ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q2GDD8 | MKKTNFLSFGCYLPKKVLTNFDLEELVDTSDEWILRRTGIKTRYIAEEEDVCELAFRASLNCLERAMHFSQKEVDAIIVATCTANKRLPAVANMLQARLGIGRHILSFDVNAACTGFLYALSIVDAMIVSGKVSTVLLVGAEAMSTIIDWNDRNTCVLFGDGAGAVLVSAGDSGGVLYEHMACDSSLGEALLAEVGGTLKMDGRSVFEAAIKRLTLAIGEALKTTGISVEELDYFIMHQANIRIIELIGEKIGIDRSKIIVTVDRYANTSAASIPITLAYMDSHGSIRKGAKILFAAMGAGFTYGVTIFEY | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q82U60 | MYSRIIGTGSYLPEKVLTNQDLESMVDTSDEWIRTRTGIERRHIAAEGQMASDLALEASRNAIEAADIQAKDIDLIIVATTTPDMIFPSTACILQNKLGMSNGPAFDVQAVCSGFIYALATADMFVSSGKARNALVVGAEVYSRIMDWNDRSTCVLFGDGAGAVILTRDQKPGILSSHLHADGSYSQVLTAPASIHSGKIQGTPFITMEGGTVFKFAVKVLEEAALEALQANQLQPSDIDWLIPHQANIRIITSTAKKLGIPEEKVVATVSQHGNTSAASVPLALDQAVRDGRIQPDQHIVLEGVGGGFTWGSVLVRW | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q04DM7 | MRTIKIIQTASQLPEKIVSNDDLAGMMDTSDEWIRSRTGIFKRHIAVDETTASLAASVLQKLLKGSGISADQIDFVLVATMSPDSMAPSTAAQASALAGLSNAFAMDINVACSGFVYGLTLAHGLVNTLGSHYGVVIGAETLSKLVDWQERSTAVLFGDGAAGVLVEAVDGPERLLAADLKTFGKEAKSLTAGHLWSSTTWNQPEKGSRYFQMDGHAVYSFATRQVAASIKRTFEKISADIGDTDYFLLHQANQRIIDKVADLLKQPADRFLSNLSKYGNTSAASIPLLLDEMVTGNIVKSGQLLTLSGFGAGLSVGSIV... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q30YM1 | MTTKSYILGFGSHAPERILTNTDMEAFVDTTDEWITTRTGIKQRHIAAEGETTSDLGAKAALQALANAGLHADALTHILVATCTPDAMCPSTACLIEHKLGVSGLMALDLNAACSGFLYALNMAQGIVALTPDAKVLVVAAEVLSRRINWNDRSTCVLFGDGAGAVIVGSHPNEGRAVEVADSLLSSDGALGDLLLISGGGTSVPYKHGQPVGDEFFVRMEGREIFKHAVRSMARVCEELLERNGIAREDVDMLLPHQANLRIIEAVGKKLGIPADKVFVNLQEYGNTSAASVPLALADADSKNLLPPGRTVLLTTFGGG... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
A1B364 | MRRAIVRGTGHYLPERVVENSWFEDKLDTSDEWIRARTGIERRHFAAEDQRTSDLGILAAQAALADAGLEAAQIDAVIVATSTPDLTFPSVATMVQAGLGMRHGFAYDLQAVCAGFVYALANADALIRAGLADRVLLIGAETFSRIMDWTDRGTCVLFGDGAGAVVLEAAEGQGSSADRGILATDLNSDGQYRDLLYVDGGVASTGTAGHLRMQGNLVFRHAVEKLADTAHRALDRAGLTPDQVDWLVPHQANLRIIEATAKRMHLPMEKVVLTVADHGNTSAASIPLALSVANAEGRFKPGDLLVAEAIGGGLAWGSVV... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
P44432 | MGFLTGKRILVTGLASNRSIAYGIAKSMKEQGAELAFTYLNDKLQPRVEEFAKEFGSDIVLPLDVATDESIQNCFAELSKRWDKFDGFIHAIAFAPGDQLDGDYVNAATREGYRIAHDISAYSFVAMAQAARPYLNPNAALLTLSYLGAERAIPNYNVMCLAKASLEAATRVMAADLGKEGIRVNAISAGPIRTLAASGIKNFKKMLSTFEKTAALRRTVTIEDVGNSAAFLCSDLASGITGEIVHVDAGFSITAMGELGEE | Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).
Catalytic Activity: a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[A... |
O24990 | MGFLKGKKGLIVGVANNKSIAYGIAQSCFNQGATLAFTYLNESLEKRVRPIAQELNSPYVYELDVSKEEHFKSLYNSVKKDLGSLDFIVHSVAFAPKEALEGSLLETSKSAFNTAMEISVYSLIELTNTLKPLLNNGASVLTLSYLGSTKYMAHYNVMGLAKAALESAVRYLAVDLGKHHIRVNALSAGPIRTLASSGIADFRMILKWNEINAPLRKNVSLEEVGNAGMYLLSSLSSGVSGEVHFVDAGYHVMGMGAVEEKDNKATLLWDLHKEQ | Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).
Catalytic Activity: a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[A... |
Q9K151 | MGFLQGKKILITGMISERSIAYGIAKACREQGAELAFTYVVDKLEERVRKMAAELDSELVFRCDVASDDEINQVFADLGKHWDGLDGLVHSIGFAPKEALSGDFLDSISREAFNTAHEISAYSLPALAKAARPMMRGRNSAIVALSYLGAVRAIPNYNVMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASGIADFGKLLGHVAAHNPLRRNVTIEEVGNTAAFLLSDLSSGITGEITYVDGGYSINALSTEG | Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).
Catalytic Activity: a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[A... |
Q9ZFE4 | MGFLTGKRALIVGVASKLSIASGIAAAMHREGAELAFTYQNDKLRGRVEEFASGWGSRPELCFPCDVADDSQIEAVFAALGKHWDGLDIIVHSVGFAPGDQLDGDFTAVTTREGFRIAHDISAYSFIALAKAGREMMKGRNGSLLTLSYLGAERTMPNYNVMGMAKASLEAGVRYLAGSLGAEGTRVNAVSAGPIRTLAASGIKSFRKMLAANERQTPLRRNVTIEEVGNAGAFLCSDLASGISGEILYVDGGFNTTAMGPLDDD | Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).
Catalytic Activity: a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[A... |
Q9X450 | MSIPTVKAKLLQGRKGLIVGIANDRSIAWGRARAFRALGAEIAVTYLNDKALPLV | Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).
Catalytic Activity: a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[A... |
Q1RH28 | MTTGLLQGKRGIITGIANNMSISWAIAQLARKHGAELCFTYQSEILEKRVKPLAEEVGCNFVSELDVTNPESITNLFAEVKEKWGTFDFLLHGMAFSDRNELKGRYIDTSLGNFNNSLHISCYSLVELAREAEKLMNDGGSIVTLSYYGAEKVIPNYNVMGVAKAALEASVRYLANDMGENNIRVNAISAGPIKTLSGSVIGDFNSMLRSHAATAPLKRNTLQQDVAGAAVYLFSQLASGVTGEIHYVDCGYNVMGSNKIVG | Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).
Catalytic Activity: a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[A... |
Q9ZDG4 | MTTGLLQGKKGLITGIANNMSISWAIAQLAKKHGAELWFTYQSEVLEKRVKPLAEEIGCNFISELDVTNQKSISNLFNDIKEKWNSFDFLLHGMAFANKNELKGRYVETSLENFHNSLHISCYSLLELSRSAETLMHNGGSIVTLTYYGAEKVIPNYNIMGVAKAALEASVKYLANDMGENNIRVNAISAGPIKTLASSAISDFSTMLKSHAATAPLKRNITQEDVGGAAVYLFSELSKGVTGEIHYVDCGYNIIGSSKLL | Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).
Catalytic Activity: a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[A... |
P16657 | MGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSSIVLPCDVAEDASIDAMFAELGNVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKVAHDISSYSFVAMAKACRTMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIAAMNELELK | Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis (By similarity).
Catalytic Activity: a 2,3-saturated acyl-[... |
Q2FZQ3 | MLNLENKTYVIMGIANKRSIAFGVAKVLDQLGAKLVFTYRKERSRKELEKLLEQLNQPEAHLYQIDVQSDEEVINGFEQIGKDVGNIDGVYHSIAFANMEDLRGRFSETSREGFLLAQDISSYSLTIVAHEAKKLMPEGGSIVATTYLGGEFAVQNYNVMGVAKASLEANVKYLALDLGPDNIRVNAISASPIRTLSAKGVGGFNTILKEIEERAPLKRNVDQVEVGKTAAYLLSDLSSGVTGENIHVDSGFHAIK | Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). It has a preference for a long chain (C12) substrate compared to the shorter (C4) acyl group. Involved in the elongation cycle of fatty acid which are used in the lipid metabol... |
P71079 | MEQNKCALVTGSSRGVGKAAAIRLAENGYNIVINYARSKKAALETAEEIEKLGVKVLVVKANVGQPAKIKEMFQQIDETFGRLDVFVNNAASGVLRPVMELEETHWDWTMNINAKALLFCAQEAAKLMEKNGGGHIVSISSLGSIRYLENYTTVGVSKAALEALTRYLAVELSPKQIIVNAVSGGAIDTDALKHFPNREDLLEDARQNTPAGRMVEIKDMVDTVEFLVSSKADMIRGQTIIVDGGRSLLV | Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). It confers resistance to triclosan.
Catalytic Activity: a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] + H(+) + NADPH
Sequence Mass (Da): 27178
Sequence Length: 250
... |
Q93HE4 | MKPTGRGYLLLDAHPVGCFRSVELMRAEVPVPEKPPARRPTALVIGSSSGYGLASTIAGLVRYGIDGVGIGLERPAGHRSATAGWYRTVATDAIARELGADFSFRNADAFADTTKTETLDLLAERFGGVDYLIYSVAAPRRTDPRSGTTYQSVLKPLGAPHTTRNLEFADDGAAQVREVTVAPATEAEAAATVGVMGGEDWSRWITALAERGLLRSGFRTVALTYIGSPLTSAIYRGGTIGAAKAHLESTARALTERLAAVDGRAFTSVNGALVTQALTAIPGIPLYVSLLRGVLGDRFPSPVAQSLDLWHQLTARRPDV... | Function: Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP).
Catalytic Activity: a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + ... |
Q73Q47 | MIVKPMVRNNICLNAHPQGCKKGVEDQIEYTKKRITAEVKAGAKAPKNVLVLGCSNGYGLASRITAAFGYGAATIGVSFEKAGSETKYGTPGWYNNLAFDEAAKREGLYSVTIDGDAFSDEIKAQVIEEAKKKGIKFDLIVYSLASPVRTDPDTGIMHKSVLKPFGKTFTGKTVDPFTGELKEISAEPANDEEAAATVKVMGGEDWERWIKQLSKEGLLEEGCITLAYSYIGPEATQALYRKGTIGKAKEHLEATAHRLNKENPSIRAFVSVNKGLVTRASAVIPVIPLYLASLFKVMKEKGNHEGCIEQITRLYAERLY... | Function: Involved in the fatty acid synthesis (FAS II). Catalyzes the reduction of the carbon-carbon double bond of crotonyl-CoA to yield butyryl-CoA. In vitro it can also use hexenoyl-CoA and dodecenoyl-CoA as substrates .
Catalytic Activity: a 2,3-saturated acyl-CoA + NAD(+) = a (2E)-enoyl-CoA + H(+) + NADH
Sequence... |
Q6AJ07 | MSDVITPGEIDIVGILDLLPHRYPFVMVDRILSIDPGKEIVGLKNVTFNEQYFQGHFPGEPVMPGVLMLEGLAQVGCVHAFYTEPDAVGKKLAFFAGVDKARFRKPVRPGDQLIYKVQLVKEKRSIIFMSAKGYVDDQVVVQAELMASFS | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 16687
Sequence Length: 150
Subcellular Lo... |
A5EV60 | MGIEEIRRYLPHRYPFLLIDRIIALETQNYIHALKNVTANEPFFQGHFPNKAVMPGVLVVEAMAQAAGILGVKSAKAAAGLPDEPEEDGIYFFVGIDKARFRKTVVPGDQLILEVKLLRSRRGIWSFDARATVDDAVVCTAEIMCTSAGKGAA | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 16788
Sequence Length: 153
Subcellular Lo... |
A8LK44 | MNAKDNETAEFETTADLAMIQRILPHRYPFLLVDKVIDMVRFKSALGIKNVTFNEPHFQGHFPGEPIMPGVMIVEALAQTSAVLVGHSMASADEDVSVYFMSIDNCKFRRKVVPGDVMSLRVETMRGKPGGKVWKFLGEAIVEDTVAAQAEFTAMISFPQAAA | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17979
Sequence Length: 163
Subcellular Lo... |
A7ZHS0 | MTTNTHTLQIEEILELLPHRFPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGKLEPGELYYFAGIDEARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALVDGKVVCEATMMCARSREA | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
PTM: The N-terminus is blocked.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17033
Seq... |
A8H6K5 | MSNQLNTMDIKEILKFLPHRYPFLLIDRVLDFTPGETLHAIKNVTINEPFFQGHFPVQPVMPGVLILEAMAQATGLLAFKTMSEEPSNDALYYFAGIDKARFKRVVEPGDQLHFEVQMIKERRGIGVFTGVAKVDGEVVCSAEIMCARREISK | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17271
Sequence Length: 153
Subcellular Lo... |
A0KZ12 | MSNQMNTMDITEILKYLPHRYPFLLIDRVLDYTPGESLHAIKNVTINEPFFQGHFPVQPVMPGVLILEAMAQATGLLAFKTMSDDVPPPGVLYYFAGIDNARFRRVVEPGDQIHFEVKMIKERRGIGVFYGEAKVDGEVVCSAEIMCARREINQ | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17447
Sequence Length: 154
Subcellular Lo... |
A8FY31 | MSNQLNTMDIKEIMNSLPHRYPFLLIDRVLDYTPGETLHAIKNVTINEPFFQGHFPIQPVMPGVLILEAMAQATGLLAYKTMEAAVTDDSLYYFAGIDKARFKRVVEPGDQLHFEVKMVKERRGIGVFTGVVKVDGELVCSAEIMCARREIKK | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17289
Sequence Length: 153
Subcellular Lo... |
Q01T92 | MAILDINEIRAILPHRYPFLLVDRILEMETDRIVGIKNVTFNEPQFTGHFPDFPVMPGVMIVEAMAQTAGVLVLHSMPDRANKLVLLVAIENARFRKPVVPGDTLRMEMKIIKRKASVAKMAGIATVDGVVVAEAEVMCKLADKEEKPPAAPEIKVPAEAAV | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17808
Sequence Length: 162
Subcellular Lo... |
P46310 | MANLVLSECGIRPLPRIYTTPRSNFLSNNNKFRPSLSSSSYKTSSSPLSFGLNSRDGFTRNWALNVSTPLTTPIFEESPLEEDNKQRFDPGAPPPFNLADIRAAIPKHCWVKNPWKSLSYVVRDVAIVFALAAGAAYLNNWIVWPLYWLAQGTMFWALFVLGHDCGHGSFSNDPKLNSVVGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESWHPMSEKIYNTLDKPTRFFRFTLPLVMLAYPFYLWARSPGKKGSHYHPDSDLFLPKERKDVLTSTACWTAMAALLVCLNFTIGPIQMLKLYGIPYWINVMWLDFVT... | Function: Chloroplast omega-3 fatty acid desaturase introduces the third double bond in the biosynthesis of 16:3 and 18:3 fatty acids, important constituents of plant membranes. It is thought to use ferredoxin as an electron donor and to act on fatty acids esterified to galactolipids, sulfolipids and phosphatidylglycer... |
P48622 | MASSVLSECGFRPLPRFYPKHTTSFASNPKPTFKFNPPLKPPSSLLNSRYGFYSKTRNWALNVATPLTTLQSPSEEDTERFDPGAPPPFNLADIRAAIPKHCWVKNPWMSMSYVVRDVAIVFGLAAVAAYFNNWLLWPLYWFAQGTMFWALFVLGHDCGHGSFSNDPRLNSVAGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESWHPLPESIYKNLEKTTQMFRFTLPFPMLAYPFYLWNRSPGKQGSHYHPDSDLFLPKEKKDVLTSTACWTAMAALLVCLNFVMGPIQMLKLYGIPYWIFVMWLDFVTYLHHHGH... | Function: Chloroplast omega-3 fatty acid desaturase introduces the third double bond in the biosynthesis of 16:3 and 18:3 fatty acids, important constituents of plant membranes. It is thought to use ferredoxin as an electron donor and to act on fatty acids esterified to galactolipids, sulfolipids and phosphatidylglycer... |
P48623 | MVVAMDQRTNVNGDPGAGDRKKEERFDPSAQPPFKIGDIRAAIPKHCWVKSPLRSMSYVVRDIIAVAALAIAAVYVDSWFLWPLYWAAQGTLFWAIFVLGHDCGHGSFSDIPLLNSVVGHILHSFILVPYHGWRISHRTHHQNHGHVENDESWVPLPERVYKKLPHSTRMLRYTVPLPMLAYPLYLCYRSPGKEGSHFNPYSSLFAPSERKLIATSTTCWSIMFVSLIALSFVFGPLAVLKVYGVPYIIFVMWLDAVTYLHHHGHDEKLPWYRGKEWSYLRGGLTTIDRDYGIFNNIHHDIGTHVIHHLFPQIPHYHLVD... | Function: Microsomal (ER) omega-3 fatty acid desaturase introduces the third double bond in the biosynthesis of 18:3 fatty acids, important constituents of plant membranes. It is thought to use cytochrome b5 as an electron donor and to act on fatty acids esterified to phosphatidylcholine and, possibly, other phospholip... |
Q59J82 | MAPPHVVDEQVRRRIVVEDEIKSKKQFERNYVPMDFTIKEIRDAIPAHLFIRDTTKSILHVVKDLVTIAIVFYCATFIETLPSLALRVPAWITYWIIQGTVMVGPWILAHECGHGAFSDSKTINTIFGWVLHSALLVPYQAWAMSHSKHHKGTGSMTKDVVFIPATRSYKGLPALEKPAVEEEVSEQEHHHHEESIFAETPIYTLGALLFVLTFGWPLYLIVNFSGHEAPHWVNHFQTVAPLYEPHQRKNIFYSNCGIVAMGSILTYLSMVFSPLTVFMYYGIPYLGVNAWIVCITYLQHTDPKVPHFRDNEWNFQRGAA... | Function: omega(3) desaturase that uses both 18-carbon and 20-carbon n-6 polyunsaturated fatty acids as substrates.
Catalytic Activity: a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (9Z,12Z,15Z)-octadecatrienoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O
... |
P48626 | MGSLGISEIYDKNSFNEMEFEFDPSAPPPFRLAEIRNVIPKHCWVKDPLRSLSYVVRDVIFVATLIGIAIHLDSWLFYPLYWAIQGTMFWAIFVLGHDCGHGSFSDSQLLNNVVGHILHSAILVPYHGWRISHKTHHQNHGNVETDESWVPMPEKLYNKVGYSTKFLRYKIPFPLLAYPMYLMKRSPGKSGSHFNPYSDLFQPHERKYVVTSTLCWTVMAALLLYLCTAFGSLQMFKIYGAPYLIFVMWLDFVTYLHHHGYEKKLPWYRGKEWSYLRGGLTTVDRDYGLFNNIHHDIGTHVIHHLFPQIPHYHLREATKA... | Function: ER (microsomal) omega-3 fatty acid desaturase introduces the third double bond in the biosynthesis of 18:3 fatty acids, important constituents of plant membranes. It is thought to use cytochrome b5 as an electron donor and to act on fatty acids esterified to phosphatidylcholine and, possibly, other phospholip... |
P96843 | MINDLRTVPAALDRLVRQLPDHTALIAEDRRFTSTELRDAVYGAAAALIALGVEPADRVAIWSPNTWHWVVACLAIHHAGAAVVPLNTRYTATEATDILDRAGAPVLFAAGLFLGADRAAGLDRAALPALRHVVRVPVEADDGTWDEFIATGAGALDAVAARAAAVAPQDVSDILFTSGTTGRSKGVLCAHRQSLSASASWAANGKITSDDRYLCINPFFHNFGYKAGILACLQTGATLIPHVTFDPLHALRAIERHRITVLPGPPTIYQSLLDHPARKDFDLSSLRFAVTGAATVPVVLVERMQSELDIDIVLTAYGLT... | Function: Involved in the catabolism of the rings C and D of cholesterol. Catalyzes the ATP-dependent CoA thioesterification of 3aalpha-H-4alpha(3'-propanoate)-7abeta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. It can also use the hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP. It requires that... |
Q0S7V5 | MTEQPTTTPSALKRAAREFGELTAVADGDVRLTFTQLHDRVRDFAAALSSQDVRPGDHVAVWSPNTYHWVVAALGIHYAGATLVPINTRYTATEALDILERTKTTALVVAGNFLGTDRYASLRDESSTFDLPTVVRVPVDGGDAELPGVFDFDDFLALADEDTRAEADARAAAVSPDDVSDVMFTSGTTGRSKGVMSAHRQSVGIAQAWGECAEVTSDDNYLIINPFFHTFGYKAGFLVCLLNGATVVPMAVFDVPKVMATVHDEQITVLPGAPTIFQSILDHPDRPKYDLSSLRVAITGAAAVPVALVERMQSELSFDA... | Function: Involved in the catabolism of the rings C and D of cholesterol. Catalyzes the ATP-dependent CoA thioesterification of 3aalpha-H-4alpha(3'-propanoate)-7abeta-methylhexahydro-1,5-indanedione (HIP).
Catalytic Activity: 3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoate + ATP + CoA = 3-[(3aS,4... |
Q8FBI2 | MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVKAEKLVEGAMAILRQAINGDLDWKAKRQPKLEPLKLSKIEAAMSFTIAKGMVAQTAGKHYPAPITAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVKGKAKKLTKDVETPKQAAVLG... | Function: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a... |
Q8ZNA7 | MTTTSAFMLNVRLDNVAVVAIDVPGEKVNTLKAEFATQVRAILKQIRENKALQGVVFISAKADNFIAGADINMIGHCQNAQEAETLARQGQQLMAEIQALPVPVIAAIHGACLGGGLEMALACHRRICTDDVKTVLGLPEVQLGLLPGSGGTQRLPRLVGVSTALDMILTGKQLRARQALKAGLVDDVVPQTILLEAAVELAKKERLAQRTLPVRERILAGPLGRALLFRLVRKKTAQKTQGNYPATERIIDVIETGLAQGSSSGYDAEARAFGELAMTPQSQALRAIFFASTEVKKDPGSDAPPGPLNSVGILGGGLMG... | Function: Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities.
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O
Sequence Mass (Da): 77255
Sequence Length: 715
Pathway: Lipid metaboli... |
Q46AU8 | MFIKYAEVLNLVKNILKSMVGEALIGSGPEVAHIDLVIGPRGGSVEAAFMNSLAMPRQGHTPLLAVLEPNIQPKPTTLIVNKVTIKNVSQAALMFGPAQAAVAKAVMDSVADGVLPEEQADDIFIIVSVFIEWDAKDKDKVYEFNYEATKLAIARAMEGRPTVEEALAKKDSANHPFA | Function: Catalyzes the condensation of formaldehyde with tetrahydromethanopterin (H(4)MPT) to 5,10-methylenetetrahydromethanopterin.
Catalytic Activity: 5,6,7,8-tetrahydromethanopterin + formaldehyde = 5,10-methylenetetrahydromethanopterin + H2O
Sequence Mass (Da): 19171
Sequence Length: 178
Subcellular Location: Cyto... |
Q9FA38 | MAKITKVQVGEALVGDGNEVAHIDLIIGPRGSPAETAFCNGLVNNKHGFTSLLAVIAPNLPCKPNTLMFNKVTINDARQAVQMFGPAQHGVAMAVQDAVAEGIIPADEADDLYVLVGVFIHWEAADDAKIQKYNYEATKLSIQRAVNGEPKASVVTEQRKSATHPFAANA | Function: Catalyzes the condensation of formaldehyde with tetrahydromethanopterin (H(4)MPT) to 5,10-methylenetetrahydromethanopterin, a reaction which also proceeds spontaneously, but at a lower rate than that of the enzyme-catalyzed reaction. Is an essential enzyme for methylotrophic energy metabolism and formaldehyde... |
Q9NW38 | MAVTEASLLRQCPLLLPQNRSKTVYEGFISAQGRDFHLRIVLPEDLQLKNARLLCSWQLRTILSGYHRIVQQRMQHSPDLMSFMMELKMLLEVALKNRQELYALPPPPQFYSSLIEEIGTLGWDKLVYADTCFSTIKLKAEDASGREHLITLKLKAKYPAESPDYFVDFPVPFCASWTPQSSLISIYSQFLAAIESLKAFWDVMDEIDEKTWVLEPEKPPRSATARRIALGNNVSINIEVDPRHPTMLPECFFLGADHVVKPLGIKLSRNIHLWDPENSVLQNLKDVLEIDFPARAILEKSDFTMDCGICYAYQLDGTIP... | Function: Ubiquitin ligase protein that mediates monoubiquitination of FANCD2 in the presence of UBE2T, a key step in the DNA damage pathway . Also mediates monoubiquitination of FANCI . May stimulate the ubiquitin release from UBE2W. May be required for proper primordial germ cell proliferation in the embryonic stage,... |
Q9CR14 | MDEAEASLLRHFPLLLPQNREKTVYEGFISAQGSDFHLRIVLPKDLQLKKARLLCSLQLKNILNEYHQVVQQRMKHSPDLMSFMMELKMILEVALKNKQELCVQPPSCSFCKDLLTEIGAIGWDKLACVESSFSTIKLKADDASGRKHLITVKLKAKYPVEPPDCVVDFPVPFSVSWTPQSSLVDVYSQFLVALETLKVFWDVMDEIDEKTWVLEPEKPPRSATARRIALGKNVSIAIEVDPRHPTMLPEFCFLGADHVTKPLGMKLSGSIHLWDPENSLLQNLKDVLEIDFPARSILEESDFSMDCGICYARHLNGAIP... | Function: Ubiquitin ligase protein that mediates monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCI. May stimulate the ubiquitin release from UBE2W. May be required for proper primordial germ cell proliferation in the embryonic stage, whereas it is probably not... |
P12050 | MNRKKHQILKILLLCLISSKSSASEKELNLQFIRHKFGQNTEDIELFFNSSTVLPGNYTVDVKLNDEVIGRAKLEVSQDDKESYCLKDEWLSDLGIIINRDFYNKYFNIKRECYEIGKEKNSITTFDNNSQIFSLYMPQAAYIKKGNTEHKWSYGDPGFNLNYDAYLSKNDEDSSIYGNLEGNVNIDKWVLYGRGYKYEHDKFTTDDVTLSRAIKSLEGDLIIGDTYTNTSLMDNISFYGVQLRSNNAMTPERRGDYSPIISGIAKSNARVTVKQNGVVLHSELVSPGPFHINNVRGIRSGELVMTVTEEDGSEQQTRIP... | Function: Involved in the export and assembly of K99 fimbrial subunits across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87157
Sequence Length: 783
Subcellular Location: Cell outer membrane
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P25448 | MKNKYNLLFFLFLLCYGDVALAACTGKLKISPGYSGHTYSFDSSIPNNSNIARYLVEISEKIVCDADQSGWDGKRYAQLHLYSSGALCESVSGDGITFRSNVSGLSWRFPNGIPYHCAAGQINLGGIKYADRNGKVTWNPGELRHEIFLRVDNRFDFSKSRTFSVNTISGRGGLGGDSSVVIPLIGSSFNYSYSNIATCTLTGPSEVNFNTVTTSDVLKGTTHRDLNLRAECRNRGASLGLNFKFEPQYKDVSANKQGVFYAKNTSGSLTYKLTKKADASAIPLNEFVKLIVEDKVNIHTGNTIPLLLTLQKGDGKIATG... | Function: Minor component of K99 fimbriae. Is not required for binding of K99 fimbriae to the ganglioside receptor. May play a role in initiation, elongation and flexibility of the fimbriae.
PTM: Three disulfide bonds are present.
Sequence Mass (Da): 36484
Sequence Length: 333
Subcellular Location: Fimbrium
|
Q6B858 | MELQKIASSSKPHPPVVGKVTHHSIELYWDLEKKAKRQGPQEQWFRFSIEEEDPKLHTYGIIYTGYATKHVVEGLEPRTLYRFRLKVTSPSGEYAYSPVVSVSTTREPISSEHLHRAVNVNDEDLLVRILQGGNVKVDVPNKFGFTALMVAAQRGYTRLVKILISHGTDVNLQNGSGKDSLMLACYAGHLDVVKYLRRHGASWDTRDLGGCTALHWAADGGHCNVIEWMIGDGCEVDAVDAGSRWTPLMRVSAVSGNQEVASLLIDAGADVNVKDKDGKTPLMVAVLNNHEELVQLLLDRGADASVKNEFGKGVLEMARV... | Function: Through the activation of JUN and AP-1-mediated transcription, may regulate apoptosis.
PTM: Polyubiquitinated. Polyubiquitination leads to proteasomal degradation.
Sequence Mass (Da): 38426
Sequence Length: 345
Domain: The fibronectin type-III domain mediates interaction with COPS5 and RYBP.
Subcellular Locat... |
Q8TC84 | MEPQKIMPPSKPHPPVVGKVTHHSIELYWDLEKKAKRQGPQEQWFRFSIEEEDPKMHTYGIIYTGYATKHVVEGLEPRTLYRFRLKVTSPSGECEYSPLVSVSTTREPISSEHLHRAVSVNDEDLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDTGSGWTPLMRVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARV... | Function: Through the activation of JUN and AP-1-mediated transcription, may regulate apoptosis.
PTM: Polyubiquitinated. Polyubiquitination leads to proteasomal degradation.
Sequence Mass (Da): 38341
Sequence Length: 345
Domain: The fibronectin type-III domain mediates interaction with COPS5 and RYBP.
Subcellular Locat... |
P0CY52 | SNSLFEEVRPIVNGMDCKLG | Function: Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa.
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium.
Catalytic Activity: Select... |
P81428 | MAPQLLLCLILTFLWSLPEAESNVFLKSKVANRFLQRTKRSNSLFEEIRPGNIERECIEEKCSKEEAREVFEDNEKTETFWNVYVDGDQCSSNPCHYRGTCKDGIGSYTCTCLPNYEGKNCEKVLYQSCRVDNGNCWHFCKRVQSETQCSCAESYRLGVDGHSCVAEGDFSCGRNIKARNKREASLPDFVQSQKATLLKKSDNPSPDIRIVNGMDCKLGECPWQAVLINEKGEVFCGGTILSPIHVLTAAHCINQTKSVSVIVGEIDISRKETRRLLSVDKIYVHTKFVPPNYYYVHQNFDRVAYDYDIAIIRMKTPIQF... | Function: Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa. Induces cyanosis and death in mice at 1 mg/kg body weight during blood clotting.
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. Th... |
Q2V3N5 | MDRVGSLPDELLSHILSFLTTKEAALTSLLSKRWRYLIAFVPNLAFDDIVFLHPEEGKPERDEIRQSFMDFVDRVLALQAESPIKKFSLKCRIGVDSDRVDGWISNVLNRGVSELDLLIILGMTMEDSYRLSPKGFASKTLVKLEIGCGIDISWVAGSIFLPMLKTLVLDSVWFYVDKFETLLLALPALEELVLVDVNWLDSDVTISNASLKTLTIDSDGHLGTFSFDTPSLVYFCYSDYAAEDYPVVKMENLREARIFLLVTDNEIERVRLPINDGLEDAMDNVVLRFGHVGKLMNGIRNVEYLELSADTLEVLSLCCE... | Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence Mass (Da): 55726
Sequence Length: 491
Domain: The F-box is necessary for the interaction with ASK proteins.
Pathway: Protein modification; ... |
Q9M1Q1 | MDSGSAVDIISTLSDFLLVLIISNLSFKEALSTSRLSTRWRHICRETRNISFREDEIVTFADDSVARYYQRAALVAYMVGWVNNFTGGVVESFELRLSNSYAFEEGVTTLIEFAVSKNVKHLFLDLSEPRWVTNNDAAQLEPGLIKLPESFYKITSLVTLKLFGCRFEPSRLAKPGMVKTMFFRWIRLEMLSALIAKTPLLEILNIKNCWEIGLDAITGYNDRLMKLVFKYCSFSAQQTTLDVPNIQIFKYFGKVYRFEFASANKLMEEAYLDYREESRYNVSAGAIISGFLYSMLSAKTFTICPYVLQLIQECEDPVRL... | Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence Mass (Da): 53142
Sequence Length: 461
Domain: The F-box is necessary for the interaction with ASK proteins.
Pathway: Protein modification; ... |
Q9FYF9 | MLPSRKTKRVFSCDFTPGRKRRRCVVVPSSVSPVPENTTGADLLDSIPDDLVISILCKLGSTSRCPADFINVLLTCKRLKGLAMNPIVLSRLSPKAIAVKAHNWSEYSHRFLKRCVDAGSLEACYTLGMIRFYCLQNRGNGASLMAKAAISSHAPALYSLAVIQFNGSGGSKNDKDLRAGVALCARAAFLGHVDALRELGHCLQDGYGVPQNVSEGRRFLVQANARELAAVLSSGIQARSTWLSLSQPPPPVVPNHGQQTCPLLSDFGCNVPAPETHPANRFLADWFAVRGGDCPGDGLRLCSHAGCGRPETRKHEFRRC... | Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence Mass (Da): 41012
Sequence Length: 379
Domain: The F-box is necessary for the interaction with ASK proteins.
Pathway: Protein modification; ... |
Q9SR08 | MKKRGRKSKKPEEKRAEYDPSSILPLELKIEILMKSPPKSIAKLGFVSNHWSSIIRGQVFTDLYMRRSLAHPRLLFSVYRPNMQMQFFHSCSQEDPSSDHRSVSYTLNSDLRYSFSPPIGGLIFGQNNTKAMIGNPSTGQFVPLPRIKTQRKHIFSIFGYDPVNDLYKVLCMTVRTLRGPHYFRWEDPMWEEPMTEEHQVFTLGPKQKWRMLECKYLHRHHSGSQGICRDGVMYYLASFNDKRSLMSFDLSSEEFNVTKLPEDYILQQFGNMVDHSGKIAIVSQAYSGPMDLWVLEDVSKEEWSKVAAIVPSITDIVGND... | Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence Mass (Da): 44932
Sequence Length: 390
Domain: The F-box is necessary for the interaction with ASK proteins.
Pathway: Protein modification; ... |
Q6D734 | MITLNTEKSFVELKHITKRFGNNTVIDDLNLAIPQGKMVTLLGPSGCGKTTVLRAVAGLEKPTEGQIFIDGEDVTERSIQQRDICMVFQSYALFPHMSLGENIGYGLKMLGRPKAEINQRVKEALALVDLEGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDMVLVMNKGKIMQLGAPQELYRQPASRFMASFMGDANIFPATFTADSVNIYGYLIPRPQGFAAGLSESTVGIRPEAITLSHQGEESQRCTITQVAYMGPQYEVQVDWHGQSM... | Function: Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + Fe(3+)(out) + H2O = ADP + Fe(3+)(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39329
Sequence Length: 352
Su... |
P44513 | MRLNKMINNPLLTVKNLNKFFNEQQVLHDISFSLQRGEILFLLGSSGCGKTTLLRAIAGFEQPSNGEIWLKERLIFGENFNLPTQQRHLGYVVQEGVLFPHLNVYRNIAYGLGNGKGKNSEEKTRIEQIMQLTGIFELADRFPHQLSGGQQQRVALARALAPNPELILLDEPFSALDEHLRQQIRQEMLQALRQSGASAIFVTHDRDESLRYADKIAIIQQGKILQIDTPRTLYWSPNHLETAKFMGESIVLPANLLDENTAQCQLGNIPIKNKSISQNQGRILLRPEQFSLFKTSENPTALFNGQIKQIEFKGKITSIQ... | Function: Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + Fe(3+)(out) + H2O = ADP + Fe(3+)(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40360
Sequence Length: 356
Su... |
Q92UV5 | MHIAQELADETCNSPRGAGHARLRYPSDRRTAIPRNRRPLEGLWRFRRVRDIDLQVKEGEFICFLGPSGCGKTTLLRAIAGLDIQSRGTICQGGQDISRLPPAQRDYGIVFQSYALFPNLTIEKNIAFGLENIGRPRREIASRVSELLELVGLSSQGRKYPAQLSGGQQQRVALARAMAISPGLLLLDEPLSALDAKVRVHLRHEIKELQRKLGVTTIMVTHDQEEALAMADRIVVMNQGGIEQVGTPTEIYRHPKTLFVADFIGETNQFPATVGKGAQVEIGHTRFACAEHRLPSGASVVAAVRPADIIPHGAAAHRAT... | Function: Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + Fe(3+)(out) + H2O = ADP + Fe(3+)(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 43429
Sequence Length: 395
Su... |
Q0S0Z3 | MTYALEVDGVDKSFGGATILRGVAFAVEPGSTTAIVGPSGCGKTTLLRLVAGFEKPDAGTIALAGRVVAGSGWAPAHRRSVGYVAQDGALFPHATVGANVGFGLPRRARTPARIAELLEMVSLDPSYAARRPDQLSGGQQQRVALARALAREPELMLLDEPFSALDAGLRANTRRIVADVLAKAAITTILVTHDQPEALSFADRVAVMSAGRLAQIGTPREIYSTPVDVPTAEFIGDAVVLSARVEGSRARCALGDVTVASNGVHGNARVMLRPEQIEVTTDGAGVSGTVVDVEYLGSEMLLGIRLDTGDGEVPERVTVR... | Function: Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + Fe(3+)(out) + H2O = ADP + Fe(3+)(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36074
Sequence Length: 346
Su... |
Q8U6M1 | MITVKPGSVVFENVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPNSGRILIGGKDVTMLPANERDVSMVFQSYALFPHMSALDNVAYGLQSSGLKKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTDIRELQQRIGFTAVYVTHDQDEALAVSDRIIVMKEGEIAQSGAPRELYEAPASSFIADFMGEANVVPCEVVSQTGDESLVRVGTMEHRVRSRGPRSGSAKLAVRPGAITIGAAGGSGMPGRVLHTAYLGGHIEYEVETEVG... | Function: Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + Fe(3+)(out) + H2O = ADP + Fe(3+)(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37990
Sequence Length: 353
Su... |
P37009 | MTQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANLFPATFSDGYVDIYGYHLPRPLHFGTQGEGMVGVRPEAITLSDRGEESQRCVIRHVAYMGPQYEVTVEWHGQEILLQVN... | Function: Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + Fe(3+)(out) + H2O = ADP + Fe(3+)(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39059
Sequence Length: 348
Su... |
Q8RGC8 | MSVNIKIENAQKRYGDNIIIENLSLDIKQGEFFTLLGPSGCGKTTLLRMIAGFNSIEKGNFYFNEKRINDLDPAKRNIGMVFQNYAIFPHLTVEQNVEFGLKNRKVSKEEMKIEIDKFLKLMQIDEYKDRMPERLSGGQQQRVALARALVIKPDVLLMDEPLSNLDAKLRVEMRTAIKEIQNSIGITTVYVTHDQEEAMAVSDRIAVMKDGEIQHLGQPKDIYQRPANLFVATFIGKTNVLKGNLNGSILKVAGKYEVSLNNIKDKNIKGNVVISIRPEEFVIDENQTKDGMRAFIDSSVFLGLNTHYFAHLESGEKIEI... | Function: Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + Fe(3+)(out) + H2O = ADP + Fe(3+)(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 41843
Sequence Length: 371
Su... |
Q9SKZ5 | MASRSLFSISISPSQFTVLPSINNERRRLAIAARSHRLSRRKIRKRPPDRDMSSIVSIPELPRRRDSEESLLLDSRISVAEGDTSNTDVEGDRDTTSSIRTQPPPRKGRNLSSSRIKFYGVELSPDNVAVAMVYFVQGVLGLARLAVSFYLKDDLHLDPAETAVITGLSSLPWLVKPLYGFISDSVPLFGYRRRSYLVLSGLLGAFSWSLMAGFVDSKYSAAFCILLGSLSVAFSDVVVDSMVVERARGESQSVSGSLQSLCWGSSAFGGIVSSYFSGSLVESYGVRFVFGVTALLPLITSAVAVLVNEQRVVRPASGQK... | Function: Mediates folate monoglutamate transport involved in tetrahydrofolate biosynthesis. It also mediates transport of antifolates, such as methotrexate and aminopterin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60707
Sequence Length: 560
Subcellular Location: Plastid
|
Q9SQN2 | MANRSEEAEYENDSRRNHQDKKKEGVLDLVLKRPLRWLRMLIEELHWSFFFGVIIVYGVSQGLGKGLSKVSTQYYFKDEQKIQPSQAQIYVGLIQIPWIIKPLWGLLTDVVPVLGYRRRPYFILAGFLAMISMMVLWLHTNLHLALALSCLVAGSAGVAIADVTIDACVTQCSISHPTLAADMQSLCGLCSSIGSLVGFSLSGVLVHLVGSKGVYGLLGVTAGLLVVVGMVLKESPSRSLGRKHVNDKFLDAGSAIWKTFQYGEVWRPCLFMLLSAAVSLHIHEGMFYWYTDSKDGPSFSKEAVGSIMSFGAIGSLVGIL... | Function: Could mediate folate transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55028
Sequence Length: 497
Subcellular Location: Membrane
|
Q8RWQ5 | MIHWLKQLRSAFGVAFLWLVCLIYFTQGFRSFVWTAVSYQLKDRLQLSPSASQFVFSVAFFPWSIKPLYGIISDCIPIGGKKRTPYLVISTVLSLVPWLVLGLDSTSRSSSLYLMIFLTVQNLGSAMADVVIDAMIAEAVRLEKASFAGDLQSVSWFAMAVGGVCGSLLGGYALSNLKIETIFLLFTVLPALQLLSCALVEESPANNEPLPELLDSNEFEEKSLTSNDNYPDTSKSNTRRRKGQKKGKKGDSNGKSETQKKQSKSLASQWFQSLKAATFGLGRAFKQPIILRPMAWFFIAHITVPNLSTVMFYYQTEVLQ... | Function: Could mediate folate transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53883
Sequence Length: 491
Subcellular Location: Membrane
|
F4KIL8 | MAREEQNIENRGSVHVVERESNLRSVVCGPVRWLKMLASKLHWSYVFAVVSNCGINQGFGYSLGHVATDYYMKDVQKVQPSQYQALSAITRISWIIFKPLFGILTDVLPIFGFHRRPYFILAGVIGVVSLLFISLQSNLHLYLALFWMTISSAAMAIADVTIDACTTYNSNKHPSLASDMQSLCSLSYSIGELLGFFMSGILVHLVGSKGVFGLLTFTFALVSVVGVLFSEPRVHGFSFKQNFTNAMKAMWRTIKCSDVWQPSLYMFITRALGLDIKEGLFYWFTDSKDGPLFAQETVGFILSIGSIGSILGVLLYNLRL... | Function: Could mediate folate transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55330
Sequence Length: 492
Subcellular Location: Membrane
|
Q9LEV7 | METLETEKFFSDDKPLLKPISDHSEIKTKARRNAVVSVLIQPFQWLQMLSSRLNLSFVLGVVLVYGVNQGFSGSIFKVVTDYYWKDVQQVQPSVVQLYMGLYYIPWVMRPIWGLFTDVFPIKGYKRKPYFVVSGVLGLVSAIAIVVLGKLPAALALSCLLGVSAAMAIADVVIDACIATNSINIRSLAPDIQSLCMVCSSAGALVGYATSGVFVHQLGPQGALGVLAFSPATIVILGFFIYEKRSSTVPTQKTKKDTDGLGVAVKGMCKTVKYPEVWKPSLYMFISLALNISTHEGHFYWYTDPTAGPAFSQEFVGIIYA... | Function: Could mediate folate transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55814
Sequence Length: 503
Subcellular Location: Membrane
|
Q9XIQ7 | MSSSSDTHAGESRHRRNPIRWLLGFGFFVQGFRGFPWLGANFFLTEQLRVNPSVLQLLQNSANLPMVAKPIYGVVSDSVYFFGQHRIPYIAVGALLQAISWLAIAFLSRSNVSILALSIYLLLSNLGASLVEVANDAIVAESGKQKTSETQSGELPSFVWMVSSLGGILGNLLGGIAIKTFSAQSTFLVFGILALLQFLVTINIREKSLNLPENPSPAGGIRKHLSDLSHVLRKPEISYSIAWIAVSTAVVPVLTGTMFFYQTKFLKIDASLLGISKVFGQIAMLLWGFAYNRWLKAMRPRKLLTAIQVTIAFFVISDLL... | Function: Could mediate folate transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48486
Sequence Length: 442
Subcellular Location: Membrane
|
F4I5Q2 | MERIMINPLLSIQNSPTKFLKPPLSSIHRQQQQQERQSNNNTLFMGEARPRRATTFACLSIRRRRNNNGVSEFEETARFEQVGGKGISVLCGLGYWVQGSRCFPWLALNFHMVHSLALQPSTLQLVQYSCSLPMVAKPLYGVLSDVLYIGSGRRVPYIAIGVFLQVLAWGSMGIFQGAREVLPSLVACVLLSNLGASITEVAKDALVAEYGLRYRINGLQSYALMASAAGGVLGNLLGGYLLLTTPPKISFLVFSALLSLQLVVSLSSKEESFGLPRIAETSSVLESVKKQISNLKEAIQADEISQPLIWAVVSIAMVPL... | Function: Could mediate folate transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59507
Sequence Length: 542
Subcellular Location: Plastid
|
Q55721 | MLVAMSMTPIAILFSTPLKRFLREKVLLGNAPSWELLAILSIYFVQGVLGLSRLAVSFFLKDELGLSPAAMGALIGLGAAPWILKPVLGLMSDTVPLFGYRRRSYLWLSGLMGSAGWLLFAAWVSSGTQAGLVLLFTSLSVAIGDVIVDSLVVERAQRESLAQVGSLQSLTWGAAAVGGIITAYASGALLEWFSTRTVFAITAIFPLLTVGAAFLISEVSTAEEEEKPQPKAQIKLVWQAVRQKTILLPTLFIFFWQATPSAESAFFYFTTNELGFEPKFLGRVRLVTSVAGLIGVGLYQRFLKTLPFRVIMGWSTVISS... | Function: Mediates folate monoglutamate transport involved in tetrahydrofolate biosynthesis. It also mediates transport of antifolates, such as methotrexate and aminopterin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53586
Sequence Length: 494
Subcellular Location: Cell membrane
|
P9WLL6 | MAMVNTTTRLSDDALAFLSERHLAMLTTLRADNSPHVVAVGFTFDPKTHIARVITTGGSQKAVNADRSGLAVLSQVDGARWLSLEGRAAVNSDIDAVRDAELRYAQRYRTPRPNPRRVVIEVQIERVLGSADLLDRA | Function: Catalyzes the F420H(2)-dependent reduction of biliverdin-IXalpha at C10 position, leading to bilirubin-IXalpha, a potent antioxidant. As biliverdin-IXalpha is produced in high amounts in macrophages infected with M.tuberculosis, its reduction by Rv2074 may play a role in protecting mycobacteria against oxidat... |
L7N1X6 | MAIHLPCLPMMKILSYLDAYSLLQAAQVNKDWNELASSDVLWRKLCQKRWLYCDMDTLQLQGKETWKQFFIDRIWQERAKFRAKAKDFTYKEIPLMCGLFGYACYISGCGLTRKGQDKSVVCMVNSKNTISTWDVHKSVITWKSPEQPASIKLLTTLPEMHIAVTVDIQSTIKLWDCHNREALATNNLKSPCKSLKAVFTKDGPIVLIGDTLGNIHIFRIPDLYLISTVNVLPYGFDGIYCSPQKKWVLLSKKHPHILPKVFYMSSFLRTSEFSAPVSTVLKLSLYERVFWTPRREDRITLMSRSGFPQVKMFETYDIKL... | Function: Substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Promotes KAT7 ubiquitination and subsequent degradation in collaboration with MAP2K1 kinase, leading to reduced histone H3K14 acetylation and increased cell proliferation.
Sequence Mass (Da): 53586
Sequence L... |
Q9Y297 | MDPAEAVLQEKALKFMCSMPRSLWLGCSSLADSMPSLRCLYNPGTGALTAFQNSSEREDCNNGEPPRKIIPEKNSLRQTYNSCARLCLNQETVCLASTAMKTENCVAKTKLANGTSSMIVPKQRKLSASYEKEKELCVKYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVRTDSLWRGLAERRGWGQYLFKNKPPDGNAPPNSFYRALYPKIIQDIETIESNWRCGRHSLQRIHCRSETSKGVYCLQYDDQKIVSGL... | Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins . Recognizes and binds to phosphorylated target proteins . SCF(BTRC) mediates the ubiquitination of CTNNB1 and part... |
P20491 | MISAVILFLLLLVEQAAALGEPQLCYILDAVLFLYGIVLTLLYCRLKIQVRKAAIASREKADAVYTGLNTRSQETYETLKHEKPPQ | Function: Adapter protein containing an immunoreceptor tyrosine-based activation motif (ITAM) that transduces activation signals from various immunoreceptors. As a component of the high-affinity immunoglobulin E (IgE) receptor, mediates allergic inflammatory signaling in mast cells . As a constitutive component of inte... |
Q9XSZ6 | MIPAVVLLLLLLVEQAAALGEPQLCYILDAILFLYGIVLTLLYCRLKLQVRKAAIDSYEKSDGVYTGLSTRNQETYETLKHEKPPQ | Function: Adapter protein containing an immunoreceptor tyrosine-based activation motif (ITAM) that transduces activation signals from various immunoreceptors. As a component of the high-affinity immunoglobulin E (IgE) receptor, mediates allergic inflammatory signaling in mast cells. As a constitutive component of inter... |
P20411 | MIPAVILFLLLLVEEAAALGEPQLCYILDAILFLYGIVLTLLYCRLKIQVRKADIASREKSDAVYTGLNTRNQETYETLKHEKPPQ | Function: Adapter protein containing an immunoreceptor tyrosine-based activation motif (ITAM) that transduces activation signals from various immunoreceptors. As a component of the high-affinity immunoglobulin E (IgE) receptor, mediates allergic inflammatory signaling in mast cells. As a constitutive component of inter... |
Q6E7F2 | MDARKNGVLITGGAGFIGKALITEMVERQIPLVSFDISDKPDSLPELSEYFNWYKFSYLESSQRIKELHEIVSRHNIKTVIHLATTMFPHESKKNIDKDCLENVYANVCFFKNLYENGCEKIIFASSGGTVYGKSDTPFSEDDALLPEISYGLSKVMTETYLRFIAKELNGKSISLRISNPYGEGQRIDGKQGVIPIFLNKISNDIPIDIIGSIESKRDYIYISDLVQAFMCSLEYEGHEDIFNIGSGESITLKKLIETIEFKLNKKAVIGFQDPIHTNANGIILDIKRAMAELGWRPTVVLDDGIDKLIKSIRCK | Function: Catalyzes the stereospecific reduction of the C-4 keto group of dTDP-4-dehydro-6-deoxy-D-glucose, leading to dTDP-D-fucopyranose. This is a step in the biosynthesis of D-fucofuranose, a component of E.coli O52 O antigen. Is more efficient using NADH than NADPH as cosubstrate.
Catalytic Activity: dTDP-alpha-D-... |
Q6E7F1 | MNKVLIIGSGFSGATIARLLAEENIKVKIIDDRKHIGGNCYDERDEKTGINVHVYGPHIFHTDNEDVWNFVNKYGTFQPYTTRLKANAKGQIYSLPVNLHTINQYYKTALSPTEARKLIASKGDQTINDPQSFEEQALKFVGEDLYKTFFYGYPKKQWGMEPKEIPASVLKRLPVRFNYDDNYFFHKFQGIPRDGYTPLFQNLLNHPNIEFELGKKVNRATVEELITSEQYGHVFFSGAIDHFYDYEFGMLQYRTLDFEKFYSEDDDYQGCVVMSYCDEDVPYTRVTEHKYFTPWEEHKGSVLYKEFSRSCDKEDIPYYP... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the conversion of dTDP-alpha-D-fucopyranose to dTDP-alpha-D-fucofuranose. This is a step in the biosynthesis of D-fucofuranose, a component of E.coli O52 O antigen.
Catalytic Activity: dTDP-alpha-D-fucose = dTDP-alpha-D-fucofuranose
Sequence Mass (Da): 44195
Sequen... |
P31994 | MGILSFLPVLATESDWADCKSPQPWGHMLLWTAVLFLAPVAGTPAAPPKAVLKLEPQWINVLQEDSVTLTCRGTHSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIVLRCHSWKDKPLVKVTFFQNGKSKKFSRSDPNFSIPQANHSHSGDYHCTGNIGYTLYSSKPVTITVQAPSSSPMGIIVAVVTGIAVAAIVAAVVALIYCRKKRISALPGYPECREMGETLPEKPANPTNPDEADKVGAENTITYSLLMHPDALEEPDDQNRI | Function: Receptor for the Fc region of complexed or aggregated immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of immune complexes and modulation of antibody production by B-cells. Binding to this receptor results in down-modulation of previ... |
P9WEP5 | MLLRLPPVFLTVLIAIASCSVYILNIAIESGFADSPYNFNQTTVGLAYMSTGIGYILSSMAGGRWMDSIMAREARKVVRSDSHGKLISLPEDHMKENAWVANTLYPLSSLWFGWTMYYGVQFMVPISALFVFGFTLMLHFTLGTTMLTEFVRKRSSAGVTVNNFVRNILSCVGTIVAAPWMKGVGLRYMMTKLCIICLLLGSLGIWLITRNAQRWRGTLDKALKEMD | Function: MFS-type transporter; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant . Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-... |
W7MM11 | MTIETMLSEEKSQSSDNRNNGSIKVGISSGEVDLESREVFRTGDDVLDFRTVSWQRATIMFCKINFAMSILAIPQAISTVGAVGGSLILVGFTSLNVYTALILGDFRNRHPECHMLADMMGLIWGMVGRELVGVQIIVLQILITAGGVATTAVGLNALSNHSQCTVIFGLASAILVTACSSVRTFSKLGWITWFGMITFTVGVLVFTIAVTQQDRPAAASPTGDFDLGWTAIANPGFVVGMVSSANLFICTSGSSMFLPVISEMRRPQDYRKACLWAGLIVGMLYLVLSLVIYRYCGTWLSVPAFGSAGPLFKKISYGIS... | Function: Transmembrane transporter; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant . Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihyd... |
W7MC48 | MTIQSNEFNVAIVGAGVAGLALAMALHRKGVLFTIYEEAKEYSVVGAGIGFGPNGMQALDLIEPGFRPLYEGLCVGNKSADAQWVFFEGYLLEPGLGDNKPWAGNLKSAWGNQDYVRKSAHRKELLDIMTSFIPIESVKFNKKLVSIKEYTDRVMLEFADGEIVAHSILAGSDGIASTVREYLLRPTHPEEALPVYSGAHCYRAVIPMDEAYEIMGEKTDVAKIYFGHNRGAVSYRITGGKELNFLLIKATPNEQWPYPGRVTKQITQEEMLADFDGDNIDDRFRRLVAKAKPVKWGLFHHAKTSTYYKDRVCILGDSAH... | Function: FAD-dependent monooxygenase; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant . Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dih... |
W7MLD8 | MAEVNWQQLINQKRATREALIPEQWLLPATITSKVTPQSTASAFELLSEAGLLTEREIDITEKYTAVSLTAKIATGELSSYDVATAFCKRAAIVHQLTNSLTEIFFDKALERARWLDEYLSKEGKTVGPLHGLPITLKDMIHVKGQYSTMGFVGHLRHPPADENAVITDMLEAAGAVFYCKTNVPQTLFVCESFNNVFGRTLNPYKLCLSPGGSSSGEAAQLGLCGSIMGVGSDIAGSVRVPAIFTGVYGFRPTVNRLPWSKQAELALKGWQGVQPTLGPMARTAQDLTLFMKTIIQAEPWRYDSTALAIPWHDAPRKDK... | Function: Amidase; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant . Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazi... |
O23344 | MATLPLPTQTSTISLPKPYLSNSFSFPLRNATLSTTTNRRNFLTTGRIIARAYKVVVEHDGKTTELEVEPDETILSKALDSGLDVPYDCNLGVCMTCPAKLVTGTVDQSGGMLSDDVVERGYTLLCASYPTSDCHIKMIPEEELLSLQLATAND | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions (Probable). Mediates alternative electron partitioning in conditions of acceptor limitation at photosystem I. Accepts electrons from photosystem I (PSI) and is capable of e... |
A2QHE5 | MSAQPAHLCFRSFVEALKVDNDLVEINTPIDPNLEAAAITRRVCETNDKAPLFNNLIGMKNGLFRILGAPGSLRKSSADRYGRLARHLALPPTASMREILDKMLSASDMPPIPPTIVPTGPCKENSLDDSEFDLTELPVPLIHKSDGGKYIQTYGMHIVQSPDGTWTNWSIARAMVHDKNHLTGLVIPPQHIWQIHQMWKKEGRSDVPWALAFGVPPAAIMASSMPIPDGVTEAGYVGAMTGSSLELVKCDTNDLYVPATSEIVLEGTLSISETGPEGPFGEMHGYIFPGDTHLGAKYKVNRITYRNNAIMPMSSCGRLT... | Cofactor: Binds 1 prenylated FMN (prenyl-FMN) per subunit.
Function: Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of ... |
Q03034 | MRKLNPALEFRDFIQVLKDEDDLIEITEEIDPNLEVGAIMRKAYESHLPAPLFKNLKGASKDLFSILGCPAGLRSKEKGDHGRIAHHLGLDPKTTIKEIIDYLLECKEKEPLPPITVPVSSAPCKTHILSEEKIHLQSLPTPYLHVSDGGKYLQTYGMWILQTPDKKWTNWSIARGMVVDDKHITGLVIKPQHIRQIADSWAAIGKANEIPFALCFGVPPAAILVSSMPIPEGVSESDYVGAILGESVPVVKCETNDLMVPATSEMVFEGTLSLTDTHLEGPFGEMHGYVFKSQGHPCPLYTVKAMSYRDNAILPVSNPG... | Cofactor: Binds 1 prenylated FMN (prenyl-FMN) per subunit.
Function: Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of ... |
Q9C7Y4 | MALILPCTFCTSLQKKNFPINRRYITNFRRGATTATCEFRIPVEVSTPSDRGSLVVPSHKVTVHDRQRGVVHEFEVPEDQYILHSAESQNISLPFACRHGCCTSCAVRVKSGELRQPQALGISAELKSQGYALLCVGFPTSDLEVETQDEDEVYWLQFGRYFARGPIERDDYALELAMGDE | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions (Probable). Mediates alternative electron partitioning in conditions of acceptor limitation at photosystem I (By similarity).
Sequence Mass (Da): 20377
Sequence Length: 181... |
P09347 | MQYARAAVMVEQNRVETWEVPIFDPAPGGALVRVVLGGVCGSDVHIVSGEAGAMPFPIILGHEGIGRIEKLGTGVTTDYAGVPVKQGDMVYWAPIALCHRCHSCTVLDETPWDNSTFFEHAQKPNWGSYADFACLPNGMAFYRLPDHAQPEALAALGCALPTVLRGYDRCGPVGLDDTVVVQGAGPVGLAAVLVAAASGAKDIIAIDHSPIRLDMARSLGATETISLADTTPEERQRIVQERFGKRGASLVVEAAGALPAFPEGVNLTGNHGRYVILGLWGAIGTQPISPRDLTIKNMSIAGATFPKPKHYYQAMQLAAR... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: (1R,4R,5R)-5-hydroxycamphor + NAD(+) = (1R,4R)-bornane-2,5-dione + H(+) + NADH
Sequence Mass (Da): 38460
Sequence Length: 361
Pathway: Terpene metabolism; (R)-camphor degradation.
EC: 1.1.1.327
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P53799 | MGSLGTMLRYPDDIYPLLKMKRAIEKAEKQIPPEPHWGFCYSMLHKVSRSFSLVIQQLNTELRNAVCVFYLVLRALDTVEDDTSIPTDEKVPILIAFHRHIYDTDWHYSCGTKEYKILMDQFHHVSAAFLELEKGYQEAIEEITRRMGAGMAKFICQEVETVDDYDEYCHYVAGLVGLGLSKLFLAAGSEVLTPDWEAISNSMGLFLQKTNIIRDYLEDINEIPKSRMFWPREIWGKYADKLEDLKYEENTNKSVQCLNEMVTNALMHIEDCLKYMVSLRDPSIFRFCAIPQIMAIGTLALCYNNEQVFRGVVKLRRGLT... | Catalytic Activity: 2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 diphosphate + NADP(+) + squalene
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47142
Sequence Length: 410
Pathway: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3.
Subcellular Location:... |
B0UXL7 | MGITKLAHLIHFDAPASMRSKEIGDYSGKIIALDTSIVVNQFRSALPGHLKLSPLAGLFYRTLAFLEHDIKPVFVLDGKPPHQKRAVLEKRAQSTGWSSSQSPNTGSAFNQECLRLLHLMGVPCIKAPGEAEALCAHLAKIGTVNAVASEDMDTLAFGGTVLLRQLNAKRDSEITEYSLPKLLEALQLKYEEFVDLCILLGCDYCDKIGGLGPSRALKLIKEHHTIEGVMEHVNRKTHPIPLNWQYKDARKLFFETPKIDDPVLAWSEPDEEGLVQFLCKEKPLKEERVRGRMKKFREMLLKRRKQREVNMQMGQTRQSR... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
Q7Q323 | MGIKGLSQLIADIAPFAVKEGEIKQFFGRKVAIDASMCLYQFLIAVRAEGAQLTSVDGETTSHLMGTFYRTIRLLENGIKPVYVFDGKPPDLKSGELNKRAERREEAQKALDKATEAGATEDIEKFNRRLVKVTKHHANEAKELLRLMGVPYVEAPCEAEAQCAALVRAGKVYATATEDMDALTFGSNILLRHLTFSEARKMPVQEFAYEKVLKGFELTQDEFIDLCILLGCDYCDTIRGIGPKKAIELINKHRSIEKILEHLDRQKYIVPEGWNYEQARKLFKEPEVQDADTIELKWSEPDEEGLVKFLCGDRQFNEDR... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
O65251 | MGIKGLTKLLADNAPSCMKEQKFESYFGRKIAVDASMSIYQFLIVVGRTGTEMLTNEAGEVTSHLQGMFNRTIRLLEAGIKPVYVFDGKPPELKRQELAKRYSKRADATADLTGAIEAGNKEDIEKYSKRTVKVTKQHNDDCKRLLRLMGVPVVEATSEAEAQCAALCKSGKVYGVASEDMDSLTFGAPKFLRHLMDPSSRKIPVMEFEVAKILEELQLTMDQFIDLCILSGCDYCDSIRGIGGQTALKLIRQHGSIETILENLNKERYQIPEEWPYNEARKLFKEPDVITDEEQLDIKWTSPDEEGIVQFLVNENGFNI... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
A7AX58 | MGIKGLIGFLSDAAPGCISEVTLESLSGTSIAIDASTALYQFTIAIREGSYLSSLTNSKGESTSHIAGLLNRCIRLLELGIRPVFVFDSTPPEAKSQTLAKRKLLREEAESSLEKAIEEDDKEAIRKYVGRTVRITQKENESAKKLLRLVGVPVIEAAEEAEAQCAYLCQRGFVTAVGSEDADALVFRCGVLLKNLTASNKPVVRVDLAKALELLELTHEQFTDFCILCGCDYCGTLKGVGPKTAYNLIKKHGSISRILEVRSETLEGYEAAQEYFRDPKVRDITTIDRCEANIDGLREFLISENDFSEERVDKLIERLQ... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
Q8KCB2 | MLDIHNPATDHHDMRDLTIIGGGPTGIFAAFQCGMNNISCRIIESMPQLGGQLAALYPEKHIYDVAGFPEVPAIDLVESLWAQAERYNPDVVLNETVTKYTKLDDGTFETRTNTGNVYRSRAVLIAAGLGAFEPRKLPQLGNIDHLTGSSVYYAVKSVEDFKGKRVVIVGGGDSALDWTVGLIKNAASVTLVHRGHEFQGHGKTAHEVERARANGTIDVYLETEVASIEESNGVLTRVHLRSSDGSKWTVEADRLLILIGFKSNLGPLARWDLELYENALVVDSHMKTSVDGLYAAGDIAYYPGKLKIIQTGLSEATMAV... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 39240
Sequence Length: 360
EC: 1.18.1.2
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Q483W3 | MKTLTTDVAIIGAGPVGLFQIFELGLQGLSTVVIDSLPEIGGQCSELYPDKPIYDIPALPNAKASEVIDNLWQQAAIFDPTFLLAERVEHIEKVSEHSFIVTTHKQTQIHCRAVVIAAGNGAFSPVKLKLPLIDKFEDTQLFYRISNIEHFRDKNVVVLGGGDSALDWSLTLQKTAKSVLLIHRSSNFKAAKSSVNKMYELCEQLKMQFLCGQVSSFQEKENKLTGLTITSKDGVNRRVELDELVVLFGMSPKLGPIDNWQLEMHQHQIKVDTQSFQTSVTGIYAVGDINYYPGKRKLILSGFHEAALAAFSIAETVLEK... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 38698
Sequence Length: 349
EC: 1.18.1.2
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Q1IZM1 | MQSKQAPDTEILVIGGGPAGLHAAFYAAWRGLSVRVLEARGEVGGQLLALYPDKVIYDVPGVPQVRAAELVAALCAQLGPLDVDLRTGEVARTLEPDGTGGWVIGTAGARHRARAVILAAGMGALLPREVRVPGADTHPDVRADLPDPAGFAGRRVLVVGGVPQATRAAVELLEAGATVTLTHRRAGFRGDPLTLARLETARQASQMRLLAPAVLSRLTPQGAELVVEGAPLAVRADTVLILNGYLPDLSPLQAWPLAWDGEYVPDGPSGQTVLPGVYVIGDLARSGGDFKLLSLAFAQAAVAANHAAHHVRPELKMRPG... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 34589
Sequence Length: 331
EC: 1.18.1.2
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P28861 | MADWVTGKVTKVQNWTDALFSLTVHAPVLPFTAGQFTKLGLEIDGERVQRAYSYVNSPDNPDLEFYLVTVPDGKLSPRLAALKPGDEVQVVSEAAGFFVLDEVPHCETLWMLATGTAIGPYLSILQLGKDLDRFKNLVLVHAARYAADLSYLPLMQELEKRYEGKLRIQTVVSRETAAGSLTGRIPALIESGELESTIGLPMNKETSHVMLCGNPQMVRDTQQLLKETRQMTKHLRRRPGHMTAEHYW | Function: Transports electrons between flavodoxin or ferredoxin and NADPH . Reduces flavodoxin 1, flavodoxin 2 and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner . Required for the activation of several enzymes such as pyruvate formate-lyase, anaerobic ribonucleotide reductase and ... |
Q2GGH5 | MTDYVTDIAVIGAGPVGIFTVFQAGMLKMRCCVIDALSEIGGQCLALYPEKPIYDIPGYPVINGKELIDSLKKQSEPFNPQYLLGQVAEKIEDYSDYFLIRTTTGIVVQSKVIIIAAGAGAFGPNRLPIDNILDYENKSVFYQVRKVSDFCDKNIMIAGGGDSAADWAVELSKVAKQLYVVHRRKNFRCAPNTALQMDNLSQSGKIKIIVPYQVKKLCGENGKLHSVIVKNITNHEEMALQVDYLFPFFGTSANLGPILNWGMEVKNYQILVNAETCLTNRNRIYAVGDIATYPGKLKLILTGFSEAAMACHHIYHVIYP... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 37424
Sequence Length: 338
EC: 1.18.1.2
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A5FJT9 | MIKTDILIIGAGPTGLFAVFEAGLLKLKCHILDALPQPGGQLSELYPKKPIYDIPGFPEVLAGDLVDGLMEQIKQFEPGFTLGERAETVEKQEDGTFIVTSNKGTKFHAPVIAIAGGLGSFEPRKPLIEDIEFYEDKGVKYFIKNPEKFRDKRVVIAGGGDSALDWSIFLANVASEVTLIHRRNEFRGALDSVEKVQELKSAGKIKLITPAEVIGINGAEHVESLDIEENGAHRKIECDYFIPLFGLTPKLGPIGDWGLEIEKNAIKVNNALDYQTNIPGIFAIGDVNTYPGKLKLILCGFHEATLMCQAAYGIINPGKK... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 38142
Sequence Length: 350
EC: 1.18.1.2
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Q0RRX8 | MLIVGAGPAGLYGAYYAGFRGMSVALMDSLPEAGGQVTAMYPEKVIYDVAGFPAIRGRELVDALVTQAAQFDPTYLLDQQAAELAHEPDAVVVTSSQGHRVRARVVVITGGLGTFTPRPLPTGTGHLGRGLVYFVPKLDVYADQDVIVVGGGDSAFDWALALEPIARSVTLVHRRDRFRAHAATIERVEASRVEILTFSEVAAIHGEDRIEKVELVQTRTGDRHVRPAQAVVAALGFTADLGPLTRWGLTMARRHIAVDSTMFTGVDRVFAAGDITEYPGKVRLIATGFGEVATAVNNAAPVVDPAAKVFPGHSSGDSTA... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 34046
Sequence Length: 321
EC: 1.18.1.2
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A9H9C9 | MTDAPTLTTDVAIIGAGPAGLFAAFECGMLKLDSLLIDALDCVGGQCAALYPEKPIYDIPGHPAIAGAALIEGLEQQIAPFDVPRLLGRRVERLSGHRGAFTLGTDRGETIHARAVIIAAGAGAFGPNRPPLAGLDGFEATGAVQYYVRRRADFAGTRIVIAGGGDSAIDWALALKDEAEKIWLVHRRDRFRAAPESLRQLDEAVAAGRIEKIVPYQLHGLRGTDGALEGVEVATLDGDTRILPADRLLPFFGLSTDLGPIAHWGMDSIRSTIPVVPSSCETTLPGVFAVGDVAAYPGKLKLILQGFSEGAMAAHAIHPI... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36053
Sequence Length: 341
EC: 1.18.1.2
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O93634 | MGVPIGEIIPRKEIELENLYGKKIAIDALNAIYQFLSTIRQKDGTPLMDSKGRITSHLSGLFYRTINLMEAGIKPVYVFDGEPPEFKKKELEKRREAREEAEEKWREALEKGEIEEARKYAQRATRVNEMLIEDAKKLLELMGIPIVQAPSEGEAQAAYMAAKGSVYASASQDYDSLLFGAPRLVRNLTITGKRKLPGKNVYVEIKPELIILEEVLKELKLTREKLIELAILVGTDYNPGGIKGIGLKKALEIVRHSKDPLAKFQKQSDVDLYAIKEFFLNPPVTDNYNLVWRDPDEEGILKFLCDEHDFSEERVKNGLE... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
Q980U8 | MDLADLVKDVKRELSFSELKGKRVSIDGYNALYQFLAAIRQPDGTPLMDSQGRVTSHLSGLFYRTINILEEGVIPIYVFDGKPPEQKSEELERRRKAKEEAERKLERAKSEGKIEELRKYSQAILRLSNIMVEESKKLLRAMGIPIVQAPSEGEAEAAYLNKLGLSWAAASQDYDAILFGAKRLVRNLTITGKRKLPNKDVYVEIKPELIETEILLKKLGITREQLIDIGILIGTDYNPDGIRGIGPERALKIIKKYGKIEKAMEYGEISKKDINFNIDEIRGLFLNPQVVKPEEALDLNEPNGEDIINILVYEHNFSEE... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
Q976H6 | MDLAELVEEIKKELSFAELKGKKISIDAYNALYQFLAAIRQPDGTPLMDSQGRVTSHLNGLFYRTISILEEGIIPIYVFDGKPPEQKAQELERRKKVKEEAEKKLEQAKTEGSIKTSELKKYAQMSIRLTNEMAEESKELLKAMGIPVVQAPSEGEAEAAYINILGLSWATASQDYDSLLFGAKRLIRNLTLSGKRKLPGKDVYVEIKPELIELDTLLKKLGLTREQLIDIGIIVGTDYNPDGIKGYGVKTAYRIIKKYGSLEKAIEKGEIPKIKVNFNVEEIRSLFLKPQVVEPKENLELVDCDSNKILDILVKTHDFN... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
Q9HJD4 | MGTDISDIVVSHETSLKDQGNQTFSIDTYNILYQLLSNVRQYDGMPLMDSHGNVTSHLYGIFYRTINLLENRIRPVYVFDGKPSPLKNRTISERQMMKEKAKAELEEAIERGEEDLRQYYSRINYITPQIVDDTKKLLDYMGIPYVDAPSEGEAQASYMTKKNVDGVISQDYDCLLFGARKILRNFAIYGRRKVPRKNIYKTVYPEYIILDEVLSANQINQDQLIGIGILVGTDFNEGIKGIGAKKALALIKKEGDIKSVLKHIGKNIENLDEIIDFFKNPPVVDYDFKFRKPDTDAIEHFLCDEHDFSRERIRDHLESL... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
Q7MV19 | MRLSELHTGDQAVIVRVEGRGVFRKRILEMGFVHGKTITVVQCAPLRDPVYYRIMDYNVSLRREDAAKIEVELISSNATSSPASNDIGEQSANPDSNESIPTNPTEDISAKTKSEIEIEVKPNGHVIRVALIGNPNCGKTSIFNRASGAHEHVGNYSGVTVEAKEGLFRHGDYKIEIIDLPGTYSLSPYSPEELYIRQYLSEETRPDLVLNVVDTCNLERNLYLTLQLKEMGLPVVIALNMFDEFEKKGDTFDYPALSAMLGIPMVPTVGRTGQGLPELFDTLISIHEGRNKIIRPIRINYGSIIEPAVEALTEKINNQL... | Function: Probable transporter of a GTP-driven Fe(2+) uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 94623
Sequence Length: 844
Subcellular Location: Cell inner membrane
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P00224 | ATYKVTLVTPSGSQVIECGDDEYILDAAEEKGMDLPYSCRAGACSSCAGKVTSGSVDQSDQSFLEDGQMEEGWVLTCIAYPTGDVTIETHKEEELTA | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 10334
Sequence Length: 97
Subcellular Location: Plastid
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