYRFFEERIYEEERYLIEFFAERYIAYQRFVPTGIPGISGYEPTH | Function: Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues.
Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.100
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 824
Sequence Mass (Da): 94769
Location Topology: Multi-pass membrane protein
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L2GWC0 | MSEIKNAQNVLNDPTKRIEEKMRALFYLRNVLTDESALIIGDAIYKNTSVLLKHEMAYVLGQMKLQCSKEILIKVLDDENEDEVTRHECAEALGNFNDKEMVPILEKYLRHASLPLKETCYLAIKKIQESKDGVDLSKFDSRDPAIPLFKDINEQNIECAGKMLDDPNECLYRKYKAMFYLRDCGTEKAKKFLVGAFKDESALLKHELAFIMGQMRMDEGIEVLNKVMNDGNEHGMVRHEAAEALGAIATDDCYRYLQKNIDSDCDILRESVLVALDVLRYENGEETEYACVL | Cofactor: Binds 2 Fe(2+) ions per subunit.
Pathway: Protein modification; eIF5A hypusination.
Function: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
EC: 1.14.99.29
Subcellular Location: Cytoplasm
Catalytic Activity: [eIF5A protein]-deoxyhypusine + AH2 + O2 = [eIF5A protein]-hypusine + A + H2O
Sequence Length: 293
Sequence Mass (Da): 33525
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A0A6V7XLS8 | MDPTLNFKNETTRVKYIYVIQANPESVELLDIKNNKLVTEAFHSDRPLINYFNHPMTHFGPMMATACKETIQQHQLLQQLTNEKFDVGISEMYEYCSAALFHKLGVKTKLAAFAIPLLQMVGRKFDIPSFASFVPNTFASHLGLQSSFYYRFFNFYNEFYDWIWMDDYILREEEQIVLQEFGSDFPDLKYLTKKVSLVFFNSNPFFEMPRPTSNKIVYIGGLVDNLATEANKKLEPKIKKILDEAVEGAVLFSFGSIADTTKLNLKIIEGIVKGFRRFPNIQFIWKLDSETIKNMSELISPVSNIHTFEWLRQPAILVHPNLKAFITHCGQNSLTESVYAGVPIIGFPLFGDQFYNADVAVTHGIGLQIDVNELNGPNAENILFEALERVKIEIFYS | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 397
Sequence Mass (Da): 45557
Location Topology: Single-pass membrane protein
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Q4SKA0 | LQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAHSDKAKESIRGKCMQYLDRAEKLKDYLKNKDKQGKKPVKESQSNDKSDSDSEGENPEKKKLQEQLMGAIVMEKPNVRWNDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWREHLALRLVKNLFELARQQKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGELTPTGPPGMTDPRNPGRKTLPNTALLPGGVGVGNNNDGILVLGATNIPWVLDAAIRRRFEKRIYIPLPEEPARAQMFRLHLGNTPHSLSDGDLRQLAHKTDGYSGADISIIVRDALMQPVRKVQSATHFKKVRGPSRSNNQVMVDDLLTPCSPGDPAAIEMTWMDVPSDKLLEPIVCMSDMLRSLSTTRPTVNTEDLLKVKKFTEDFGMEG | EC: 3.6.4.6
Subcellular Location: Membrane
Sequence Length: 423
Sequence Mass (Da): 47544
Location Topology: Peripheral membrane protein
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A0A357LGZ3 | QDMEFVQFHPTALYLPSSPPFLLSEAMRGEGAQLRNNKGELFMHRYHPMGALAPRDIVSRAIWAEMAATKARHVYLDVTHLGAEFVKRRFPTIYATCLRYDIDITEEWIPVSPSAHYMMGGVWTDLNGATTVPGLFAAGEVACSGVHGANRLASNSLLEGLVFGARAAMAAVAYAGRHEVPSLAAQEAALKTEHFGSLDDAEKLRSSLRRAMWGHVGVIRSGESLIRACAQLSRWAQLVAQPFSNRAALEVKNMVHVGQCIAEAALWRENSVGAHYRSDFPQAKRPGWQQHSRLSMGEGISGKKSRKSRGLLLALRGRTG | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.
EC: 1.4.3.16
Catalytic Activity: L-aspartate + O2 = H2O2 + iminosuccinate
Sequence Length: 320
Sequence Mass (Da): 35103
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A0A6V7WW13 | MLFLSLSLHFLIKILILDYITNQLVNLINKHFPSIIISICTLSEPLKKEYAKINNLNFNDLMTDGKAKELVRKEMIEFGEKLRKEDFGIFCRKAFIERKIQNSPPLPTTNPSTTNKFKEIILISDCRRPTDFEFFKNNFKNSSIICVRINSKIEIRQKRGFLFIEGIDNEESECALDEFKNWDFNLFNNEEEKEGGKGEGEVEKELKNIINYLKQLFN | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 2/3.
EC: 2.7.4.2
Subcellular Location: Cytoplasm
Sequence Length: 218
Sequence Mass (Da): 25586
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A0A7S0X5B0 | PPCSSARVRAPLHATPHPHIHAPPSSATPPRGLPEITALWPYEHAARHRHPRRETGGTQLFGLYSHSAFVSAGLGGEVLARVGGTSMALRHGMRAATSSVLVWGAAGLMRAPLIGTRPSACHEATVWRSRAMGCAPASPTACGGSASSNQGAMAIPASTSASDASGFAAARNVGRGGMMGRREPVAAVLPFSLRALRHFSASSHAGDKLSGDVLGDLLGNAKAVAIRLELGALAEVQTHMRYAEFADVVKANSGGDTKESEVAEACRTLQAAGVIIRLEDVVYLHPSELTRDVLRALPTVPSSVFGVTEEEMRELEAELVAMHAEIEKAAASARFNSNTIVGAGLLLLCTQLAVFVRLTYVELSWDVMEPLSYFVGVGNAILVYIYFMVYKRDFTFGDWSTRLHDHFRWKNIRLRGIDHGRYTQLLRKLRRK | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways.
Subcellular Location: Membrane
Sequence Length: 432
Sequence Mass (Da): 46502
Location Topology: Multi-pass membrane protein
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A0A6B7KA21 | GDDQIYNVIVTAHAFIMIFFMVMPIMMGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLIMSSLVESGAGTGWTVYPPLSSTIAHSGASVDLAIFSLHLAGISSILGAINFITTVINMRSTGITFDRMPLFVWAILLTALLLL | 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: 148
Sequence Mass (Da): 16053
Location Topology: Multi-pass membrane protein
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A0A6G8IRX4 | WFFGHPEVYILILPGFGLVSHIIMHESGKLISFGHLGMIYAMLSIGILGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWIATMQGSFKYKSPQMIWCMGFVFLFTIGGLTGVILANSSIDIVMHDTYYVVAHFHYVLSMGAVFAIMASIIQWFPLFTGTVMNKKFLKIQFSIMFIGVNLTFFPQH | 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: 194
Sequence Mass (Da): 21899
Location Topology: Multi-pass membrane protein
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Q4RGA9 | MQEVQQSKEKTLANNRTLAEQNLALQPDLEHKKEQLTKSYRCLQEDFESYQLRKSTLDHRTGSSSLDTLLALLQAEGAKIEEETEVSAPLRPWWGFSVWSLPPPTRVTVRFPPRLSPPEHGRLLPGRGNDPGPLHRRVSEQQEAGSPEEGEDREAAGGGAEGPAPPPGLRLRLPLSGRVGGGAGGERRQLLPHGPGPEEAPAPTVTACPRSEPGPRRRPSARRLLRIAVPRHPSQNGPALSQRVFGLPQPLPVPVPPRAASEAPPAPGPTARFYHTVESVRGDAAYRPEGFSLQLLGAAHPSFHPPKNPPTGDLGTGAPHRPDRPGCSLGVRGFFSSSGHGGPQGSGPGPGLMLASVDVPPWLPQPAVRTHLVKEGRVEEEAALKVINDGANILRQEKCMLEVEAPITVCGDVHGQFFDLMKLFEVGGSPSSTRYLFLGDYVDRGYFSIECVLYLWSLKINHPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDCLPLAALLNQQFLCVHGGLSPEINCLDDIRKASDRFKEPPAFGPMCDLIWADPGEDYGSEKTSEHFNHNSVRGCSYFFSYAAVCDFLLNNNLLSVIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKGSCLPLLSCWCVSMETDSSHLPPLLPAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELLSEVDDLYEGGASAIRKEVIRNKIRAVGKMARVFTVLREESENGVTLKGLTPTGTLPLGVLSGGKQTLQTATVEAAKAKGTHG | Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Endosome membrane
Sequence Length: 809
Sequence Mass (Da): 88788
Location Topology: Peripheral membrane protein
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D5BVE1 | MIGKWESRVDRALASRLGLAVGLALIFLFAFTLRFDNLSFWLDNPERTLFGDPPRPLMLTVDSYIYLDLGRDLLEGTYESDLPTRHVPQGAERPPTAPLLAVMLAGLQKLTGAAPEWIAIVLPPFLGALIVLPVYMLGSLFATLVWSTPSPSTRRIAGLAAAAAAAASPYFVFRSSIGWFDTDSLNVVFSALAAALALRAALARDQRQRIIAWVLYSLVLVLFLWWWNTVPHIVFGLWVLPGLATLLFHLPRGWELVTVAALVLLGLVGAVAIAGWQVLNPVAQFQMVQGLFTYIAEQTGWIFPETGQAVSEQQATGWDQFLSWVPGGWFGLAMMVIGYALLVWRAYRAVMVMASLVIVTALSATGYRFNIFGAPVFGVGVGIAVAFFWVLLSQRSYRTLVTVPLLGVTLWGAVAHAQGGNNLVPRRYPIDMEAMIQLGELSAPNAVVWAMWGHGNPLHYYARRGVVADGVFHSGRLQWVLHLPLAKNNPRLAANWMQFYVTRGYAGMQRARHLFGGDKKSWAEGLEVIQRMFIVGPEESYRQLIPKMGGELAKAREVIEYFFPAEAPPVMLYLDHHLARTPWFKLGKWDLNRQVEVGDDHTYLPFRGYQREGERLIAEVKGKQMVLDLNGATMTWGERTAPLQQVRMHDGKRLLRMGLNPNADLVLSVNQVANYGAVASRAVADALLPRLFVDLAYDNRYFTLRAMMPSFYQIWEVRGEELTAEMAARVEAGLAKGEGRGG | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 742
Sequence Mass (Da): 82411
Location Topology: Multi-pass membrane protein
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A0A7S2SMR7 | MATNPNFARNQDMPPKGGYTPFDVRRKLPKARMSGAFMFGAVSLMTMYGYYQIGQTNIERRKVRRETRERRAHILPFLQAEEDVRYNLAVAVYEDEERRIMKDVPGWEVNKNVYNHKEWMPAFDNRPW | Function: Complex I functions in the transfer of electrons from NADH to the respiratory chain. Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 128
Sequence Mass (Da): 15261
Location Topology: Single-pass membrane protein
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I0GYF5 | MLSSHHNGLKTAALLGVLTGLILTVGYWLGGSGGLVVAVIISLATNAFSYFYSDKIALRSMGARPVSEAEFPELYTMVRELATEAGQPMPRLYVSPAMQPNAFATGRDPQHAAVAVTVGITRLLTLRELRGVIGHELSHVYNRDILISSVAAGLAGIVTMLAQLAFFLPFTSSDDEDSPNPAGLLLMMILGPLAASIIQLAISRNREFQADASGATMTRDPLALASALEKIHYGTQRMPLPAEGQLTSSAHLMIANPLRGGGIAGLFSTHPPMEERIRRLHVQASLVR | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 288
Sequence Mass (Da): 30720
Location Topology: Multi-pass membrane protein
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A0A8I0GD33 | MRASSEAAREAGRDRLIALIAEDGETAQTLSGELFALADLLNDQPKVAAALTDPTRAGEDRARLAERLLTSVTPACRDIVATMARQRWSHIDDLAHAADDLGAQALAIHARSRGVSEQLRNDLFDAEEVIANHRDLRITLSERGQLSAGDRVGIIHRIFDGKVSQDAVTLLERAVRAEGAGHIASTLRRYRDDVAAIEGVTIATVHAATTPTEEQVERLRRALSTKMGCDVVLNVAQDPELVGGMRVSVGSTIYDGTIRSALDEAERRLAGKARA | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Cell membrane
Sequence Length: 275
Sequence Mass (Da): 29656
Location Topology: Peripheral membrane protein
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R6B7H6 | MREVSVEDFKLFKEKVDNFITKDAETFYFRNLMEAIHDSDYMNEVNSIIEYVSKERTAKEIDELFQMLRAKAEGQFELRDKTEKYEKKVNYSLRGLAYFCLVEALNENSSFSEKIIEDIKKKYGKDYLDIVKKIDRAYLSVDGKTILKEQNLQLPNDEEMKKYLVMKKWQDEQRLYSMKRIRPLYPLELEYIDEPDQNLMLIHKKTLVKRAKEDLKKMKIVPIEYLAKLYEAGLEDELKDMIGGKALGLTKLRASEIRIPKTYVIPYYVEIEDNEIKNLLDENKKYAVRSSANAEDGGIHSFAGMFDSYLNVEKKNITDRVRDVKKSVKNDRVKKYIEINNLQQPNMNVVIQEFIEPEISGVWIGQSEDKGVLEWIEGNGEKLVSGKETPTREVWNRNTGTQDGIKTNDYIGKQLLDIQNTLTKSNGDTADMEWCVINGELILLQYRPVTREISMEENKTLTNSDEEIFVGSPASTGEVIGKSAYYRNLKDIEKWNDGDILISMFTDPDWLDVMSRSSGLVTAVGGMLCHSAIIARELGIPCVTGIGRKALKALRDENEIYVNGTTGEVCSSRIYEKTKKKEKEVIKDDKSYKEDFEK | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 598
Sequence Mass (Da): 69132
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A0A0L0BGB5 | MNNRTPHSAASQDAGRHADEHLDDGHEYFADDYEHPEPVEDFFATQDQGAHGAKKPRSKAKRRKRLRRTVVMLVVLGIFAGTVYGVALMLRDMLGFDTVTDYAGPGGDETVFTVDSGAGPLAIANGLQAADIVADSGTFVSALTSIAGGREVQPGEYEMRLQMSSADAAEALLGDDPTLVSYAAVARDLRQNEVFGILSESTGIPVAEFEALAADPTQFGLPAQALSLEGYLHPGEYRFDVDATAPEMITEMITATQDRLVQDGITDPAEQYRILTIASIVQAEAGEGDYATVAGSIDNRLTPGNTETNGLLQSDATVAYGLGKRTYQLTPEEKADTSNPYNTFANPGLPEGPIGSPSDEAIDATVRPADVPFYFWVTVNLDTKETKFSETYAEHLGYVAEYDAWCGQNPGRCD | 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: 414
Sequence Mass (Da): 44478
Location Topology: Single-pass membrane protein
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A0A6V7W633 | MVSTSGQIDCSEVQKPIGPQPLTSSQLNKEVDEGEISDEVFSGDVDTRNASPSKNQQKETMNNELDAVTLSNLVRAPPPAVSRSVIVQALYLLIEHHNNKEKQTDLDEYTITCRLRSRNSATQGKEGAIVRHKDGPFNQTNHIFIASRLRDLEKLGRAKLVSSNARYEEIKQPAPMNLFTLIRIASERLNFSPKYTMELANRLHKSKLLTNPTTFAKAYPAGFPNEDFIKNIIKQADELCKLRVDTRLILANFVRPKSKELRGFNSNNTTVGGVNSNTSSVPIHPCILSTSENLETMLDQCLENDEMELLKLICQYFFATCLQPFTYSVHTFEFEAGPERFMCECQVLATPGFTTYLPWMRPPNVSDQLPEEFRKRNPSREYFVTDIKKVDLPKDVPEHILESEFIELLEKRAVGNSLILDTLNALVELKFVNIVGPGRRIMPSATGLELMEQEYRKKIDQLGENVTQVESNIGDAQANSASHSSLDSTNTISSVSNNNIESNSNLNSKISAAIIPPIQRNFGFRQRHLGSTHSEFSDCSTRMSLRDFPIQKQQFPCRKQFQSELTLEQQNEQQSTPQLLQQLHIGMAEVPEENFNNKDRDSYRQQRANKNSSTSESNSLFHNRTNNEPFIVRDQNGNNFDEDIKQEGACSVENSSPSKSETLQQQHRWSWMATISSLSTKRRSFPPKNQEKNREWHYSAGRSNKSSVTDDDFGQYTSKRVRFESPKFKRSASMAPSERYKENNNLLNSSRIKSTTNFGNSNSFNNFREVQQRTCTPRRRSPSPERRRSQYRNNNFSNRDHNKFSSRYHDRQQNNFCSSSYQKPQIGTKRPPSDDSDSPVKSFKQQLLNQQRQQKNNDYYPQQRQSRYDSHIRDRDFDRGRRGFQNQQSERFSNSRVCLLDRYEGFTDLILVWVNCQQPSQSSHTNSYNDYLPRGRPWQPNYQQQNNISRQQSFYQNQQKFNGKQQQTSKSRPLADINTVPTKRGKWVWVDDNEGN | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
EC: 5.6.2.1
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Length: 996
Sequence Mass (Da): 114739
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Q4SAD1 | MRRQMRRRALSSLKELDAFPKVSESYVETSASGGTVSLIAFVSMALLAVLEFFVYQDTWMKYEYEVDKDFSSKMRINIDITVAMKCQREYRNPLKCSRRRREDDCCVFPAADVGADILDLAETMITSNGLQYEPTVFDLTPQQRLWQKTLLLIQSRLKEEHALQEVVYKTLLRGAPTALPPREDAAVEPLNACRIHGHIYINKVAGNLHITVGNLQLLPSDRPPVLRRGAAGRRQSAGRHGEDYLQKQPDVPVLRHRGSHPVGHAPDIGGHAPVFRDRAGEQSGRGCGGAPCRSLRAAFLPGAGDRPRRRQPRRLGHLREVRHQLPDGDGHRAAHAPGPVPGAAVRDRRGHFLHHG | Function: Plays a role in transport between endoplasmic reticulum and Golgi.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 356
Sequence Mass (Da): 39817
Location Topology: Multi-pass membrane protein
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A0A7S0X8Y8 | SELAARLAARAASNAREVEVTDRQGNACWVEKTDAGADADADALRDFIVAATAKDCSVMLALRRLEYHGRDKDARLIPAFGNEVGNSGMMMIDVAAPGGRRIVGGGGDDSDSGRSGGGSGGVHYKQTISGGGGKSLGVHYGQTVRDSDPS | 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: 150
Domain: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Sequence Mass (Da): 15409
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A0A7S2RTL4 | MIRGSGRVVVVGINVLDMKSFVKRIPVVGETCLSTKFEEDFGGKGANQAYQASLLLKESGCPVSFVSKIGNDARGHTMVSHMQKAGVNMDHVSIMEDIYSGCSSLLVDEEGQNVIVVSAGANAYLDESDILKAKDVITDSSVILGQLEAPLEATVAAFELASAQDKKTLKILNTAPIPSKLSADFYRLLDLAHIICPNEIEAEQLTGHSDPTQAADTLLEECPNCDAVVVTLGKDGALLAKRNFKTKIAGVDGIVAKDTVGAGDSFMGALGASLALGDTLLEAVEKANRVAAFSVSNYGTQSSYQSTFI | 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: 309
Sequence Mass (Da): 32564
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A0A061HBA9 | MSNPRSAAAGTVKVKKEVEGTLEDHPTIPGAQVLTTADGKKKLIRQRGKRGGAKNNKKTSSSTSDAVRANKAGKPTKDAEVKADAAKKVKKDKNSDAPSEHSLRIARYHTLEKELARTTDPAEQARIKAEQEQLGGLEAYQEDSLKGGDRLKGGESGKWCAEQVEKLRGKKAMRVLDVGAIAGTSYDKFPWIKATSIDLNPRSERVQKCDFFDLPKPANEEEKFEMVALSLVINFVGDLKKRGEMLLHAHHYLRPGGYLYLVLPLPCLTNSRYLTHDHLRSIVSSAGYDVVVQDDSKRLTRWLLKRKKSPRNKWDRTVYRKKELVGGAYRNNFAICMGDDASAATAVAGGKKKQ | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of an adenine present in helix 65 in 25S rRNA.
EC: 2.1.1.-
Subcellular Location: Nucleus
Sequence Length: 354
Sequence Mass (Da): 39198
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A0A162XHY8 | FIFGAWSSMVXXLSMLIRAELGCTSSLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLSAPDMAFPRLNNMSFWLLPPSLTFLLTSSMVESGTGTGWTVYPPLSNIIYHSGASVDLSIFSLHLAGISSILGAVNFISTILNMRVKGNLFDKVTLFSWSVMITAVLLLLSLPVLAGAITMLLTD | 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: 192
Sequence Mass (Da): 20855
Location Topology: Multi-pass membrane protein
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A0A1E5IGW5 | MAENIKDKIKAVSFEIVWEAKGIDFVSLKCRNPLVGDRQSQGIVAGFVSMEDGTGIVHIAPGHGQEDYQAGLEYGLEIISPVNDKGLYTKEVPEFENIHIYKANPLIIEKLGREGKILAKLRLTHSYPHCWRCGNPIIFRATPQWFLSVEHNDLRKKLLEAVKNVRWVPKYSGNRITAMLERRPDWCLSRQRLWGVPIPVFYCKECGEPLLDSKVIDKISALFGEKGSNLWFEMSEEELLKGTGAKCLSCNSANFKKEEDILDVWFDSGVSYEAVLSSGNYKDLEYPADLCIEGSDQHRGWFQTSMIPSVAVKGKSPYKNVLTHGFVVDGQGKKMSKSIGNTVSSEQLINKYGADVVRLWIASSDYKEDIRISDEIIRGLSDTYRKIRNTIRFLLGNIGDFDLKKALLFKDMQETDKYALSRLQQLISSAVVAYESYEFHKATAAIGNFCTVFLSGFYLDTLKDILYCDKKDGVERKSAQSAMLEICSVIIRLISPILSFTAEEAWRELTKLLHDVMRSVFLSDFPVPNSEYILHAETLEKWEKILYVRKEALAAYEKLRQNKVIGSNLEASLNIKHGQKYNEIFKDLKLVNLTLGSWDIKCNFSDKEDDLLIEAAKSEYERCARCWRHIEGIKDGLCLRCREVIDK | Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
EC: 6.1.1.5
Catalytic Activity: ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)
Sequence Length: 647
Sequence Mass (Da): 73697
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A0A4Z2DDD0 | MSADGVLNDFLAREKKDLYGLESDLNFLPNGDNNGSEHPKVNDEPECIRRWAISFQKRIDVKDDAERKSLSVLEEQGLKDLHDWALQYRDSLSRGQKLSRAHDKELRSAQKKAAEASVGMAQVDAGQAVLWERKEQTPKLSRQIQRIINGI | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Location: Cytoplasmic vesicle membrane
Sequence Length: 151
Sequence Mass (Da): 17171
Location Topology: Peripheral membrane protein
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A0A6V7XZ17 | MAGCRFGQSMGSYVSWLYVFIKALYLLNVTGQFFILNSFIGSTYRWWGIDVLNALLAGENWQDSPIFPRLTLCDVPIRRLGDTPRYTLQCHLRINTYNEKIYLFIWWGFLLVSILTFFNFWYYLLVLICLPCTQENSVRHLLKQDRHENMVYSAKKRDRKLIKSFAEEALCKDGILLFWFIEGHAGPLIAREILGEIFDYYKGKMVNFVDFYIDS | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 215
Sequence Mass (Da): 25399
Location Topology: Multi-pass membrane protein
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L0EVT6 | MKIKNVLLSSVACLLAVSSAKAADAVKAEPETAEGVRVCEAFGSGYFYLPGSETCFKIGGYLRFEGDYGKNQYGTAGNLRSWDAFARAQVDLNAKTDTELGDLSSLISLRADGRNSTSRSVFLNQGYLSLSGFKVGYFRGWWDDDIVGETDTLANDETRLVSASYTYNAGLFGAGISLDGLGRYGNKDIGVGGKLSAAFGPVKANVIAGYDGGTKKAAVRGIVSSEVGPGTLEVAAVFANGMNYYYGVSRASLAVGYQLHVTDKFKITPGFQYFWGLGKYSAYADSAGAPVKVSLNTWRSGLAFDYEIIKNLDALLSVQFQPKFIESTGKVAKNQVTGFIRLQRTF | Function: Forms passive diffusion pores that allow small molecular weight hydrophilic materials across the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 346
Domain: Consists of 16-stranded beta-barrel sheets, with large surface-exposed loops, that form a transmembrane pore at the center of each barrel. The pore is partially ocluded by a peptide loop that folds into the pore lumen.
Sequence Mass (Da): 37083
Location Topology: Multi-pass membrane protein
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A0A4Q4NMD5 | MDSLGGGIANADLSKLSDRDKQELQQFAMNEGQKARIQSSIHSLTDTCFRKCIPAGTVKNGKLDKYEEPCMRQCVDRFLDANMVVLRELERLRG | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 94
Domain: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space.
Sequence Mass (Da): 10591
Location Topology: Peripheral membrane protein
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Q7Y435 | MFNLEIDDLMIESFEKWLLTEEEENFGSIAPVQCLKPKQNPKQLFAVQTRDKDVIVRLCNFTNKTPKIIRMGDKTAHVVLCEMNKSGRIVQLKNGLGDNPIAVMASAFDVVMETARKSQLDAVMFRFNVSRMKGKTELVKRVIERLVRRTPKFEVFQQEVMTSKKIALVVVKRRGMAIDKIKGIKLDESLFTKVESDLGDRWVSKATGESLTKDEAYAASLVSEEERNAEAEQRVAAKSRLTKEEMLKTQATYNSDYVNHPEKINLKPEEDITEAEPKKQFNTLIDRQALERSTARSLNDWTSDIITRYGFMRTIFESEADAKYAVSELVKVQDQYDPLSAEVIAASVKRLKEIMSEEVFENKITALAMDRVDQSMPADVKAEMLRSHITQIKTDALRNVASGMFEAIASNMGEMMADIDLDLPGAEGFVLSEYADAAYINMNNFLTDRKLEEFEGISDPEELVKMCDALDNAFSNYGVKLDPGTILYRGMDFRSQMWETARKQKAFYFKNYVSTSLAPNIFGGWNANVASAVAGVDSMAGSRGEGGANVAFSIAGAENIPVLPVGNKAFAYKECEILLPRGVVLSFDTVTRATASTDSQETYYIEAHIMNKNELAALQESGEMIADGDAFIREGVVKPASDLSFSSFISEAKTERKKADKATLRQLIADLVSVDAMPDKFKM | Function: ADP-ribosyltransferase that efficiently ADP-ribosylates one of the two alpha subunits of host RNA polymerase RPOA on an arginine located in the C-terminal region. ADP-ribosylation of RPOA alpha subunit enhances the transcription of viral early genes. Also ribosylates RPOA subunits beta, beta' and sigma 70 and performs an autoribosylation reaction.
Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
EC: 2.4.2.31
Subcellular Location: Virion
Sequence Length: 683
Sequence Mass (Da): 76384
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Q4RI45 | MNEPGPAVSATNVGASGRSPSKTVAPRAAGSTVRQRKATSSGTRSGSRSTGSAGTGGMWRFYTEDSPGLKVGPVPVLVMSLLFIASVFMLHIWGKYTRS | Function: Necessary for protein translocation in the endoplasmic reticulum.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 99
Sequence Mass (Da): 10274
Location Topology: Single-pass membrane protein
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A0A0S1AZZ7 | MAGLQRTTYGVVAAGGALILLCGLLPWTWRAIPAHPLAWSVTSVILVAAYMALALLLLLPRLARVRVLAARDVSELETSRKALETGNRELQAMAGRLFSVQEDERRAISRDLHDDIGQAVTAIKLAAHAAMDEDDAQRRREDLEQIVELVDSTVVRLRNLSMLLRPPQLDALGLEAALRWQAGQLFRSSPVELLMDVEDLPQRPHNEVEQACFRIAQESLTNALRHALASQVRLCLEDDGGGRLRLRVTDDGEGFDPDGPRGLGLVVMRERAQSVGGWLRIHTAPGEGTQVELHLPYRMPQAAACQGA | 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: 308
Sequence Mass (Da): 33827
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A0A6J1XBH4 | MAQELSEKDLLKMNVEQLKKEVKNTRVPISKTGKEIKDFVEAEAGNDPLLKGVPEDKNPFKEKGGCVIS | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Location: Cell membrane
Sequence Length: 69
Sequence Mass (Da): 7671
Location Topology: Lipid-anchor
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A0A6V7X3E1 | MVVGGSSLIGADTSDSDLDIIFIIPITCLSNEEINKCRECKYNIKQYQKLCRDHDILFGDGEYVNSILKHLVNLINKARNDEPTNIYQINFINGRVPLIEINYRSQKMDILLAPIPFKNIPESLNLTSYENDEIINDNINTLNKSIDKMMETDDIQYIKSILILTGYRYTYRAKFHLIHYSTRENFTLLLRAVKLWAKKKHIYSNIFGYLSGSILIVMVTKICLIYPFGEINFLLQQFFQIYGAWSWPLPLITEQMTLNILEDKFKNFKNFWTFDKLNSSEDGLFSGDKMPILTSLFPEQNTAHNVNEFTLKIILREMKKVKTISLIMIINRKTYRTLST | Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
EC: 2.7.7.19
Subcellular Location: Nucleus
Sequence Length: 340
Sequence Mass (Da): 39664
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Q5BXE0 | LNPSSRLKGEKDWKKYETARCLHKVIDKIRADYRADFKHKEMRIRQRAVALYFIDKLALRAGNEKDEDEADTVGCCSLRYEHIKLHEELNGQPYVVEFDFLGKDSIRYQNSVSVPKRVFKNVKLFLKNKKENDDLFDRLNTSVLNQYLRELMDGLTAKVFRTYNASRTLEEQLERLTNPDDPPHAKLLAYNRANRAVAVLCNHQRSVPKSFAKSMENLQKKVQIPYNSSSYIADRCKT | Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
EC: 5.6.2.1
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Length: 238
Sequence Mass (Da): 27834
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A0A2H1VV58 | DPISPHQVSIVFHSAATLKFDEPLPVAIDQNVRSVQRLLDICDQLPNMQAFIHVSTAYSNAELAVVEERVYPAPVPLAQACTLAETLPGDLLGQINTQYISPKPNTYTFTKALAETVVQEHGNRGYPVAIFRPSIVISSHRHPFPGWIENLNGPSGVVVAAGKGLLHVFCCRSAARADMLPVDMAIDTLLCVAWETAVD | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 199
Sequence Mass (Da): 21609
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A0A7S2R987 | MDAVKRKRQERNKRRAAKKRSRKMDAYSKVGGKVIGVVGTDGGAIGGDVAGAGKESAKVGKSKTVKRVDCKSKVKSKSMQKLASVFKIDDGDLARAGKEVLAWMIAPTSVETFFQDNYEDKPLYISRPDQRNYYEGLLSKKLIQQLVKDGKLKHNRDFSLTQYRNGSRKTLKHDTEQIATSSTVWPLFDGKEKCSVRLLRPHEHSTFLWKVVSSLEGFFKCGGGANAYLTPRGSQGFAPHYDDIDALIIQLEGKKHWTVYEHYKTPQSVLDKEQSEEGDKSEEGDDKEDDEEEEEESEDDEVEKARVAKDLFPRYPLKSSKDFTQEQVDEHLEIALKKTLEPGDFLYVPRGMVHQAKAAEDSDSLHITVSVNQLNSWANFIKEALPHAVEKVCNNDLAHDCADMRRTLPRDYTDFMGVINSDQEGDPRRVQFMSEMIRLISENVLQYIDFDIIADRMAIKFQHDRHAPIGVLKPRYQGADDDDEPVDLDTKFSLVAKGVATLTVEQDSALVYHSCKNTRTWHETDQRGLDFELDDAEAIETILFSEPGSVLVVKDLNHSGTDDDKLRIVDFLLSEGIVVRV | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase.
EC: 1.14.11.-
Subcellular Location: Nucleus
Sequence Length: 581
Sequence Mass (Da): 65698
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A0A6V7U3C0 | MTSRPLIYGTSGFRAKADEQLQLIVYRAAFYAAVRAKKLGKAVGMMITASHNPGCDNGLKLVDPSGRMLAMECEEELTKIANGTEEEFEKFKNEEIQQIKNNEEKDNPTPIIVIATDTRPSSAILYEEAVKGIKLLGISVDIKYFEHHTTPQLHYIVRAINEKKPVDDYIQQFRRALEKSREFLNFEENTNLSPLYLDCANGVGSLWIAKYLENNGFICKNGLDVTKEGEVENLDKNIILVNLFNINTNDGELLNNGCGADFVKIKTSLPANFPTNLPVGTRCASFDGDADRLIYFYPNLEGKICLLDGDHICAIFTKFINEQLNEAKTNGELINLNFGVVQTAYANGNSTRYFSEKLNIKPLVTKTGTKHLEEAALNYDIGIYFEANGHGTVYFSDKFYKLIKEGENGKEKEQVPRYIKLLSLFSKLVNEVDGDAIADLLTVEFLLRYFNWTIQDWEKNTYSNCPSFQLKVPVSNRNLFVTPEDNETKLLQPIGIQNKIDECVSKFLNARAFIRPSGTEQIVRIYSEANSLEEAKQLANELEKIVKAETLKE | Cofactor: Binds 1 Mg(2+) ion per subunit.
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 2/2.
Function: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation.
EC: 5.4.2.3
Catalytic Activity: N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate
Sequence Length: 553
Sequence Mass (Da): 62441
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A0A1C8ZRZ6 | MKVLFFRPESDGEDTYNFNTTINGIEIINIPLFKVECIQYNLPEDVEMFDALAFTSRNAVRCFKDVNLIKDLKVYAIGDETAISIKERFGICPIVPKKFTSMELAEKILRDGVRTLIAVRSKLANNDMRKTLENKIRYIEVYDYDLSTIYNNIELAGKLISNCEVDGIAITSSSIARVIAKYINKECMTKIFSIGPVTSRVLIEIVGEAKIIESKTHSISGILETIVKVMGNNG | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Length: 234
Sequence Mass (Da): 26320
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G2SPK7 | MRKKDDVLEIGVLNLMHDKEDTKRRFERVLTREDCRVNLTWFYPVMHYQDREVPENVRQMSQPLDLNKVKELDAFIVTGAPLEKLDFDDVTYISELQELFDCLSTEGIEQLYVCWGAMVAANYFYGVDKYLLNQKLFGVYPQVILENSPLLEGLSDGFLAPHARYAELSCSQVREVPELSVVSVSETNHLFLAEARKERQTFLFSHLEYGRDALDKEYYRELQAHPEDAPVLAKAANYYDDPAKMTGMRFGWGKAQRHFFENWLKQAEENRFKKVCTQ | Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
Function: Transfers an acetyl group from acetyl-CoA to L-serine, forming acetyl-L-serine.
Catalytic Activity: acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
EC: 2.3.1.30
Subcellular Location: Cytoplasm
Sequence Length: 278
Sequence Mass (Da): 32517
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A0A2H1WI93 | VRNRMGFANFNLLLFGQVISYFLASKLLFDKVNETIHIVIDEYFHIPQGLAYCNGNYSYWDPKITTLPGLYLVSSVVGTYFKCNTYNLRVFGNQYINDVRLSKRSLIAKDVDKSKLKRYYGLKDVYYAARYHLSTGPNRTTIPFRNRETAEAQAVINTITIFSTLTPTIKFFIN | Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
EC: 2.4.1.256
Subcellular Location: Membrane
Sequence Length: 174
Sequence Mass (Da): 20127
Location Topology: Multi-pass membrane protein
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A0A2H1WVQ7 | LTRRQRIIQRNRTERLSDLLDWRNLGIYYRQARAEALKIVYPDYVDHMDQELGKRFNYPRPISEPPSPTHSMRRERKSSSSDDANTNEDTIPNEDIIAKKNQINIRKSLEILNISDDGTDPALEISFEKPNFAESEHENYRTPNENFLEPLNEAMVEQIDQLIAKLQDCA | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
EC: 2.4.1.11
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP
Sequence Length: 170
Sequence Mass (Da): 19915
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A0A6V7XZD1 | MDLKRMIYFLEVIITKTINIDYLNILNCYQLIKMCIKYCFCNYNDDESQKCNYDEKTCIKDEFAACFRVVRQEFNEETKTFELIHLFGCAPLEKGSNGSHLTCNAWRFAHSSPKSIFCCYEGNYCNKHLTIPSFPLIERSTKKIEYSTSYSSIYTLESFFFTFFGFLIGLCLIILFAIPLIRKKRGGKKEEEEIISLTKNNLENSKSFFEDSGSGAGRIILNKRRIALDLQMKEIFSKGRYGEICKAIYRGSYVAVKIFNTTEEESWRNERDIYLSQMFNHENILQYIAADILSNVDSLTQMLLITDFHPLGSLYDYLRSNYSLNFEEALNLVLSIINGLEHLHNPVRGTGECQKLEIAHRDIKSKNILVKRPGVCCIADFGLAIVKKEENNFLKIIW | EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 398
Sequence Mass (Da): 46165
Location Topology: Single-pass type I membrane protein
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A0A6V7Y6S5 | MNQHPKGKFEHFPDFRNVMYIGGIVVEEQGILTRRKTKKKKPECIVYVAFGTVYEDGGLKDNLLEMLNIFNGHQNCLFKIRIGKNEITETYKATNIEFLEGFAPQQEILAQTNTKLFISHCGQNSFNEAMYAGVPLLCIPKFADQFYLSSLAEHLGIGKFVWVSRREKINENGIEVKKEIKNENFIVDFSEALDEMMSGNYSRNDYKEGCMQLRTA | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 216
Sequence Mass (Da): 24826
Location Topology: Single-pass membrane protein
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A0A6V7XRM4 | MNVAGGMTIDDAKFMINDVFLNYHNFQFKIKLPHFTPTNVQNIEITNEFIEQKQILFDPNTKLFISHCGQNSLTEAIYAGVPLICIPYDGDQFLNSSLIEHLGIGIFVSLWEDNKKKNKNPAFGNEFTSAVAEMLGK | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 137
Sequence Mass (Da): 15474
Location Topology: Single-pass membrane protein
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A0A4R1HEC2 | MTESEKKAAQHNLADASERSSRRRLPLPDWPTTRQFLAALSALGVTLLILGLMNIWDFLHAEQSNWLHLANSVLLVSGIALLAFTFHVARRDLVAPLTELRHWVNEMHNGKLSARLPKSDQPDFSKLYRDINALAERLESLSLDMQSEVEQQTNRIQQKTHSLEILYDIAANINAANDLEDLLTRFLHTLKDVVNARAGTVRMLTNDGNMQLIASSGLSPEVVKKEQLVSIDRCLCGQAAQNGEVYALDDLKGCGQFAGRPFFDTEKVEMIAVPLRYRGKVLGVYNLFTKQHGLVEREDMKDLLTSIGHHLGMAIEKSRLDEEANLLSIMEERTRLANELHDSLAQSLASLKFQVRVLDETLHSGEESALWQELERIENSLDEAYTELRELIAHFRAPIDKRGLVPAVEQAVERFRRNSQISAFLQLEWDGTKLPAEVEIQVLRIIQEALANIRKHSKANAVRVLMRATPGHDYMVMIEDDGVGMPDKVIEGGPGEHLGLKILEERAARIHGKIKIESESGEGTRVTLTFPLPRDDNDADSNVTVDLPSNLVSNK | 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: Cell inner membrane
Sequence Length: 555
Sequence Mass (Da): 62275
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A0A1T4WZQ3 | MFSRIQQKYPGIRFANLGIGEICVSSLPLAVSTVLGSCVAVTMFCPVTRTGGLFHALLPERAPHGKLHDAEPCRFVDEGIRELLRQMERSGADMPRLVCKIFGGANAVFEEFYAVGMRNVDMARQVLAEEHRSVQSEDVGGTRGRKLFFITHTGEVFTKKLSSDVCFLPEGNANR | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 175
Sequence Mass (Da): 19320
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Q4SY57 | VAIIIPYRNRHEHLKHLLFYLHPMLVRQQLDYGIYVINQDGEGVFNRAKLMNVGFAEAAKEYDYECFIFSDVDLVPMDDRNLYRCFEGPRHLSVAIDKFDFKLPYSTIFGGVSSFSKQQFLTVNGYPNTYWGWGGEDDDMYKRIVFHGMSINRPDHMKGRYKMIKHQRDEHNEVNPKNPDKLSHTHETMDKDGDGGRYMPRDCLSQHKVAIIIPYRNRHEHLKHLLFYLHPMLVRQQLDYGIYVINQDGEGVFNRAKLMNVGFAEAAKEYDYECFIFSDVDLVPMDDRNLYRCFEGPRHLSVAIDKFNFKLPYSSYFGGVSALTKEQFLTINGFPNTYWGWGGEDDDIYQRIIFHGMSIFRPDHITGKYKMIQHQRDKHNEVNPKNSEKLTQTHLSMDKDGIKNLNYTVKEIAKDRLYTFINVDIHAPVS | Pathway: Protein modification; protein glycosylation.
Function: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 430
Sequence Mass (Da): 50500
Location Topology: Single-pass type II membrane protein
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A0A6V7V162 | MFYKNIKLFILLIKCLFIFIQKSEEANILVISPALSLSLIYKMGHLADLLVNAGHNVTVFIPEMDNIEETGTKLAQKIIRMKGLFNVIEQITNFDAFNEEISSYSARRSEDEGMVIYCESILKKKDELEILKNSNFDLAFSNMIDYCLQGIIKYLGIEKQIWISTGPLPEGPLWFLGIPLPLSISPLLQQTTMLGPRMNMMERATNIWQFALSWYSVMQTLRKENELFRSYISPDFPSLDKVLAEVDLAFVYNDEFLDPALPTLPKVISIGGLGIKPANYSINKFGIKLVKAIESSKKGTIIFSMGSITDTKFFNKEKWQNILKAFSYFEEYSFIVKISAGDIFTQEYTKNMPNIHLFEWFPQSDLLGHPKIKLFITHGGYNSLIESTIRGVPVLTIPLFFDQLRNSKCAEYRGNGRILIRKDLLNFEKIKEELNEMLINISYYKQNSQRLSNLHNQKPNRPEEAIIKWTEFVISNGPLKEMIPETVNLSLIEYLCLDILFFILIIIILIILILIKIIKKLIINLFITKKHKKE | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 534
Sequence Mass (Da): 61580
Location Topology: Single-pass membrane protein
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A0A317PHP0 | MTKLRTTILLSLAAFTLAGTMQPSQAGNGWGPGDFKPGIHKPFKPGFKAPGPKGPGPKKPHHHHDNNFEGAALGLLGGMIIGSAIANAQQQPVYVDSGNAHVAWCIDRYRSYDIPSDTYMSNSGYRKYCNSPYR | Function: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport.
Subcellular Location: Cell membrane
Sequence Length: 134
Sequence Mass (Da): 14486
Location Topology: Single-pass membrane protein
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A0A1E4ZIN9 | MIEDFTEPSPFKPVKHQWAYDHWKSQQQQHWIPEEVEFGQDIEDWQKISDNERNLLTNIFRYFTQGDIDVAGGYCDKFIPYFKNTELRMMLSTFASMETIHIDAYALLISTVNMPDTEFNAFNDYKEMSDKHEYLNNFNMNSPIDVLVSIAVFACFTEGLQLFGSFTMLLNFSRFNLMKGMCQVVTWSIRDETIHVSGMVRLFHAFKKSLGIKDSEIHERITDIASDVVKLEEAFINLAFEMGDQKGLTAQETKQYIRYLCDWRLKNMGIKPIFNIKEHPLPWLIPLINTVEHANFFEARATEYSKSSTTGAWGDAW | Cofactor: Binds 2 iron ions per subunit.
Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Length: 317
Sequence Mass (Da): 37006
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Q6QUX4 | MTFMEVAKPKWYERALVIAVQGVFFNAYFAAYLISPKLAHRI | Cofactor: Binds 2 iron ions per subunit.
EC: 1.10.3.11
Catalytic Activity: 2 a ubiquinol + O2 = 2 a ubiquinone + 2 H2O
Sequence Length: 42
Sequence Mass (Da): 4892
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A0A2H1WHD0 | RVVALYVAPAVVREQLRELAARAPDLDDTEVEISWGAREVRAVYCVEERRLELRVWLAPAHPLVAPRLAAAGAGGAGGVQWLQLYMAQQHGSVLGALRLWTGAVCARVEAAPQCYICYCRLQPSTGRLPKVPCHQCKNKFHNLANGSRRATNPTARCAERRSDVPVPDPRPRRGVVSVYILLCTLDTLNRLNYENEFGINRFFT | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal 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: 204
Sequence Mass (Da): 22717
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B3PML0 | MKYLLGNLKMNFTYQECEKYLDTLEKALSEANLKNVILGVAPSAEAMSLILKFKDRHFLFGTQNIFYKDKGAYTGEVSIRSAKEFGLDFTLTGHSERRHTFGETNDLINKKIMAINQTTIQPILCIGENLEEFNQKRTKDVLTEQITSALKNVDSNLDNLIISYEPVYSIGNGQVPENNYIEQVVSLIKKITNNKYKVLYGGSVAPKNIEELNKIKNLDGYLVGSAALDAVAFVKMAQTMDKQ | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 243
Sequence Mass (Da): 27350
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A0A3G3AFE4 | FIFGIWAGMVGTSLSLLIRAELGNPGSXIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNNMYFDQMPLFVWAVGITA | 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): 18702
Location Topology: Multi-pass membrane protein
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A0A061H6X6 | MKLVSLLVLLPLLAGSVSGSTRLERSVRSTPPSSSSAAARPSSGGDAAALLTAARNKLEETEDALLHSLIARGKLAGVHGGSGVSDWHGCADVFKSLPAMPRDNTTLPHQWKGHANQPDFLLAHVPSSTATTADDDAGGASSSSTIDRFFYANIAGALSGSPTTAAGAAAKAGGAVAEAGAGATRAEMLASSLSLQLISDRIHIGEDVARAKLAQDRQTLCPLIAARDSQGLVKAVTNTTQEQAVLDRVLRKVSIWSARPAPAPAPAAGAGTANTAPATTSTTSAATSDPDAARIETFANNVQQLFKQFLIPLTTQLEVVYLLSIKCD | Pathway: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
EC: 5.4.99.5
Catalytic Activity: chorismate = prephenate
Sequence Length: 328
Sequence Mass (Da): 33595
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A0A558NR03 | MSVQNAEQQLKFLLQQGLPLDSRPYRVLAQQTGLSEEQVLQRIQHWQQEGLIRRMGAIVDHHQLGYNANAMLVFDIPTEQVDLVGETIAASGRVSLCYRRPRRPGWHYNLFCMIHGRCRDQVLQQIAQLRQSLGLSVFPFQILFSRQQFKQCGGDYFEPDAKGAANGN | Pathway: Porphyrin-containing compound metabolism.
EC: 4.1.1.111
Catalytic Activity: 2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2
Sequence Length: 168
Sequence Mass (Da): 19226
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A0A830GN09 | MRLRSGFLGVLFVVALVLSTVVFAGFALHRSAITTQERQALESDAWTVATDIDTRLREKRSTVALWASNDAVADHGSTAQQRAVTTLRRQTAFEGASVVAANGTMTAFDAADASPEDRATLVGQDFGDRTYVQTALRGQSHISTPFEAESGNYVVILSAPIRTNGTVVGTLNAAFHLTATDFFERATASLTSGRSLRVATRADTTLYDQSREFDAPLTATATVESTGWRVTVAADRTPLERRLRQSTGLQVGAVLATLLVVASLGVWASRRTIEQIERLSDGLGELEAGEYDTSLDLGPATEWRRISDRFDALAATLDRRESQLSVFSRVFRHNLRNDMSVIMLSTERILSAEDTDEAVQSSAERIYSRAESFMATTEHARTIHDELLDGRPATPVPADVRTVIEDVAHSLRTRYPEATVEASVADAAVVDGGRRLPIVLTELGENAIAHNDQPPGTRHLAFDAWRADETVAIAVSDDGPGMPETERELLVGNLEETPTAHGSGLGLWLVKWLVDSLDGSIAVSTPDGEGTTVTVRVPVDGDEEG | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 545
Sequence Mass (Da): 58858
Location Topology: Multi-pass membrane protein
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Q4TC88 | MSRSYNDELQFLDKIGSNCWRIKKGFVPNMQASGGELLRERRAGEADVRGAAERLSGRRGRLPPSHEADRERGGAARNRPRQWRLPEEVHRSPRRSLRLRLRHRQHGSVRHERPGSRGVSRGRRLRHQLRRPAAEDQPGRGRRPAGEGAAGPVAVRPHPRGRRLQGRHPHGGQGPGGGPGDGRGLVPEGGLRLGRGQGALRGVRAHAAGRPQQGVLQGQEEGPPSAGHSGSREPLRRDPGGGGDLQRLRRQEDGRRPPGPGVRDDPQRQPRPGPPGGHRRAGCHGEGHEEGPHLGQRPSAGVCAHHLAGGPGLPEGDGGGGELRLGQPLLHDLPHQTGEWAGRGAGPARSHQLSSQAFSKVFATTPDDLDMHVIYDVSHNIAKVEEHVVDGRQRTLLVHRKGSTRAFPPHHPLIPVDYQLTGQPVLIGGTMGTCSYVLTGTEQGMTETFGTTCHGAGRALSRAKSRRNLDFQDVLDKLADLGIAIRVASPKLVMEEAPESYKNVTDVVDTCHQAGISRKAIKLRPIAVIKG | 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: 531
Sequence Mass (Da): 57370
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A0A6V7U4D8 | MTRKKSNKTASNNNNSDPFKRIQNTRQCPKCNKKVDYSIYLEHYEKCKNREGEVEEDDDDIIFCGEGQGHKENEQVSREVNNSKKNQKRTDKSSVVVNVEEEDSRSNSEAPRSSALNSGIVSENVFDGNARRAPASPITICDDSSNEVPITVFKPKNYCSDLPLAQIYDLCVERLQSFLNEQEELLRNLPPPKCDTNRPLDLTDENDSLMDPPPTENLSNKLLPVHYSLRFVWQILQKALHCVKNGHENILETATKFWGDSLRKVYSFLTTSVPAQQLFCRILVRRRGFHIARNIRYHDLGPKLMPLFIELCENGFFEEAFSINENGDPNSSNITLDEAFNLLQVDDFKIICKKFHIDTRIGRQGIIRELKKHSIRKDVFGRCNLKHLLNCIKQLTGKCYRIKQDVLYFFNSFFSVYAPNLMDVGAAAIRPHQCYVDLCDSLIFSMLQRQAETLNFVNNLNLKYSLIDLFSDFDGLTRYVKAKYDEQRLVCLIDKSLFEEAKSVAAELKELFSKEFLDGEEDAKIFQFINLPVYLRKFTPPWIYCRCIFRGVEAAQRLRDYELAVNWLIFLLSKEELKHFCINSRGRWYKRLVLNLNKHLKRNEEAAKFCCLGIEENFVLISDKLSLQERLDKLSQRVVDCPQALLENRLVLDEPEKVSITGLTLGKGLGDGLQVNHFYIPSTSTQPNVDENVLPETTIQSDTLSSSSDTSSCSSFTSTRRGGPSEQQQPSTQTTTAPTNTNINKCNVEEIALRHFIENENYKEGVHAEGKIWHMLFRLFFWDIISCVEFENELANNVWISWMQNDPLDLNYTMFYENRSNLIDARLEKILNSLSECILNITSPTTFEERIPSSSGSPQRKSPRKSLHCPCFIHSTVDKHYNEKSAKTMENSARSSTIEWHDFEGGKEQLLRFLHCCSPVLLHALFKKLCTNFRQSRSGFPDLTLWNAEDRKLAVVEVKGPNDKLSTKQQIWLDFFKSQGVRAVVCHVSAKNDRSIE | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
EC: 3.1.4.1
Subcellular Location: Nucleus
Sequence Length: 997
Sequence Mass (Da): 114791
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A0A8I0KNS5 | MTLSLVALTRPDTDMFTLRLRELMSRRAIVRGAAVTEQVPLDGQPAGALAAIATADWVCVTSPSAARLICSATSPIPDGVRVGAVGEATARVLRDHGLRVDLVAGGSGRDLVAAFPPPTRPGRRVVLPASRRASSTVPDGLTQLGWSVDRVDLYDTRPLPRIPEVFAAADVVAATAGSAVRALAEAGLWHREGPRLVTIGRPSWRVARDLGIPSVAHAPTPTPEGFAAALAPFCPLV | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Length: 237
Sequence Mass (Da): 24779
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L0JVH6 | MAQVEAPAVDHPLDPLTAEEIEAAADIFEAETDLDGEIKYHNITLAEPPKPKVKEFEPGDTFDRKAAIVAREDGETYEATVSLAENTVLEYEHLPDVEPAVMPEEIEEAREIVKNDPEWREAAAKRGVENFDLVMVDPWSASGFEPEEHKGKRLCRALSWIKTSENDNGRARPIEGLFAFVDLDEMKVVEIEDNGVPDEDSPLPPEDADYRADRVETRDDYEHLDVVQPDGPSWEVDGNKVEWLDWELRVGWTAREGLVFHDVKFNDGDESRQVLHRASACEMAVPYGDPDPNHSWKNAFDIGEYHAGRMANQLTEGCDCLGVMKYFDVEMNTIEGEAETLESAICMHEEDDGILWKHTEERKPHTEVRRRRRLVISFIATVYNYDYAFYWYFYPDGGIEAEVRLTGIDSNGVVPADETAEDTYGQYAIVAPQVKAPIHQHFFNFRLDFDIDDSSMRAYEVHNEPTGSERDRKNGFRAKETLLERENEARQDIDPNRGRYWRIASSETENSYGRSCGYKLEPHTNVSAPMKPTSSYMRRSGFIQNHFWVTPYNDSERFAAGDYPNLNDDTTGLTEWTEEDRSLVDEDLVVWYTQGVNHVPRAEDWPVLPVEIASFHLKPEGFLDSNPSISLPAEPCHTEHDITSPDNGSSGDDCSSADD | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 659
Sequence Mass (Da): 74974
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A0A7J8K2R1 | MALIEVERKFVPGPETEDRLQELGGTLEHRVTFRDSYYDTPELSLMRADHWLRQRENSGWELKCPGTAGVSGPHTEYRELTDEPTIVAQLYEVLGTEVLGAGGVIAVLGPLGLQEVASFVTSRSAWKVVLSRVDKEEHSLKVDLDTADFGYAVGEIEALVNEEAEVPAALEKINKLSSMLGVLAQEKAPAKLIMYLQRFRPQDYQRLLEVHSSREKPQGTKDARQ | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Hydrolase highly specific for thiamine triphosphate (ThTP).
EC: 3.6.1.28
Catalytic Activity: H2O + thiamine triphosphate = H(+) + phosphate + thiamine diphosphate
Subcellular Location: Cytoplasm
Sequence Length: 225
Sequence Mass (Da): 25147
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A0A101T181 | MNWHERAACRSEDPELFFPVSDDGSSLLQIERARQVCHRCPVLRECRGWALRNGETDGVWGGLTPRQRRELSVPDPAGA | PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO).
Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Function: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA.
Subcellular Location: Cytoplasm
Sequence Length: 79
Sequence Mass (Da): 8946
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A0A6V7XDP2 | MAPPPDTPVGSVWRRASLLAAVTGTEPLSRTAAVATAGATTDMFFQATLARSFISTLKLRGDDDVVDRLNYYYTPIMLAIACLVVSAKQFGGSPIECWVNPHSRESMEEYIEAFCWIQNTYWVPMYEHIPDSHETREGGNIKIHLKFKKFLGQQIGYYQWVPFILIAQALAFSLPCILWRLLNWQNGTNIHHLISAAEGARTVLDQNEREKVFHALALTFTEMIDLRETEYCPHPAASIFTRFRPTRLLKGQLISCLYLFIKCFYTANILLQFSLLNAALKSDEYLFYGFQVISDLIEGKAWTK | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 304
Sequence Mass (Da): 34607
Location Topology: Multi-pass membrane protein
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A0A1F7G0T5 | MLLEAMRTPACGVMIARGDLAVECGYQRLAEVQEEILWVCEAAHAPVIWATQVLENLARDGIPSRAEISDAALGNRAECVMLNKGTHILAAVETLDDILRRMQNHQDKKSSMMRKLKMANTFSFSCLTAQCNPGDDPSTHPVQLQDSQAVLKKTPAFQKHPALNNSVIQES | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 171
Sequence Mass (Da): 18827
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A0A126Z673 | MTTVLVVVGPDIGRRGLRLPGGAAAGQGSGANESVAELRRGLEGLDGLVDVAVDFRQTDDEAELITWLHQAADDGWGVVLDPGGFTHYSYALRDAAALVVDTGLPLIEVHLANPASRDDFRAAGVISAVSTGIIAGLGVDSYRLAVRAAAERVQLRAAAAAPAAPSAG | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Catalyzes a trans-dehydration via an enolate intermediate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 168
Sequence Mass (Da): 17136
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Q4S225 | MFTLSELVVLMAVLSATASGYFVSIDAHAEECFYERVNSGTKMGLMFEVAEGGFLDIDVEITGPDGKQIYKGDRESSGKYSVAAHMDGTYKFCFSNKMSTMTPKIVMFTIDIGEAPKGQDMETEAHQNKLEEMINELAVAMTAVKHEQEYMEVRERIHRAINDNTNSRVVLWSFFEALVLVAMTLGQIYYLKRFFEVTGSGKTLAFVIPIIELLLKREEKLKKMQVGALVITPTRELALQISQVMEQFLQRFPQFTQILLIGGSNPIEDVEKFKDQGANIVIATPGRLEDMFKRKADGLDLACWVKSLEVLVLDEADRLLDMGFEASLNAILGHLPKQRRTGLFSATQTQELEKLVRAGLRNPVRITVKEKGAAASAVQKTPSRLSNYYTICRSEDKFNHLVAFLRQHKHEKNLVFFSTCACVEYFGRALETLIKKANVCCIHGKMKDKRNKIFAEFRSLKSGILVCTDVMARGIDIPDVNWVLQYDPPSSAR | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 493
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): 55550
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A0A6V7WHR5 | MLNKWAEENFKADYEFLIGGSLMLEVNTKNSDIDAIYVVRKNTEYFWDEEREENNDGTKKLKSRATQFFGRLSSKCLDNKEKNCSDQSFYCYLCLQDKVSNLKRITEIRVPLLKFKFYGIDIDISYVQIPEEIKDNKNWMDEALNNAENNSLGRVFPLSGYKSNLIIKELLPKEEQKIKIFRSALILLKIWAENNSIYGNQFGFLSGTSMLIMLTKIYLLYPNTCSVLVIVDRFFLTFLTWLVWITLIFKAKLFIKSLI | Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
EC: 2.7.7.19
Subcellular Location: Nucleus
Sequence Length: 259
Sequence Mass (Da): 30372
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A0A6V7WRW2 | MYMRRGPEKLAVVDLTTTKKIPNMLVECRMDCTDLLHKDANLFYLLKRYGGRTLVFCNSVSAVRRLQAILRKLTRRNIDTLPCILHGRMKEKERLKSVEKFAASENSILLATDVAARGLDFQSVQQIIHYQVPQTTENYIHRSGRTARALNSGLSILFVDPMDLQYYQKICRGMEKNEDLEVLTIDDRKLFESCKYLVELATEAESIEHRGRKQRTKSSWFQRMAKEADLIWDSGEESISTQKNVLDDDNWHQKKMDRKLKQIETTLQKMLYSLTPSNLCKENNNHEAEDKHNEDAKERVRKRMKLERGKNKWLKKRPKLK | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 321
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): 37679
|
A0A968NAS4 | MDIFLIVFLVVQVLIITLAVTTGFAYLTWYERRLLARFQNRVGPNRAGPLGLLQPVADAVKLFFKEDVIPTASDKVVYLLAPVLAVMTAIVIWAVIPFGCFNLNGDHTACFDPARRDEVWNALQVAEVNIGILFILAVTSIGVYGITLAGWASNSKYAMLGGIRASAQLISYELAFGMAVLSVVMFGGTLSTWEIVLAQEGLWFFFPLILGFLLFMISATAELVRTPFDLVEAEQELTSGYNTEYGSMKFALFFMSEYIKMIAMSAIATTLFLGGWRFPGLETLGDGVAALAGPWPAAIIVGLVSLGSFLLKVAMFLFMLVWLRASWPRMRYDQLMQFGWKSLLPLAILNLVMIPVVVVLVPDNRYIQTAILFVLGIAAIFGAARIGGRGRVKSKVELVQPVAEGKQASAASSAPASQQTSGVAS | 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 ubiquinone. 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. This subunit may bind ubiquinone.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 425
Sequence Mass (Da): 46249
Location Topology: Multi-pass membrane protein
|
A0A0M8SD95 | AIGRAGNPDTLDGVDVVVGTGTSIVSGEGLIATAGAVDTHVHLLSPRIMEASLAAGVTTIIGQEFGPVWGVGVNSPWALKHAFNAFDAWPVNIGFLARGSSSDAAPLVEALAEGGASGFKVHEDMGAHTRALDTALRVAEEYDVQVALHSDGLNECLSVEDTLRVLDGRTIHAFHIEGCGGGHVPNVLKMAGVPNVIGSSTNPTLPFGRDAVAEHYGMIVSVHDLKPDLPGDAAMARDRIRAGTMGAEDVLHDLGAIGITSSDAQGMGRAGETIRRTFAMAAKMKGELGPMAGDGEGDDNARVLRYIAKLTINPAIAHGLAHEIGSIEVGKLADIVLWRPPFFGAKPQLVLKSG | Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
EC: 3.5.1.5
Subcellular Location: Cytoplasm
Sequence Length: 354
Sequence Mass (Da): 36673
|
A0A6V7XPM1 | MNFYRQRFFHVLAFRLCCCFFSNTWFVPDEYFQSVEVAYHIVYGKGHLSWEWLPEWALRSPLHPLIYAFPFWLLKLFCLDFGFIIRWIPNIIHAFLFAIADICFINWAKSVIGFSFDALYIILPLYFTNWFIVYCSTRTLSNTLECCLMLIALNFYTKNDANYVETKKNDDSEEENLAKFSILKIDSFCICLIFVSIAAVIRPTTWLLWIPLCYGHFVFYLLEGLDVINQEIVTERMEKYILSYSPFVIIIPLFTFILDSFYYGRPTSTFFNFFHFNIIKSGNALFGSHPWHWYFTQGLPSILLFASIPLFTILVKLIRSRFYVDVRLDRRFLIFIEKFFFSKITLGFYL | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 350
Sequence Mass (Da): 41757
Location Topology: Multi-pass membrane protein
|
A0A1V5VW57 | MKLSILAAIDRNYGIGKDNALLWHLPADLRFFKTKTTGHTIIMGRNTFESIGGGKPLPNRTTIILTKNPHYNAPENCKIAHSLQHAIDMCANKDELFICGGAQIYALALPLVHTMYITHVHATLQADTFFPKWNPNEWKKVSETHCDADEKHAYSYTFAEYIKY | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Length: 164
Sequence Mass (Da): 18606
|
A0A2L2TPU9 | MEKTTAQYLKEDIFVEKIHSEKIRGAYRAWDGQAMDVDISWGYYRGVPFYCIIKEQNQGKRDSLIVVRSFLYKFNIRDTKPTTIFSSRFLLSMTDWLSQEVRVDQVDHLIGMDPDTVFQNNFISELLKESKYPNTVGVCGYVAVDFSGGNWNLWSIYQNAEYTIAQGLRRLHQSIATKKVSCLPGCCQLLKICDMTCGDKVLIEQFGYYPRHLDGMIKRIRTTASEDRNHICQLLTTFPEAQSRQALRARAYTDVPHSWSVFLSQRRRWTLGATSNDLLLFTARHCQWWERILAFSNVLTWSLNVFVIASIGCMIVAFMHQPWWIIMAFAGIMIVPLIYYIIIEIWLPESMLERFQYLLGLFIFVVLGPFLNIAVMVFAVFNMDSFGWGKTRKVIVETPEEQLKEKQNIRDTGSDSNSLPGTFSSDQREEVTTSATVRKPAVVYVPPTTQHL | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
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: Cell membrane
Sequence Length: 452
Sequence Mass (Da): 52190
Location Topology: Multi-pass membrane protein
|
A0A5B7TKX3 | MNIKKFIKKNLLIELLISMCVILFVYAAISKFLGFENFLAQIGQSPVLSSFTYWVAWIVPISEVIVAILLITPNYRLFGLLSFYSIMVMFTTYIVIILNFSDFVPCSCGGILESLGWKQHLIMNISFCLLALYLLFQMTNTTSKNFDDQQKLIKHIKES | 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: 159
Sequence Mass (Da): 18255
Location Topology: Multi-pass membrane protein
|
A0A6V7UK02 | MLFGKPIHILMHQRRAKRAVSDNMSVRINMQKDETELVKNGRKPSKTANGDHSGENEPSHGSFGDIMVHQAIHTIEYVLGCVSHTASYLRLWALSLAHAQLSEVLWDMVLENAFAFNDIKGYIALYAIFFAFGVLTFSILVLMEGLSAFLHALRLHWVEFQSKFYLGQGYIFAPFFFKDILQRASASC | 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: 188
Sequence Mass (Da): 21315
Location Topology: Multi-pass membrane protein
|
A0A6V7VS02 | MGWAEDSRKIDKLVEGANEQLRMLYIPLLKNDKQILVENDEMIEQDNSIQTVFHRLQMLPYFVQRGLCNSYYPSRRFRRYNTNLDIEELIYHISHRYDVPERLDLVLQKIVGHSSKHQSIKNAFTAGISRSFKYIWPKLVKGILKK | Pathway: Lipid metabolism.
EC: 2.7.7.41
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 146
Sequence Mass (Da): 17383
Location Topology: Peripheral membrane protein
|
A0A1W9VQE0 | MGKNYFITGIKHCGKSTIGKKISKPLNLDFLDLDNLIESNVKMGVREFYKNQGRENFMLQESNSLKSITQNHSQGFVCATGGGICDNPLAFNQLKKIGYVILLIEEFDLTYNRILAGGIPAFLTSENPKKEFYELYIKRLEIYRTNADIIIECKARDPEIIKNEIIQKLEELHNVRK | 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: 177
Sequence Mass (Da): 20293
|
A0A7J8BKG7 | MIFPVYRCALRRLRRLRGRSFSTSAMEVAFRGVRKVLCVAEKNDAAKGIADLLSQGRMRRREGLSKFNKIYEFDYHLYGQNVTMIMTSVSGHLLAHDFKMQFRKWQSCNPLVLFEAEIEKYCPENFVDIKRTLERETRQCQALVIWTDCDREGENIGFEIIHVCKAVKPSLQVLRARFSEITPRAIRMACEHLAEPDQRVSDAVDVRQELDLRIGEEPLELFDCLRAVGHELRNQQRVCVSIRAAPCSFLPRFPGAAFTRFQTLRLQKIFPQVLAEQLISYGSCQFPTLGFVVERFKAIQAFVPEVFHRIKVTHDHRDGTVEFNWKRHRLFNHTACLVLYQLCMEDPMATVVEVSSKAKSKWRPQALDTVELEKLASRKLRINAKETMRIAEKLYTQGYISYPRTETNIFPRDLNLTALVEQQTADPGWGPFAQSILERGGPTPRNGSKSDQAHPPIHPTKYTSSLQVGVPNSAACWSPEGGEGQCRTGISHGGLSVSERSDFEIFLPFQKKNVSVKILLFHNLPVSIWKTPHGGSCSLPSPTHFPLCQLLSLLPLPLLLSSSSLPLPPLLLSLSSPPPPPPPPLLLLPLPLPPPSILFFLILKVIHVHFRQFRKYKRL | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
EC: 5.6.2.1
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Length: 619
Sequence Mass (Da): 70430
|
A0A1V5W9M2 | MNIIQEGNGLTQVLKIQVSAADYADKVEATLKDYRKKAKFDGFRPGTVPMGIVKKMYGKYVLVEEVNKLLSDALSNHIAENKLPVLGEPLPNMEQQQSINWDTDTEFEFCFDIAIAPEVSVELSKKNKFDYYKIVADDAIIQEQIDHLTARFGSQQSVDTIEGTELVRGNFTQVGVENPYKREGGTLLLSKVATESELQVFKNAKIGDTVEFNPKKAFENDTELSSMLAADKDQTDVLYADYQFEITEILRFAKSDVDQSLFDKAFGEGVVSSEAEFKDKIRADFEERVGPNSDYKLLLDIKKKLVESAKFDLPEEFLKRWLLESNKDNDKVTPEQIETEFPLFLEDLRWQLISGKIIKDNGIQITEEDIRNGAKEYTRMQFAQFGMMNPSDEDLEHWSKEIIKNRDQVNRIVESEQDKKLIAYFKEVVKLNEVEKTIEQFNAMFEKN | Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 448
Sequence Mass (Da): 51412
|
L2GRS5 | MSGPISAETQDVSDYKSCTSQLCMTTVHKFAFIPLYLFSSLVSTLLNKHITTTLEFHPTFLLLLMQSVIIVALLMLLKTINVCTFVLELRHMFYWIPSAVSMVLMIFSGLRALSHLSISMFTLFKNYSVIVIAVLELLLLGRTISRLSVLCFAMMIVSGMLVDYSETRVDRVGYAWICTNVVASAVYVIVLRMTIVHHIRARQREAEKNTRRGDKKDAVAHSPHDHGRKCYVDDEGIAATDRAGKELLRRMLRVVTSDETGDAMHPDTREMPSGAVCTTRNGGTCTAPVIVFCNEAARKVRNNRIGDYVRMFEGLDGSQSEHTSPDGGAGKNAQAVDAHGNRETKKRDFTPRKKGKQNQPNDFESLMYSQILSIPFLFLLSLLFDNYASISSFKRVLENDVLSSPDYMDTLLLNMEKVTDLAVVHNILIIKAFIGDLLELSGSAYFDDRVFLFIALSGLSVFFVALSTVWCLRSLSSTTLSMMGATNKIVVGMSGVFLGERIGVLKAMSIVVGGMASILYVETIRKE | Function: Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 527
Sequence Mass (Da): 58577
Location Topology: Multi-pass membrane protein
|
A0A7S2WHR5 | KNGSKQEMRTWAWSTVPEVRDAYEDYLRAPIIRAWKTDKNLDSKADVWTVTMQMPLSTGEKVHQVQALAFFEYHLDGRAHLSMDGLAYLEHSSPLPGVGLLIEGEARLNQRQALSI | Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular Location: Cell projection
Sequence Length: 116
Sequence Mass (Da): 13183
Location Topology: Multi-pass membrane protein
|
A0A2H1VQI4 | MDTLKWLSDLFWDERWWLPRGAKWADVTNGPDKTVLHPDVSDFYYVIPLTIGLLVLRYVLNIYCFIPLGLALGIRNKKKKNLQHIPVLETAYRKNALIKDTTALAKQLDMSERQVERWWRLRRNQDKTSSLTKFCEHAWKTFYLFFSTPTVYYIVWDKDWFWDLDKCYTNYGKHELTMDIYWFYLTTMAYMIALSITFFHDVKRKDFWGMLAHHVVTILLLCISWIISAFRIGIVVIVLLDLTETWLEFVKALKRANFEKLATSLFVAFVPAWFYTRMYLFPLYLYSTSIRSMVFWGHVFALYIVNAMLFVLFFLCVYWSVLIVKVVFDTLKSGVPRDVRSSSSEVSEAEVDKLLLQTIDKKNALNKSL | Pathway: Lipid metabolism; sphingolipid metabolism.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 369
Sequence Mass (Da): 43747
Location Topology: Multi-pass membrane protein
|
A0A177E4K0 | MPVLLPPLYLAFLATQLYALRIHCPHPPSGLVYPTSIQVLKFFSVVAGSLSWTLIVSLPTSTAIGTTVVIAFFPSSSLLLTWTALTTLSRTFSVIFGRVTPKYIVSTAPFAHVRHPTYISYASELLGAVFFILASYLPTYFSKRIDIEGTGLSMPVRCVGLVTMVAGFMWLYRR | Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.100
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 174
Sequence Mass (Da): 19185
Location Topology: Multi-pass membrane protein
|
A0A6N4RBV0 | MEALFTLVMLAIGLSVDTFAAAVSKGASLKKALKKKQKREIAIIFTACAVAAPALGYSIGFLLSELVEAFDHWIAFFLLSGVGLHMAYNGFQPQPTSSSPALNQTKVFLMAIATNIDAVAVGIGIAFTELNIVWVCIATALGTLAAVYLGITLGKRGGKLLGPKAEIIGGLILVLIGFKTLLSHLFG | Function: Probably functions as a manganese efflux pump.
Subcellular Location: Cell membrane
Sequence Length: 187
Sequence Mass (Da): 19580
Location Topology: Multi-pass membrane protein
|
A0A7S0T4E5 | DDRAQRRGLGKFLMFLCESLAKRAGMSGVMLTVQKANQGAMRFYSGAKYAVSLLDPGKVDPWGAAEYDYHILDKLWDPACKLEVEKTAQAAWRENKRRVEAE | Catalytic Activity: acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H2A]
EC: 2.3.1.257
Subcellular Location: Cytoplasm
Sequence Length: 102
Sequence Mass (Da): 11525
|
A0A7S0SGZ5 | MRASTTLARWSAPRTAPVEPRSSNRLRACPTTSSTRRCRVFCVGDDAKEATRALPDATCVPESRHWSVADSAALYNLQGWGAPYVAASKSLGHVVVRPLGKAGEDGEDDSAPEADLFAIAMEVRARLDSGGPLVLRFPDVACRQAATLRAVFAKAAHTWGYGARFQGVFPVKCCHDKDLLLALVIDGAADGFGLEAGSKPELLLALAVMRRARALQREEPADARPQRDTQVRAHRQDADASLSPPGPPRPSELCGPREPPPPLVVCNGYKDGAYIRLAIGAWSLGVRTVVVLEKPSELPAVIAAVRALPPGALRPYLGVRARLGTTHGGRWGATSGDDAKFGLGAREILWAVHTLAAENMLDCLRLLHFHVGSQVSDIATIKEAMRESSQMYAELVRLGAPMGFVDVGGGLGVDYNGTKGWGGDASTNYDMQNYANDVVAALQDMCTRTGVAPPVVVSESGRAIASAAAVLIFEVTSTEPRGVRTGVAPEPEEASQSREEGSTTTRAAGSASTATLDDLRIMTPSSFLLHNFREVLRSLEMAQHGVGGRSGAANVQESLNDAAQFRTEADRLFKLGIMGLEGRAQAEELFASVRGLAFDLTRRGRGPEGESPPMEVQSALRQPAAWYHANMSVFRSIPDAWAIGQLFPIVPLHRLGEEPTVAGSLADLTCDSDGRVDRFVGPAAASSNGDRGRAVSCLPLHALRAEETYLVAAFLVGAYQDSMGSRGHNLFGSPAVANVCVSPREHSRILKSDEIRFQMGGTTVTVVKGQTTADVLRDAGADPAELLAWARDDASRGGDQSGTGNRSSDQSGASTGSGGQSDARSHNGDQSGTGAGAGGEEVLGRYQEVLFKSYTYLESNENT | Pathway: Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.
Function: Catalyzes the biosynthesis of agmatine from arginine.
EC: 4.1.1.19
Catalytic Activity: H(+) + L-arginine = agmatine + CO2
Sequence Length: 863
Sequence Mass (Da): 91459
|
A0A4Z2D0V4 | MEVVEILFVIYVITLVFLCPYTKVEESFGMQALHDLLYLRTNISMYDHIYFPGVVPRSFLGCLLVGSIVSPIIYLSTLLRMDKFISQYIVRICLGLLTTLSLIKFSHCVKKVFGKHVYLRFFMICCSQFHLAFYASRALPNIYALMLVLYSLGHLVKGNQTKFVMSAGIAILVLRSELMLLFGPCLLYGLFAGYIKPRLKLLKTIITTAIISIGSSVLVDSMLWGKLIWPEFEVFYFNTILNKSGQWGSLLCTCMLLFAWIAVVVFSLPLQKVFGYQHGLMYLESTKLLLVAFIFIGLYSFLPHKELRFIIYVLPIFNLAVADVWSYLEKPMLNLRGTYLDLIMTKRKPNRISHFHAALVFGCYAHLLVNTVCSIVLILAARKNYPGGEALTRLSHMDHLINRSVY | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 406
Sequence Mass (Da): 46364
Location Topology: Multi-pass membrane protein
|
A0A1Y2L9A0 | MKKTVIPASLFAFSILLTSSYAVTAEQSHSKWGYDGAGAPSHWSTLDPANQICGTGKNQSPINLTNRIEADLSPIEFHYDVTAKDIVNNGHTVQINLNSGAYINLDNHRFDLIQMHFHAPSENHIDGKSFALEAHLVHADKDKNLAVVAIMYDIGTENTALASFWTNMPHMAGDSKATPNNTNIASVLSEDRDYYRFNGSLTTPPCSEGVTWLVQKQPQTISDAQLKAFTGTQHGPNNRPVQSVFARPILQ | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 251
Sequence Mass (Da): 27561
|
A0A1Y5TY99 | MKQLASLYSTLLDACGLLAGFVFVLLALFVSIDVVIRNVGLGNFGWLIEISEYALYGATFIAAPWVLRLGAHVRVDLVVGNVPRRAALALEIVTDLIGLAISLILFWYSLAATIASAESNSLIFKDLVVTEWWLLAVLPASMALLAIEFVVRLVRAVRGRTEAGNDTVLDGL | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 172
Sequence Mass (Da): 18602
Location Topology: Multi-pass membrane protein
|
A0A1Y4BBR7 | MKHSKGVVRKKKGTGLKIFLLLFFIIGISALVVAYKFIHPIYVDTKEKVFQITSEMDEGTFRRDGNTYVYDKDGAKIGKIGNENYSYVKSSDISTYIKNGYIAQEDKNFAVHHGVDYKALVRAGVSYIKNRGVITQGGSTITQQVIKNNLLSSERTFTRKFTEALAAFELEKIYTKSQIMEFYCNSNYYGNGCYGVEGAARYYFGKSAKEVTLAEAAMIVGTSNRPNDYNPADSYKNATRKKEEVLKNMLSEGYITQEEYNLAIKENPEVVAQPDDTDNDNYMVSYAVHCATLRLMERQGFQFKYGFSSGKEYKKYNKKYSSLYAECAKEIRSGGYKIYTSFDQSIQEKLQKSVTEGLSKELEGAAVCVDNSSQMIVAIVGGKSEKDEFNRAFLSERNPGSSIKPLLDYGPALNEGVATPATVLNDEPIDYNGYSPKNAYSGHLGPITVREALARSVNTVAVKLFQQTGNDVCLSYLEKMKFSSLCYADSTIASISLGGMTYGVKPVDMAKGYSTLANGGKYVDNDCITKLEREDGSIVYQPHGNTKEIYSVDTAYMLTDMLQGVFREEYGTANQLYKKGKILAGKTGTTDDNKDAWFCGYSVDYTTVVWTGCDTPKTIEGLTGSSYPAEIFCSFMDKITDASQDFSIPDTVYLAQYDKGDTTSILNGNDLYTLRPKEYDYYSRLNDEKREAYLLQQRIEKEKQEAEKAVSDFEDFTIKNTAQAKNLENQYAGVLDVIDKIENDTEQAPYLERAAYKYGLLKESVENKWDDVIAAEEEAAKEKEQLSMAEDTAESEDEAAEALQTQKRNIVEWYIDAMYDREVYGTGAQKLVADAENALSQYEGYDDYDDLKKDVDNAVAYVTALPTPEDIQSQENNLQYPNAADYPIP | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
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.
EC: 2.4.1.129
Subcellular Location: Cell membrane
Sequence Length: 889
Sequence Mass (Da): 99660
Location Topology: Single-pass type II membrane protein
|
A0A6J1ZN75 | MLGRGVWSSLRQGLSRGLSRKVGGWASGEGRKMDIAGIYPPVTTPFTAIAEVDYGKLEENLHKLGSFPFRGFVVQGSNGEFPFLTSIERLEVVSRVRQAMPKDKLLLAGSGCESTQATVEMTVSMAQVGADAAIVVTPCFYRGRMSSAALIHHYTKVADLSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGIKDSGGDELWGACVPWPMSWGLRCASWSDSASQGNGKMPRSCSTASLSQTLRQTVYPNSILGKSRRRAKVECLSRARQCCSEPHWSLRQEGKCDPALWDPRAEENHGLVWLLRRPLPRPVTGAKPHG | Function: Catalyzes the final step in the metabolic pathway of hydroxyproline.
EC: 4.1.3.16
Catalytic Activity: (4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate
Sequence Length: 321
Sequence Mass (Da): 34867
|
A0A6V7X584 | MYFKTTHKYFFKILYTIKLKYKFCSLINISKEQLQTYTQITELQTNQISGFWIFIWVLSKIPELFDTLFLILKGRPIRFMHWFHHSMSILFGTINFIGDNAYLVWVVWMNFFIHSIMYSYYMLTCFSFRFPKLYLNY | 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: 137
Sequence Mass (Da): 16908
Location Topology: Multi-pass membrane protein
|
A0A7S2RGF2 | QKMVALGLLLLLVGLVTGQHGTDQVYIAEFHLEHSGGTTGKILIKVDPQNAPIGAARFKQLVEKNFYKDACFFRVISGFMAQVGIPAIPHYMPEFKKHIRDEEKVVLSNTRGTVTFAMAGPNTRTTQIFFNFGDNSRLDRLNFPPFGEIISGIEELDRIKVTGEGAPNGPGPSQGLLVSKGNEYLLKNWPQVSCIRQTKIQGSPGGSNTIINAEKIATDTKKNPDVKMVAPAGLRDPVDPKASLYIHNTDSNNFMLVLGVVVVFGVVFFFFRSNKKATQTRDLDA | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 285
Sequence Mass (Da): 31263
|
A0A7S0SHW9 | ENFRALCAGDRGTGSETGLPLDYTASTFHRIIPGFMAQGGDFQRNDGTGGESIYGGKFEDESLSHMRHTERGLLSMANSGPATNGSQFFILFDRAKHLDGKHVVFGRLSAGHRVLDEMEGLGSKGGAPRKEVRIARRG | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 138
Sequence Mass (Da): 14912
|
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