ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B0S919 | MFVLKSASPRRKQILFDLGFDLKIDPEHIDESQKELESPLEYLERMVHSKLGTLFEPNNVYLAADTIVVYQNQILHKPIDTNDAFRILKILSGKNHSVFSGAALRHPNGTEYFYEETMIGFQNWNDFEINEYIKRSKPFDKAGSYGIQDKEGPVLQWIGSYTNVMGFPLRSFLSRHELWIGSWEERIMRRD | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 22348
Sequence Length: 191
... |
Q72WC1 | MIVLRSKSPRRKQILESLDLDFRIESEDIDESSLKDEHPLEYLKRISLSKLGTRSKDELLISCDTIVVQENSILQKPENFSQAIEMLERLSGKTHIVYSGLGIYYNRLEQFAFDSSKVHFHTWNKEQIKKYIERYSPFDKAGSYGVQDIEGPVQSFEGSYTNILGFPIRMFFQYHELWKKYLKGNQA | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21940
Sequence Length: 187
... |
Q9JXS2 | MGLELPLILGTSSVFRREQMERLGIAFQAASPDFDETPMLGESAPQTALRLAEGKARSLTGRFPEALIVGADQVAWCDGRQWGKPMNLANAQKMLMHLSGREIEFYSAIVLLNTVTGRMRRHIDKTVVVMRQLDELHILRYLEREPDAVYCSCALKSEDLGALLIERIESTDPNALIGLPVFRLVDFLKNEGVEVL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (... |
Q13VL1 | MSDSLNRPPRLILASSSPYRRELLQRLRVPFDVAVPAIDETPLAGETPEVTALRLAQAKARAVAGGLGAGVAALVIGSDQVATYDGLQIGKPGTHANALAQLQAMRGREVQFHSALCLFDSRSGTVQAVDVVTRVQFRDLPDAALEAYLLAETPYDVAGSAKSEGLGIALLEAIHSDDPTALVGLPLIALSRMLLAVGYPLLGAQ | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (... |
Q126I4 | MNSALNPVAASTAATALTPTSRPLVLGSTSPYRRELLQRLHLPFEVATPDVDETPLPGETPRLLAERLALAKARAVARNFPHAVVIGSDQVADLNGLPLGKPGTHERAVAQLRQMRGQTVVFQTAVAVVCLDSGFEQSSLAAVRVTFRNLTDGEIENYLRAEQPYDCAGSAKSEGLGIALLESIDNDDPTALVGLPLIRTCKMIQAAGVALFADRGEHP | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (... |
Q9HZN2 | MPDLILASSSPYRRELLTRLRLPFESASPDIDESHRAGESAEELVRRLSASKAEALAGRYPQHLVIGSDQVAVLDGNILGKPHTPERAIQQLRDASGKSVTFLTGLALLNSASRRIQVACVPFTVHFRHLDESRIRRYVEAERPLDCAGSFKAEGLGVSLFRSTEGEDATSLVGLPLIRLVDMLLEEGVEIP | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (... |
Q88LM1 | MLPLLLASSSAYRRELLARLHLPFTWASPDIDEQRLDGEPPVELVRRLARQKAEALAGSHPRHLIIGSDQVAVLGEQVLGKPHTFERACEQLLECSGQQVSFLTGLALLNSATGQCQVDCVPFTVTLRELSREQVERYVAAEQPLDCAGSFKAEGLGVSLFQSTHGCDATSLIGLPLIRLVDMLTKEGVMVP | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (... |
Q3IHD5 | MKYPLILASSSLFRQSLLQKFNLPFDTFSPNVDESALNNETPAQLVKRLSELKARAASKHFSKGLVIGSDQVAVFNEQILGKPHNKHNAVKQLSLFSGHSVTFLTGLCVYDLTSGESKTCIEPFNVTFKTLTDAQISAYCDAEQPYNCAGSFKSEGLGICLFEKLTGDDPNSLIGLPLIKLSQLLAEFGLDVLSAQSNTPLS | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (... |
O27140 | MKILITGRPGSGKSTMVGRLRDYLEGMGFSVGGIITPEVRVGGSRWGFEVVDIASGRRGLLASVETEGPRIGRYGVNVGVMDELAVPAIRRAMLEDDCIIIDEIGPMELKSREFRRTVDEVLSSDVLLIAAVHRKTLQSIKKREDIRVFVVDPEKRDRVYLRIIDLLGDYHGMR | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 19426
Sequence Length: 174
EC: 3.6.1.15
|
B2A6V4 | MTESNILLTGKPGIGKTTVIKRTVELLSCSSTGFYTREIKRGDPRVGFEIISLQTGERLPLAHTDFTTAEDRVGKYGVKAENLLGFLKEINEAMTSNKPQCLVIDEIGKMEFFTPGFHETVDKAFQSSYPLLATIMKKSHKFCDYLKNRGDTDVIEVTENNRDDLPEKLAKRIEEQL | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 19950
Sequence Length: 177
EC: 3.6.1.15
|
Q8ZTE6 | MTWRERAELRIGISGMPGVGKTTLVLKIAELARSRVKVCGFVTVEVREGGTRIGFDVVDLANGRRMALARVGRGEPSVGKYVVNLEACNVISEALRRECDLKIIDEIGAMEFKCKNFGEDLQTALHTSPRVIATVHRNYIDIAKKLGLEIIWLTRENWGLVFRQLLIQLGLTQ | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 19335
Sequence Length: 173
EC: 3.6.1.15
|
Q97WP0 | MLEESKNALRVFITGNPGVGKTTILLFLINKLSENNYKVAGFYCPEVRENGRRIGFRIVDITTNEGDWLAKENAPGRVKIGKYTVLEDSAKRITEITLSNINKADVLAIDEIGPMELKIPTIKKLIETILNNQKPLIAVLHRTQKPMGGRIYVITVENRDSIKYEILNYILSSLD | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 19730
Sequence Length: 175
EC: 3.6.1.15
|
A3DNY5 | MKNYIITGRPGIGKSTLFNNIINTLRKSGIIVGGIKSPEVRDSKGFRIGFKIIDLMSNEEGWLAKRNYYSTIKVGKYGIVLDESSRIIREALRKALEKADVIGIDEIGPMELKIHVFRTMLEQVLNSDKPKILVIHYRLRDPSILDKIYRVENEKYVLTEHNRDLLNKVLPQKIVMEIKQIIKK | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 21219
Sequence Length: 184
EC: 3.6.1.15
|
Q4JCN8 | MDKPFRIYITGKPGIGKTTLLFNIYRILKEKNWRITGFYCPEVRVNNTRMGFKIKSVLSGKEAWLARVDARSGIRIGKYYVVLEDNFVRQLEEEIFSFPDIILIDEIGPMELSSVSLKNLINKILTSNYPVIAVVHRSIKFDDGVIYEVTIQNRDILLEEILGRVTSNKNNI | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 19842
Sequence Length: 172
EC: 3.6.1.15
|
Q96YL7 | MQTRLRVYITGEPGVGKTTIFLKVIDKLKSQGYSISGFYCPEVREKGQRIGFKIKSLDNEVEDWLASIYAKSSIKIGKYYITINEDIINKIKEKISKSEIIGIDEIGPMELSVPKLKEIIDYVLNEKPIVVAVVHRKISFKDGKTFVVTYENRNRLDNEIFNYIISSIQ | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 19398
Sequence Length: 169
EC: 3.6.1.15
|
Q9HJH0 | MIPLAIKIGITGPVGSIKSEALQKIIDMLKNDNLNVQGVLVSKVTNNGKLTGYTIEDIESKRKAQFCFDNFVSRVKIDKLGVDTKILEEILIPSLQKARETADVIVIDEIGKLENTTKKVHAEIEETLKCGKPLIVTLHKRSRNPVLQEIKSLEGVRVFDITPINKNILPFKVMHVLKGEE | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 20194
Sequence Length: 181
EC: 3.6.1.15
|
Q5JF42 | MALRIFVTGPAGVGKTTLVERVAREVDRWGYIVGGVITREVRRGGRRIGFKITALDTGEEGTLASLRGTSHLPGVPFGKYVVHVDEIERVAVPAIRRAIVEADLIVIDEIGPMEYTSNEFIRAVGEVLKSEKPLLAVVHRKFIDRFRPLGEVHTLSFENRNAEFGIILDRVMKELKGIRG | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 20001
Sequence Length: 180
EC: 3.6.1.15
|
Q9WXP3 | MKILITGRPGVGKTTLIKKLSRLLQNAGGFYTEEMREGEKRIGFKIITLDGEEGILARTDLPSPYRVGKYYVNLKDLEEIGVRSLERAFQEKDLIIVDEIGKMELLSRKFREVVEKIFDSEKDVIATIKKSSDPFVEKIKNRNDVVIFELNEKNRNSLLNEILSVLKFNRGEKQ | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 20034
Sequence Length: 174
EC: 3.6.1.15
|
A1RYX5 | MAAKNFLLTGRPGIGKTTCVVKTAELLVSRGVKVGGMVTHEVREGGSRVGFKVRDLLTGREGFLAKVGAGAGPRVGKYVVHVEELEAVGVGAILRAVSEAQVVVIDEIGPMELYSPSFLPAVLKALDSDKPVLATIHERESSSGRLRGILERGDVKLYTVTLQNRDLLPPQLAREIASLVAR | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 19393
Sequence Length: 182
EC: 3.6.1.15
|
Q37165 | MIIYATAVQTINSFVKLESLKEVYGLIWIFVPIFSLVLGIITGVLVIVWLEREISAGIQQRIGPEYAGPLGILQALADGTKLLFKENLRPSRGNTPLFSIGPSIAVISILLSYSVIPFSNHLVLADLNIGIFLWIAISSIAPIGLLMSGYGSNNKYSFLGGLRAAAQSISYEIPLTLCVLSISLLSNSLSTVDIVEAQSKYGFWGWNLWRQPIGFIIFLISSLAECERLPFDLPEAEEELIAGYQTEYSGIKFGLFYVASYLNLLISSLFVTVLYLGGWNISIPYISILELFQRDQIFGTTIGIFITLAKTYLFLFVSIA... | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
P51931 | MEFILSLIGSLLLIICVLVSVAFLTLLERKVLGYIQIRKGPNKVGLMGIPQPFCDAIKLFTKEQTYPLLSNYLSYYISPIFSLFLSLFVWMCMPFFVKLNSFNLGGLFFLCCTSLGVYTVMVAGWSSNSNYALLGGLRAVAQTISYEVSLALIGFKILLFSLL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P18929 | MEFILSLIGSLLLIICVLVSVAFLTLLERKVLGYIQIRKGPNKVGLMGIPQPFCDAIKLFTKEQTYPLLSNYLSYYISPIFSLFLSLFVWMCMPFFVKLYSFNLGGLFFLCCTSLGVYTVMVAGWSSNSNYALLGGLRAVAQTISYEVSLALILLSFIFLIGSYNMIYFFFYQVYMWFLIILFPMALVWMSISLAETNRTPFDFAEGESELVSGFNVEYSSGGFALIFMAEYASILFMSMLFCVIFLGCDVFNLLFYMKLTFISFVFIWVRGTLPRFRYDKLMYLAWKCFLSFSLNYLLFFIGFKILLFSLL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q2I3H4 | MFLINVLTVTLPILPAVAFLTLVERKALGYMQLRKGPNVVGPYGLLQPIADAIKLFTKEPIYPQTSSKFLFTVAPILALTLALTVWAPLPMPYPLINLNLSLLFILAMSSLMVYSILWSGWASNSKYALMGALRAVAQTISYEVSMTTITLSMVLMNGSFTLTAFATTQEHLWLIFPMWPLMMMWFTSTLAETNRAPFDLTEGESELVSGFNVEYSAGPFALFFMAEYANIIMMNALTVILFMGTSCDPQMPEISTINFVMKTIILTICFLWVRASYPRFRYDQLMYLLWKNFLPLTLALCMWHISILISLACIPPQA | 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 ... |
Q9B6E8 | MIINIVEILIFLVCVLFSVAYLTVAERKTLAYMQRRLGPNFVGYYGLLQAFADAVKLLLKEIVLPKESNYIILVISPLITLITALIGWVVIPLGPGITLGELNLGILFSLAIGSLGVFGSLLSGWSSNSKYSLLGSIRSTAQLISYELILTSIFIIIIMFVSSLNITTIIETQRVVWYCIPLLPLLLIFFIASVAETARPPFDLTESESELVAGYFTEYSGSPFVFFFLAEYSNIILISAFNGYLLLGGYLSFNYSYLFNILFNDYSYVSFLFEGLINSSAYAIKLVFLMFSFIWVRAAFPRFTYDNLINFCWIILLPLL... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q35140 | MIIMTILSLLLSNAVTLRRDISILFNRIVIIALIYCILHDTMSLSIISKGVGLHGGLLHITNITQVFQIFIFLISILILQLTSFDPIKKFYIMRHPRFINKWPRAIGYSIPLSSIQAVLKDYLFKIQGFNKEHLKIIEYPLILLFVICGAVFLMSTNDLVSIFLSIELQSYGLYILSTIYRNSELSTTGGLIYFLLGGFSSCFILLGASLLYANSGTTSLDGLYIINSISDVNDNMTSWYKSYYLNFSLLIFSVGFLFKVSAAPFHFWSPDVYDAIPTIVTTFVAIIAKISIFILLLELVYHTNNYLSEFSWIYGLLVSS... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q36451 | MTPMTTLIMLFSLLLGTTLTLTSSHWLLMWMGLEVSTLAIIPLLTYTNHPRSIESAIKYFLTQATASMLLMFAASLNTWMTGHWTLMQIDNTISSGIMTFALAMKLGLAPFHYWVPEVLQGSSLMSGMILLTWQKLAPISIIYQISPTLNMDILLTLAISSTLLGGWNGLNQTQLRKVMAYSSIAHMGWMVLIIIYFPTLTTLNLTLYIMSTVALFTVFHTTNITKTKPLSLMWNKAPIMTLAIILLLLSLGGLPPLTGFAPKWLVIQELIKHDNMIMATVLAITALLNLFFYMRIIYSSTLTTFPTTNNNKFHWYSKST... | 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 ... |
P12771 | MHQMISIFLFLTVVSGTIIVVSAENWFVIWLGLELSTLALIPILWFCFTPRNIEATIKYFLVQAFSAALLLNSALIQAWFSGSWSALIPMESFPSLCLSVALAFNLGLAACHFWLPDVLQGLPFIQGLIIATWQKIAPLFLLFYFNQLNFSYFIILAALISILVGGWGGLNQTQTRKILAFSSIGNMGWIVVTSAFSLGTAAMMLFIYLVINTSIFLILDFLSIFTLGHLNNTSQLSPISITLVILTILSLGGLPPLTGFILKFSSLYSLINNGFIFFSSVMIIGSLLSLFFYLRIAFNTTLILFPQHLISLTAWRNSTE... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P15577 | MRAHLLHCELAFSFGKYFYSTSFLNLLMINLMFSKLGAIFFLNLALYLLALALFFFFLFNVKVALLKSVSQIYYFNNIFFFKFFVLIFFLNLAGIPPLLGFFLKFLIFFFLFFKTNLAFILIFLGFNMATLFFYLSTVKSFVNRKQASVLNSFNFFIRAELSFLYFFNFFYFFLFFAFFFLDSTFLIFLNLFF | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q33819 | MHRNILMVLIANVVLGTLIVLSSHHWFTLWVGLEMNTLSILPILSYQFTPRNVESSVKYFLVQSVSAGIVLNVVIIQAWLYSSWSLMEPLNQATSFLMTLALGLKLGLFPCHYWFPDVIQGVGFIQGLVLSTWQKIAPFAVLVYVVESLNISLLASLGVLSVLVGGWGGLNQTQMRKIFAFSSIAHIGWICSTVGYSVSVACVMLVAYIIINSSVFFMANSFDLKSLSHVGRLSLYNFVGGAGLVLSILSLGGLPPLFGFLIKFISLKCLVENGCFILAGVLVMGSLLSLFFYLRIAFNSSLTLFPQHSLVVFSWRSNRN... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P03897 | MNFALILMINTLLALLLMIITFWLPQLNGYMEKSTPYECGFDPMSPARVPFSMKFFLVAITFLLFDLEIALLLPLPWALQTTNLPLMVMSSLLLIIILALSLAYEWLQKGLDWTE | 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 of complex I .
Catalytic Activity: a ubiquinone + 5 H(+)(in) + ... |
Q34950 | MILTALSSAIALLVPIIILGAAWVLASRSTEDREKSSPFECGFDPKSTARIPFSTRFFLLAIIFIVFDIEIVLLMPLPTILHTSDVFTTVTTSVLFLMILLIGLIHEWKEGSLDWSS | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P16265 | MLEFAPICIYLVISLLVSLILLGVPFLFASNSSTYPEKLSAYECGFDPFGDARSRFDIRFYLVSILFIIFDLEVTFFFPWAVSLNKIDLFGFWSMMAFLLILFIGSLYEWKRGALDWE | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P26847 | MEFAPIFVYLVISLLLSLILIGVSFLFASSSSLAYPEKLSAYECGFDPFDDARSRFDIRFYLVSILFIIFDLEVTFLFPWAVSLNKIGLFGFWSMMVFLFILTIGFVYEWKKGALDWE | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q35100 | MYTEFYGILVLLIFSVVLSAIISGASYILGDKQPDREKVSAYECGFDPFGTPGRPFSIRFFLIGILFLIFDLEISFLFPWCVVCNQVFPFGYWTMIVFLAVLTLGLVYEWLKGGLEWE | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
B1X495 | MTIMLEAYLTLAAVLFCIGVWGLINSRNAVRVLMSIELMLNAVNINLMAFSNYLDGELIRGQVFAIFVITVAAAEAAVGLAILLSLYRNRQTVDMERFNLLRW | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
Q36423 | MSMFGLFTCLSIYFSGVYVFCSKRKHLLVVLLSLEYIVLSLFMLIVLFLVEFDYDYFFPVIFLVFSVCEGALGLSILVSMIRSHGNDFFNSFFLSLC | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q34948 | MYSSIMSLVFLLPIVAVVNLISNQSHFLMTLLSLEGITLSLVLFVPISLSIMSASNVSISVILLTFGACEASLGLSLMVLMSRSYGTDMLNSLTANKC | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
O79554 | MELMKMTLYTTFMITIIALSLQQKHLMLALMCVETMMLIVFTMLVMFNSNSLTVSQTPMPIILLTISVCGAAVGLSLVVAITRTHGNDFLKNLNLL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q9XL45 | MIPTYMNIMLAFTISLLGMLTYRSHLVASLLCLEGMMMSLFIMTTLIASNTHSPLINIMPIILLVFAACEAAVGLALLISISNTYGLDYIHNLNLLQC | 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.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location To... |
Q36903 | MRLTILLIIIGLIGYIINSGPLGRTNIIKLFISIEIMLLGVTLLIILSGYNNDDILGLIIGIIVLIITGIESAIGLTILVNYYKIKGSLPTNI | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P03904 | MTLIHFSFCSAFILGLTGLALNRSPILSILLCLEGMLLMSMDGIVLTPLHLTIYLSSMMLYIMLPFAAPEAATGLSLNSDHYTTHGTDKLFSLNLLEC | 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.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location To... |
Q9B6D4 | MFIGTIILVLSFLGFVFNRRNIILAFICLETMLLGINLILLRNSVLFDDISGSLFAIVIIILAGVESAIGLSLLVSYYRLRGVINSYGI | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q37375 | MAFLLYYTLFISFMLWLAALLIISFSVYGSPEKVKLIKKTSLFFSFFQFILIIFFWILSDNISVLAEFDIYNFQFYKQWLFLYNFHYVIGMDNISLLFLLLTFFLTPICILISWNSIKYRYNSFIICLIFITFILFNIFCVLDLVFFYIFFESILIPMFILIGVWGSRQRKIHAVYQLFFYTLLGSLLMLLGILVIYSHIQTTDIRVLYNTNFSFYRQLILWASFFFAFCVKVPLFPFHIWLPEAHVEAPTVGSVILAGVLLKLGTYGLLRFVIPIFCDATYFFLPLVYTLCLLGIIYTCCSTIRQVDLKKVIAYASVSH... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
B1VKJ3 | MEFIYKYAWIVPFLPLSASVPIGLGSLFFPGATKSVRRTWALISIFLLSVAMFLSFNLFLQQITGGPIYRYFWSWVINNKFSLELGYLIDPLTSIMLVLVTTVGTMVMIYSDNYMSHDKTYVRFFAYLNFFNASMLGLVISPNLLQIYIFWELVGMCSYLLIGFWFTRPSAANACQKAFITNRAGDFGLLLGILGFYWVTGSFEFQYLSEKLNELTAIDGVGSFFVTSCAFLLFLGPVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARLFPLFKALPLIMYLISWIGGITALLGATMALAQKDLKRGLA... | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
Q2QD43 | MEYTYQYSWIIPFISLPIPILIGVGLLLFPTATKNLRRLWSFPSILLLSIVMIFAVYLSIDQINTSYIYQYVWSWTINNDFSLELGYFIDPLTCIMAILITTVGIMVLIYSDNYMSHDQGYLRFFAYMSLFNTSMLGLVTSSNLIQIYIFWELVGMCSYLLIGFWFTRPTAANACQKAFVTNRVGDFGLLLGILGLYWTTGSFEFRDLFQIFNNLIDNNEVNFLFLTLCAVLLFAGAVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARLLPLFIAIPYIMNLIALIGIITVLFGATLALAQKDIKRSLA... | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
A6MMR6 | MEHTYQYAYIILFLPLPVTMSIGFGLLFVPTATKNIRRMWAFVSVLLLSMVMGFSVNLAIQQINGSFIYQYLCSWTINNDFSLEFGYLIDPLTSIMSLLISTVGIMVLMYSDNYMSHDQGYLRFFAYMSFFNTSMLGLVTSSNLIQIHIFWELVGMCSYLLIGFWFTRPIAASACQKAFVINRVGDFGLLLGILGFYWITGSLEFRDLFEIVNNLIHNNGVNFRFAILCACLLFLGAVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARLRPLFIVIPYIMNLISLIGIITLLLGATLALAQGDIKRSLA... | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
Q9ZZM3 | MHPTTLILSSTLLMIFALLLYPLITTLNPTPQQENWALTHVKTAIKMAFLVSLLPLFIFLDQGTETIVTNWQWMNTTTFDINLSFKFDHYSIIFTPIALYVTWSILEFASWYMHADPNMNRFFKYLLLFLIAMIILVTANNMFQLFIGWEGVGIMSFLLIGWWYGRADANTAAMQAVIYNRVGDIGLILSMAWFATNLNSWEIQQMFASSKELDLTLPLMGLILAATGKSAQFGLHPWLPSAMEGPTPVSALLHSSTMVVAGIFLLIRLHPLMENNQTALTTCLCLGALTTLFTATCALTQNDIKKIVAFSTSSQLGLMM... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P50368 | MNLIILFLPFVGAFISGFLGRFVGTTGAQILTCACILTSALLSLYYWLSINELIIGLFSFEGDQVYFTDWNFLSNNTFINLGTWVDSEYIKISWEFTFNEITLPFLFTVLFISFLIHLFSVNYMANDPHIQRFFSYLSLFTFFMAILVTGANYFVLFVGWEGIGVVSYLLINFWFTRIQANKAAILAFNTNRIGDMALSIAYFVMLPAFGSADFSTVFSLPAYINQTTITIIGFLLLVGAMAKSSQIPLHNWLPGSMEGPTPVSALIHAATLVTAGSYLLIRSSPILEYAPTVLLVITIIGASTAFFAATCGLVQNDIKR... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q9ZZ44 | MNMIIFNSAFLLIFIILLYPLISSLSPKELYPNWSSSHVKTAVKTSFFISLIPLFIYLDQGLESITTNWNWINIGPFDINMSFKFDMYSIIFTPVALYVTWSILEFALWYMHSDPNMNRFFKYLLLFLISMIILVTANNMFQLFIGWEGVGIMSFLLIGWWYSRADANTAALQAVIYNRVGDIGLILSMAWLAMNLNSWEIQQLFILSKDKDLTLPLLGLVLAAAGKSAQFGLHPWLPSAMEGPTPVSALLHSSTMVVAGIFLLIRLHPLMQDNQLILTTCLCLGALTTLFTAACALTQNDIKKIVAFSTSSQLGLMMVT... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P15552 | MVISPSLIISSLNLGILTILLGSIFFFSKSYFSKGNVNFPLIKTTSACLSVNNDKEETIEYNSGPFAMAILKVLAFLSVLSLLVTCNNSIQSINITLSLWLSNTPLNISLNFIYDQYFLVFLSVALIVTWSIMEFSFYYMTEDPNSSAFFRLLTIFLLNMLILTCSNSLFLIFLGWEGGGFLSFLLISWWTTRNDASSSALEAVITNRIGNIGLITFMALSALNFNSSNLTNILSSNENLTPLLPFLLFGLILAAAGKSAQFGLHPWLPALLEGPTPVSALLHSSTMVVAGVFLLVRTSELFSSPLITHSLVLILGGTTA... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P04540 | MFLIFFLFFIMFGFISGSFMFGRNFLSFWLSLVMIIFIVLCMIFSFLMVSVCLYGYYYYDFCLILMLDFCFIWLTYVCSGFYMFIMLLINMVFCFIVFYAFYYMYFDMLLGRFLIIFWIFVVCMNLFILSYDFLTAYCGWELLGLFSFFLISYFWYRFFALKFGFKAFFIGKIGDVLLIFAFSIIFLSNGFCMTTFYFLNFFCMDYYYIEFSICLLVGCAFTKSTQFGLHIWLPDAMEGPIPVSALIHAATLVVCGIILLSFVYWCFDFWFSYFYNLIGWSTLILILMTLCVFYNFDVKRYVAFSTICQISFSMFCCLCI... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q0H8X0 | MYLSLLLLPMFGSAVTGLLGRKIGVTGAHIITCSCLITSAILAIVAFYEVGLCNSSVSINLISWIDSELMDVSWGFMFDSLTVSMLLPVLVVSSLVHIFSVDYMSADPHNQRFFAYLSMFTFFMLVLVTGDNYLIMFVGWEGIGISSYLLINFWFTRIQANKSAIKALVVNRVGDMFLSIGFFAIFFVFGNLDYSTVFSIAPFINETIITIIGLLLLLAAMGKSAQLGLHTWLPDPSMEGPTPVSALIHAATLVTAGVYLLLRSSPVIEYGPTTLIVITWVGALTAFFAASTGLLQNDLKRVIAYSTCSQMGYLFMACGL... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q37024 | MILFITLPLLNVIISGLLSRYIGVNNIKRLNIINLFIILILLIYYYINIIKTDNEYTLKIIEWINIEYLNINYSFNLDLLSITMLIPIILISLIVNIFAWEYMKDDSHNPRFYTYLALFTLFMIILVLGDNYLILFLGWEYIGIASFLLIGFWYNNIDNIKSSLNALFINKIGDIFFIIALIYLIYIYKSLNYSLIFSLVSYINIDINNIIILCLVIAASAKSAQFGLHNWLIWAMAGPTPVSVLLHAATLVIAGIYLLMRSSPILENCPNILLFNLWLGAITSLISGLIAINSNDIKRIIALSTMSQLGIMFISIGLSS... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P03922 | MNFPLIFNSSMLITISILILPILMSTFNMNIMNLHHLIKTSVKTAFLISIIPLIIFLDQGLESITTNFHWMNINTFDINMSFKFDIYSSIFIPIALFVTWSILEFATWYMASDPMISRFFKYLLTFLVAMVILVTANNFFQFFIGWEGVGIMSFLLIGWWYARAEPNTAALQAVIYNRVGDIGLILSMAWVAMNLNSWEMQQVFMLNSDNLTLPLLGLILAATGKSAQFGLHPWLPAAMEGPTPVSALLHSSTMVVAGIFLLIRISPMMNNNQTALTICLCLGAMTTLFTAACALTQNDIKKIVAFSTSSQLGLMMVTIG... | 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 ... |
Q9B6D3 | MYNAISLIIILPCISWLFPLFFGRQLGYVFVTRMTSTLIIITTLITYYYFYQLLGNNNPINLELFNYLNIDYLDINYNFEIDALTITMLLAITTISSMVHIYSIGYMETDPHQVRFFSLLSMFTFWMIILVTGSNYFVLFVGWEFIGVTSYLLISFWVTRLQAMKSALSAVLMNRFGDAFFVLGLCVIAYVFGTLNYSTIFATAYLINTDLLVLIMLALFIAAMAKSAQFGLHNWLTLAMEGPTPVSSLLHAATLVTAGIYLLLRSANILEYTPTVLFIILWIGALTTLSAGLIAICSNDLKRIIALSTMSQLGMMTIAI... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q85FH2 | MNISELIHDFVLALVELGILLGSLGAVLLVNTVNSAFSLGLVFTCISLLYFVLNADFVAAAQLLVYVGAINVLTVFAVMITDEPAGSETTARGIGYIITAGTCTILFSILSFVIHNTKWSDLSLIPQSGISTSGTLGSNVQQLGYKLLGEFVIPFELLSILLLAALVGAINLARNEDAFIVNKKSAASAPYKNSTFF | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to prot... |
Q37626 | MDFLFYIFSSLTLISGSLVIQARNPVHSVLFLVLVFFNAAGLLVLLGLDFFALIFLVVYVGAIAVLFLFVVMMLNIRITEISEKRLRYLPVGGVLGVLFLFEICILIDNDCIPLLSYDIENTALLANYNQLSFIDWRMYLSTSHTIDALGSLLYTYYFYFFLVASLILLVAMIGAIVLTMQKGIRIKRQQVFLQNTRDFAKTIRKVA | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P03926 | MTNYMFILSLLFLTGCLGLALKPSPIYGGLGLIVSGCIGCLMVLGFGGSFLGLMVFLIYLGGMLVVFGYTTAMATEEYPETWGSNWFIFSFFVLGLFMELVVFYLFSLNNKVELVDFDSLGDWLMYEIDDVGVMLEGGIGVAAIYSCATWMMVVAGWSLFAGIFIIIEITRD | 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 ... |
O99827 | MLFSEIKFLIFMSVICLSSSHPILMLSSLILLTLFLSLIFYFIYQFSIMSMMMILIILGGMLIIFMYMISLCPNKKMSFYKKLSVTFTMMLILIPYDSFMTKLEMININKIYSVNFVNMIILMMIFLIVMLTIISKNLSWINAPIQKFN | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q9ZZM2 | MTYIVSLFLLGLVLGLVAVASNPAPYFAALGLVVAAGVGCGVLVGYGGSFLSLVLFLIYLGGMLVVFAYSAALAAEPFPESWGDRSVLGYVVVYTVGVMLVAGWFWSGWYETSWVVVDEFKEFSVLRGDTSGVALMYSYGGGMLIVCAWVLLLTLFVVLELTRGLSRGALRAV | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
O63849 | MNSLFMIFSLGIVGASLMVISTPNPVYSVFWLVIAFVNAAVMFISLGLDYIGLIFIIVYVGAIAILFLFVIMLIQQPNKIDSQDHSHFLPIGLSVIFLFYSLLTNSPKYISNPVIGSRTNIGAIGSHLYTTYYELVLIASLVLLVAMIGAILLAKQPNSPFLYNSHGESLRSRQDLFLQISREHL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
P15553 | MVVYVTLIVMLFGSTLVFYSLSPYYSALGLVVFSVPGSFVLSFLGSSFVPIVLFLVYIGGMLVVFPYSSAISPERFPSVNNLGEVVGLVFLFSSWVFMSFDNFQDLKNIFHCFVSGESLVGSNTFYNSGGVLVILGVFVLLVALVGALIISRGIESTIIRAIWLW | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
Q9YDF6 | MSQEASVDGRFGVASSPTIEEAAGLLEKLLDGSSMVVVAGVCSSEYEGRGASVSTEGDKLLIVKPGGAVILHGPRGFRPLNWQPSTSHTEVATADGLLTLKFYRRTPREVLKIACGSIWYIAWVRFPEEGAFWMYMTEDDLRKAVALHPRELLGEDIRFFAEEKRTPSGKADLYGVDERGNIVIVEVKRVRADESAVRQLEGYVRDYPTQAKVRGILVAPDISDAARRLLESRGLEFRRVDLKKAYSLLKPGRGRSVLDFL | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
Sequence Mass (Da): 28928
Sequence Length: 261
Subcellular Location: Cytoplasm
EC: 3.1.-.-
|
A1A3C3 | MRIIVADCSAEYSERLNASLPLAKRVLLIKADNSLLIFSELGSYKPLNWMSAPCSIRDITPDHADDDVDTEVPQKVIRASADKSNDVLEVTLQRIYSDESYDLGEDPGLIKDGVEDHLQKYLAEQIERIGKGAKLVRREYPTAIGPVDIMAIDGNGEHVAIEIKRNGGIDGVEQLTRYCDLLNRDPLLAPVHGIFAAQTITPQARVLAQDRGFKCLLLDYEEMKGTEDDSLRLF | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
Sequence Mass (Da): 26055
Sequence Length: 234
Subcellular Location: Cytoplasm
EC: 3.1.-.-
|
B3DTU8 | MRVIVADCSAEYSGRLNASLPLAKRVLLIKADSSLLIFSELGSYKPLNWMTAPCTIREIDPAAKSAQHSRESVAGGAVDGDSATHSPESVAAGEPEKVLRVSADKGSDILEVTLQHIYSDQTYDLGEDPGLIKDGVEDHLQRYLAEQIERIGKGAKLVRREYPTAIGPVDIMAVNAEGEHVAVEIKRHGGIDGVEQLTRYCELLNRDPLLAPVHGIFAAQTITPQAQVLAKDRGFTCLILDYDDMKGTEDDSLRLF | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
Sequence Mass (Da): 27867
Sequence Length: 256
Subcellular Location: Cytoplasm
EC: 3.1.-.-
|
C4LJL1 | MRLVIATCSVDYVGRLTAHLPKATRLLMVKADGSVSVHADDRAYKPLNWMTPPCTLTVHPIAIDDPDTDFTDGSSVGNSEEQGTDGSAHTAHEEELWVVENKKGEQLRITVHDKISDTTYDLGEDPGLTKDGVEAHLQELLAQHPEALGEGFTLVRREYPTPIGPVDILTRDASGKTVAVEVKRRGGIDGVEQLTRYVELLNRDEILAPVQGLFAAQEIKPQARTLAEDRGFTCVTVDYDELRGTPSQELRLF | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
Sequence Mass (Da): 27841
Sequence Length: 253
Subcellular Location: Cytoplasm
EC: 3.1.-.-
|
Q2J6P5 | MRLVIARCSVDYVGRLTAHLPSAVRLVLVKADGSVSIHADGRAYKPLNWMSPPCVIAEADGVWRVTNRAAEQLVITLEQVLHDSTHDLGVDPGLRKDGVEAHLQVLLADRPDAIAPGLTLVRREYETGIGPVDLLCRDADGSTVAVEIKRRGEIDGVEQLTRYLVRLEADPALPHPVRGILAAQSITPQARLLAADRGLGCAVVDYDELRGLEPSIPTLF | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
Sequence Mass (Da): 23841
Sequence Length: 220
Subcellular Location: Cytoplasm
EC: 3.1.-.-
|
P00644 | MLVMTEYLLSAGICMAIVSILLIGMAISNVSKGQYAKRFFFFATSCLVLTLVVVSSLSSSANASQTDNGVNRSGSEDPTVYSATSTKKLHKEPATLIKAIDGDTVKLMYKGQPMTFRLLLVDTPETKHPKKGVEKYGPEASAFTKKMVENAKKIEVEFDKGQRTDKYGRGLAYIYADGKMVNEALVRQGLAKVAYVYKPNNTHEQHLRKSEAQAKKEKLNIWSEDNADSGQ | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond.
Catalytic Activity: Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.
Sequence Mass (Da): 25471
Sequence Length: 231
... |
P43270 | MKKITTGLIIVVAAIIVLSIQFMTESGPFKSAGLSNANEQTYKVIRVIDGDTIIVDKDGKQQNLRMIGVDTPETVKPNTPVQPYGKEASDFTKRHLTNQKVRLEYDKQEKDRYGRTLAYVWLGKEMFNEKLAKEGLARAKFYRPNYKYQERIEQAQKQAQKLKKNIWSN | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5'-position of the phosphodiester bond.
Catalytic Activity: Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.
Sequence Mass (Da): 19472
Sequence Length: 169
... |
Q6NPD7 | MSDQEAPLRNGVEHKIFEVLPFVDDDYGGVIVEMKTPMDTKNFVAALRDSFEQWRLQGKKGVWLNLPLSHVNLVEPAVKEGFRYHHAEPTYLMLVYWIPEAESTIPLNASHRVRVGAVVLNHNKEEKYGSLCGSGIWKIPTGVVDEGEEIFAAAIREVKEETGIDTEFLEILAFCQTHESFFAKSDLFFVCLLRPTSFDIQKQDLEIEAAQWMRFEDSASQPITHKNDLFKDIHHICSMKMEKSYSGFSKKPITTFFDDKLGYLYLNKQEDMEQPIS | Function: May mediate the hydrolysis of some nucleoside diphosphate derivatives. In vitro, uses both ADP-ribose and NADH as substrates; however the relevance of such substrates in vivo is unclear.
Catalytic Activity: ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+)
Sequence Mass (Da): 31816
Sequence Length: 277... |
Q8NFP7 | MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPGGAAVREVYEEAGVKGKLGRLLGVFEQNQDPKHRTYVYVLTVTELLEDWEDSVSIGRKREWFKVEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSMAPSSPDSDP | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit. Mn(2+) may be the true cofactor in vivo.
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside ... |
Q8LET2 | MSSTTTDSTELQNLIKLFQNCQTHPRQHFPAKSSAVLVCLYQEQREDKNELRVILTKRSTTLSSHPGEVALPGGKRDQEDKDDIATALREAREEIGLDPSLVTIISVLEPFVNKKGMSVAPVIGFLHDKKAFKQLPNPAEVEEIFDVPLEMFLKDRNRRAEEREHEGERYLLQYFDYYSEDKERSFIIWALTAGILIRVASIVYQRLPEFQERKPSFWNQPN | Function: Coenzyme A diphosphatase which mediates the cleavage of CoA into 3',5'-ADP from CoA and 4'-phosphopantetheine. Can use malonyl-CoA, hexanoyl-CoA, lauroyl-CoA, myristoyl-CoA and palmitoyl-CoA as substrates, but not isobutyryl-CoA or propionyl-CoA.
Location Topology: Single-pass membrane protein
Sequence Mass (... |
Q96G61 | MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPGGAAVREVYEEAGVKGKLGRLLGVFEQNQDRKHRTYVYVLTVTELLEDWEDSVSIGRKREWFKVEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSMAPSSPDSDP | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit. Mn(2+) may be the true cofactor in vivo.
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside ... |
Q93ZY7 | MSVLSSRTGRDRQRYDNNFRLVSGCIPYRLMKADETEEDSGVDFVNKLEVLMVSSPNRHDLVFPKGGWEDDETVLEAASREAIEEAGVKGILRELPLGVWEFRSKSSTVEDECLGGCKGYMFALKVTEELEDWPERKNRERRWLTVKEALELCRYEWMQRALEEFLRVMEDERRLRTEEETVHDSSKLEEESQIDPWYCFVVN | Function: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives.
Sequence Mass (Da): 23869
Sequence Length: 203
Subcellular Location: Mitochondrion
EC: 3.6.1.-
|
Q9BQG2 | MSSVKRSLKQEIVTQFHCSAAEGDIAKLTGILSHSPSLLNETSENGWTALMYAARNGHPEIVQFLLEKGCDRSIVNKSRQTALDIAVFWGYKHIANLLATAKGGKKPWFLTNEVEECENYFSKTLLDRKSEKRNNSDWLLAKESHPATVFILFSDLNPLVTLGGNKESFQQPEVRLCQLNYTDIKDYLAQPEKITLIFLGVELEIKDKLLNYAGEVPREEEDGLVAWFALGIDPIAAEEFKQRHENCYFLHPPMPALLQLKEKEAGVVAQARSVLAWHSRYKFCPTCGNATKIEEGGYKRLCLKEDCPSLNGVHNTSYPR... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA . The NAD-cap is present at the 5'-end... |
Q52K88 | MSNLSARTGRDHQRYDNNFRLVSGCIPYRLVKDEEEDSTSVDFENKLQVLMISSPNRHDLVFPKGGWEDDETVLEAASREAMEEAGVKGILREDPLGVWEFRSKSSSVEADCCLGGGCKGYMFALEVKEELAIWPEQDDRERRWLNVKEALELCRYEWMQSALEEFLRVMAEEGSTKEDSLAISSISNRGERQIDPRYCFVV | Function: Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can use diadenosine 5',5'''-P(1)P(6) hexaphosphate (Ap(6)A), diadenosine 5',5'''-P(1)P(5) pentaphosphate (Ap(5)A) and adenosine tetraphosphate (p(4)A) as substrates, but not diadenosine 5',5'''-P(1)P(4) tetraphosphate (Ap(4)A), diadenosine 5'... |
Q86X67 | MSLYCGIACRRKFFWCYRLLSTYVTKTRYLFELKEDDDACKKAQQTGAFYLFHSLAPLLQTSAHQYLAPRHSLLELERLLGKFGQDAQRIEDSVLIGCSEQQEAWFALDLGLDSSFSISASLHKPEMETELKGSFIELRKALFQLNARDASLLSTAQALLRWHDAHQFCSRSGQPTKKNVAGSKRVCPSNNIIYYPQMAPVAITLVSDGTRCLLARQSSFPKGMYSALAGFCDIGESVEETIRREVAEEVGLEVESLQYYASQHWPFPSGSLMIACHATVKPGQTEIQVNLRELETAAWFSHDEVATALKRKGPYTQQQN... | Cofactor: Divalent metal cations. Mg(2+) or Mn(2+).
Function: NAD(P)H pyrophosphatase that hydrolyzes NADH into NMNH and AMP, and NADPH into NMNH and 2',5'-ADP. Has a marked preference for the reduced pyridine nucleotides. Does not show activity toward NAD-capped RNAs; the NAD-cap is an atypical cap present at the 5'-e... |
Q8JZU0 | MSLYCRTFFRRKSFGCYRLLSTYVTKARYLFELKEDEEACRKAQKTGVFYLFHDLDPLLQASGHRYLVPRLSRAELEGLLGKFGQDSQRIEDSVLVGCSEQQEAWFALDLGLKSASSSRASLPKSEMEAELGGSFIKLRQALFQLNSVDSSLLFTAQALLRWHDGHQFCSKSGQPTQKNVAGSKRVCPSSKIIYYPQMAPVVITLVSDGARCLLARQSSFPKGLYSALAGFCDIGESVEETVHREVAEEVGLEVENIQYSASQHWPFPNSSLMIACHATVKPGHTEIQVNLKELEAAAWFSLDEVTTALRRKGSLALQPS... | Cofactor: Divalent metal cations. Mg(2+) or Mn(2+).
Function: NAD(P)H pyrophosphatase that hydrolyzes NADH into NMNH and AMP, and NADPH into NMNH and 2',5'-ADP . Has a marked preference for the reduced pyridine nucleotides . Does not show activity toward NAD-capped RNAs; the NAD-cap is an atypical cap present at the 5'... |
Q9CA40 | MSTGEAIPRVAVVVFILNGNSILLGRRRSSIGNSTFALPGGHLEFGESFEECAAREVMEETGLKIEKMKLLTVTNNVFKEAPTPSHYVSVSIRAVLVDPSQEPKNMEPEKCEGWDWYDWENLPKPLFWPLEKLFGSGFNPFTHGGGD | Cofactor: Magnesium may be the real cofactor in vivo.
Function: Mediates the hydrolysis of some nucleoside diphosphate derivatives. Its substrate specificity is unclear. In vitro, it can use NTP, dNTP, 8-oxo-GTP, 8-oxo-dGTP, dGTP, dATP, dTTP or dihydroneopterin triphosphate (DHNTP) as substrate. Has some NADH pyrophosp... |
M4I1C6 | MGNETVVVAETAGSIKVAVVVCLLRGQNVLLGRRRSSLGDSTFSLPSGHLEFGESFEECAARELKEETDLDIGKIELLTVTNNLFLDEAKPSQYVAVFMRAVLADPRQEPQNIEPEFCDGWGWYEWDNLPKPLFWPLDNVVQDGFNPFPT | Function: Involved in a cytosolic pathway for the biosynthesis of free monoterpene alcohols that contribute to fragrance. Lacks terpene synthase activity, but has a diphosphohydrolase activity with geranyl diphosphate and farnesyl diphosphate as substrates. No activity with 8-oxo-dGTP and dGTP and unable to dephosphory... |
Q94B74 | MSASSSSTNPMSREDATTLLPSVQDKYGGVMTEMTHPMDPSLFSTLLRSSLSTWTLQGKKGVWIKLPKQLIGLAETAVKEGFWFHHAEKDYLMLVYWIPKEDDTLPANASHRVGIGAFVINHNKEVLVVQEKTGRFQGQGIWKFPTGVVNEGEDIHDGSVREVKEETGVDTEFDQILAFRQTHKAFFGKSDLFFVCMLKPLSLEINAQESEIEAAQWMPWEEYINQPFVQNYELLRYMTDICSAKTNGDYEGFTPLRVSAPDQQGNLYYNTRDLHSRN | Function: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. In vitro, it can use both NADH and ADP-ribose as substrates; however the relevance of such substrates in vivo is unclear. Confers tolerance to oxidative stress .
Catalytic Activity: ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2... |
A2VE79 | MMKLKSNQTRTYDGDGYKKRAACLCFRSESEEEVLLVSSSRHPDRWIVPGGGMEPEEEPGTAAVREVCEEAGVKGTLGRLVGIFENQERKHRTYVYVLIVTEVLEDWEDSVSIGRKREWFKIEDAINVLQCHKPVQASYFETLRQGYSANNGTPLVAPTYSVSAQSSMPGIR | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction (By similarity). InsP6 (inositol hexakisphosphat... |
O95989 | MMKLKSNQTRTYDGDGYKKRAACLCFRSESEEEVLLVSSSRHPDRWIVPGGGMEPEEEPSVAAVREVCEEAGVKGTLGRLVGIFENQERKHRTYVYVLIVTEVLEDWEDSVNIGRKREWFKIEDAIKVLQYHKPVQASYFETLRQGYSANNGTPVVATTYSVSAQSSMSGIR | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction . InsP6 (inositol hexakisphosphate) is not a sub... |
Q566C7 | MMKLKSNQTRTYDGDGYKKRAACLCFRSESEEEVLLVSSSRHPDRWIVPGGGMEPEEEPSVAAVREVCEEAGVKGTLGRLVGIFENQERKHRTYVYVLIVTEVLEDWEDSVNIGRKREWFKIEEAVKVLQYHKPVQASYFEALRQGYSANNGTPVLPTTYSSSMSGIR | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction . InsP6 (inositol hexakisphosphate) is not a sub... |
Q9LE73 | MTGFSVSLFVSNLSNVASYLSPIFENIPSTKVVPAQIEKVVSLVSRTGRDLQRYDHAGYRQVVGCVPYRYKKQEVNGVETQVIQVLLVSAQKGKGMLFPKGGWETDESMEEAALRETIEEAGVTGELEEKLGKWQYKSKRHSIIHDGYMFALLVSQEFERWPEAEMRQRRWVSLDEAREVCQNWWMREALEAFINLKCLADDDESGN | Function: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. In vitro, it can use both NADH and ADP-ribose as substrates; however the relevance of such substrates in vivo is unclear.
Catalytic Activity: ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+)
Sequence Mass (Da): 23701
Sequence... |
Q9NZJ9 | MMKFKPNQTRTYDREGFKKRAACLCFRSEQEDEVLLVSSSRYPDQWIVPGGGMEPEEEPGGAAVREVYEEAGVKGKLGRLLGIFENQDRKHRTYVYVLTVTEILEDWEDSVNIGRKREWFKVEDAIKVLQCHKPVHAEYLEKLKLGCSPANGNSTVPSLPDNNALFVTAAQTSGLPSSVR | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction . Can also catalyze the hydr... |
Q8R2U6 | MKFKPNQTRTYDREGFKKRAACLCFRSEQEDEVLLVSSSRYPDQWIVPGGGMEPEEEPGGAAVREVYEEAGVKGKLGRLLGIFENQDRKHRTYVYVLTVTEILEDWEDSVNIGRKREWFKVEDAIKVLQCHKPVHAEYLEKLKLGCSPTNGNSSVPSLPDNNALFVTAAPPSGVPSSIR | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction (By similarity). Can also ca... |
Q6N1Y8 | MGDLTLPINSGAALAIHVALSAGIVAAIIVVAAWLREKRSGARPDVPYEGGVLPAQPQQGPLNAPYFLIAALFVIFDMEAAILFAWAVAARDAGWLGLIEAAVFIGVLLLALVYLWLDGALDWVKGKRR | 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 ... |
Q92ID5 | MLQNSELLQEYLPIAIFFGIAVLVSGLIMILPNLLSTKKYNKDKLEPYECGFEPFSDARSKFDICFYLVAILFIIFDLEIAFLVPWAISLNTIGKIGFFSMMFFLFVLIIGFIYEWKKGALDW | 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 ... |
A7NL04 | MLADYAFIGVFFIGAVIFPLVPLVAAYFLGPKRPTPIKLDTYECGLEAVGDIRVQFKIQYYLYALAFVIFDIEVVFLYPWAVAYGQIGLFALIAMAIFLVILVGGLVYEWKKGALEWV | 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 ... |
O67334 | MVAINSNGFVTTTVEELLRWGRRNSLWPVTIGLACCAIEMMHTAASRFDLDRLGVIFRASPRQADVLIVAGTVVNKVAPMLKLIWDQMPDPKWCISMGGCASAGGPFPTYSTLQGVDRIIPVDVYIPGCPPTPQGLIYGILQLQRKIKEQGITKYDKLFADFNREIEKEGIFVPRELKV | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), a... |
A7GV50 | MAINFEELHPQEQAELERNIFFTTLEQIKGWARSNSLWPMTFGLACCAIEMMGVGSSHYDLDRFGSFFRTSPRQSDVMIVSGTVTKKMAPIVRRLYDQMPEPKWVIAMGSCATAGGPYVNSYAVVKGVDQIVPVDVYIPGCPPNPAALIYGINKLKEKIRYEAKTGKQVTNK | Cofactor: Binds 1 [4Fe-4S] cluster.
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 tw... |
A0QU35 | MGLEERLPGGILLSTVETVAGYVRKGSLWPATFGLACCAIEMMSTAGPRFDIARFGMERFSATPRQADLMIVAGRVSQKMAPVLRQIYDQMVEPKWVLAMGVCASSGGMFNNYAVVQGVDHVVPVDIYLPGCPPRPEMLLHAILKLHDKIQQMPLGVNREEAIREAEQAALAVPPTIELKGLLR | Cofactor: Binds 1 [4Fe-4S] cluster.
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 tw... |
Q1D8S3 | MADADLANIVTTRRDESMGWLQSIVSKGLGWARKYSLFTYPYATACCGMEYMSVAASRHDISRFGAEFPRFSPRQADLLMVVGTINLKQAPILKRVYEQMAEPKWVVAFGVCASSGGFYDNYAVLQGIDRIIPVDVYIPGCPPRPEQVLDGLMLLQDKIGNQVHRIAEREEANPTAARHNLLLSMNK | Cofactor: Binds 1 [4Fe-4S] cluster.
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 e... |
Q9PGJ4 | MGVIQAIDRLMTNPIPDGQVDDILRPQGESPLLQKGYVTTSVDALLNWARTGSMWPMTFGLACCAVEMMHAGAARLDLDRYGIVFRPSPRQSDVMIVAGTLVNKMAPALRKVYDQMPDPKWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALVYGILQLQKKIWRTQTNAG | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), a... |
O68854 | MSEALNELASYLREARGALIADAEVKYGELTVTAKAENLIALLTFLRDDVQCGFVSFIDVCGVDYPQRPDRFDVVYHLLSPRQNQRVRVKVATGENDPVPSATSVFPGADWFEREAYDMYGILFTGHPDLRRILTDYGFEGYPLRKDFPLTGFVEVRYDNEAKRVVYEPVELKQEFRNFDFLSPWEGTEYVLPGDEKARPR | 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 ... |
P56896 | MTGERPVHLTAIIGSFGGAVENLGAAHGIYAFAVPPEQIVEFCRFLKEHPALEFDFLSDICGVDHYPETPRFETVYHLYSLKNKWRVRIKCRLGEPPHVPTVTGVWRTANWHEREAWDMYGIRFEGHPDLRRIYMWEGFEGFPQRKDFPLRGYKDKLNPFGAEGPPPTQPDLATNDIPQGGR | 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 ... |
Q5ZRU0 | MTKNEYLIEKLQADLANHITELTSAYGEVTIECEVQNLLPVMIELRDREEFSFDQLIDLCGVDYLHYGDYDWETESATEHGFSRGVERQEAKAYAVNKPRFAVVYHLLSTKKNHRLRVKLFVEESHLIVPSVHHLWKSANWFEREAYDLYGILFDGHPDLRRLLTDYGFIGHPFRKDFPLSGEVEMRYDAKLQKVIYAPVDIVPRIVVPKVIRNDNRYIGNEGSKND | 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 ... |
B1ZA44 | MEAITTNGITLRRTVAAAQGDDALRAMGERITGALGPAVTDWSIAHGELTLIVQGSDIVYALTYLRDDPNCAFRCFIDICGVDYPQRARRFDVVYHLLSLRHNMRVRVKVQTDAATPVPSAIPVFPAANWFERETYDLYGILFSGHPDLRRLLTDYGFEGHPLRKDFPLTGFVEVRYDQDEARVVYEPVKLTQEFRNFDFLSPWEGTDYVLPGDEKKSS | 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 ... |
Q2RJU5 | MDNFIQELQRLFPDLEVREGVDVPALVVPADQLLALMTELKEKRGFNFLADLTAVDYPEDERIEMVYHLLSVPGMAEIRVKVNLDRQHPEVPSLTALWPAANVQEREAFDLMGVKFPGHPDLKRILCPDDFVGHPLRKDFRLQTEGGE | 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 hydrog... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.