ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P40407 | MRKTIFAFLTGLMMFGTITAASASPDSKNQTAKKPKVQTGIDTLLPDYKKQLKGKRIGLITNPAGVNTSLKSSVDILYENPDIKLTALFGPEHGVRGDAQAGDEVGSYIDEKTGVPVYSLYGKTKKPTPEMLKNVDILMFDIQDVGTRFYTYIYTMAYAMEAAKENGIPFMVLDRPNPQGGNHIEGPILEPEYASFVGLYPIPLKHGMTIGELASLFNKEFSIDADLTVVKMKHWKRKMDFDDTRLPFVLPSPNMPTVESTFVYPATGLIEGTNISEGRGTTKPFELIGAPFIKSTELEETLNSLHLPGVTFRAASFTPTFSKHQGTLCHGVQLYVTDRDKFEAVKTGLSVIKTIHDLYPEDFEFLSTGSFDKLAGNGWIRTKIENGTSVENIINSYEKTLQQFSKTRKKYLIY | Function: Catalyzes the exo-lytic cleavage of beta-1,4-N-acetylmuramate (beta-1,4-MurNAc) from the non-reducing ends of peptidoglycan chains . Specifically hydrolyzes the natural, peptidoglycan-derived disaccharide MurNAc-GlcNAc and the artificial substrate para-nitrophenyl beta-N-acetylmuramic acid (pNP-MurNAc) . Requires a MurNAc entity at the non-reducing end, and cannot cleave GlcNAc-MurNAc . Probably plays a role in cell wall turnover and recycling .
Catalytic Activity: Hydrolysis of terminal, non-reducing N-acetylmuramic residues.
Sequence Mass (Da): 46036
Sequence Length: 414
Domain: Contains an N-terminal catalytic domain and a C-terminal auxiliary domain . A putative active site is located in a cleft within the interface of two subdomains .
Subcellular Location: Secreted
EC: 3.2.1.92
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Q8FD58 | MATNLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGSTGEAFVQSLSEREQVLEIVAEEAKGKIKLIAHVGCVSTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLDQIDTLVTLPGVGALKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVIDLLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLPELKALAQQLMQERG | Function: Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate.
Catalytic Activity: aceneuramate = N-acetyl-D-mannosamine + pyruvate
Sequence Mass (Da): 32594
Sequence Length: 297
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 1/5.
Subcellular Location: Cytoplasm
EC: 4.1.3.3
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Q9LTW4 | MYINTLFWKQNPTGDKKNQEEKMQKTLLSCLITTLLLITVADSMKDTSVRLKLAHRDTLLPKPLSRIEDVIGADQKRHSLISRKRNSTVGVKMDLGSGIDYGTAQYFTEIRVGTPAKKFRVVVDTGSELTWVNCRYRARGKDNRRVFRADESKSFKTVGCLTQTCKVDLMNLFSLTTCPTPSTPCSYDYRYADGSAAQGVFAKETITVGLTNGRMARLPGHLIGCSSSFTGQSFQGADGVLGLAFSDFSFTSTATSLYGAKFSYCLVDHLSNKNVSNYLIFGSSRSTKTAFRRTTPLDLTRIPPFYAINVIGISLGYDMLDIPSQVWDATSGGGTILDSGTSLTLLADAAYKQVVTGLARYLVELKRVKPEGVPIEYCFSFTSGFNVSKLPQLTFHLKGGARFEPHRKSYLVDAAPGVKCLGFVSAGTPATNVIGNIMQQNYLWEFDLMASTLSFAPSACT | Function: Aspartic proteinase that can use azocasein as substrate and regulates endogenous sugar levels (e.g. sucrose, glucose and fructose) by modulating starch accumulation and remobilization . Influences general morphology and development .
Sequence Mass (Da): 50568
Sequence Length: 461
Subcellular Location: Plastid
EC: 3.4.23.-
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P39370 | MNAIISPDYYYVLTVAGQSNAMAYGEGLPLPDREDAPHPRIKQLARFAHTHPGGPPCHFNDIIPLTHCPHDVQDMQGYHHPLATNHQTQYGTVGQALHIARKLLPFIPDNAGILIVPCCRGGSAFTAGSEGTYSERHGASHDACRWGTDTPLYQDLVSRTRAALAKNPQNKFLGACWMQGEFDLMTSDYASHPQHFNHMVEAFRRDLKQYHSQLNNITDAPWFCGDTTWYWKENFPHSYEAIYGNYQNNVLANIIFVDFQQQGERGLTNAPDEDPDDLSTGYYGSAYRSPENWTTALRSSHFSTAARRGIISDRFVEAILQFWRER | Function: Probably catalyzes the hydrolysis of the 9-O-acetyl group of 9-O-acetyl-N-acetylneuraminate (Neu5,9Ac2). Is required for growth of E.coli on Neu5,9Ac2, an alternative sialic acid commonly found in mammalian host mucosal sites, in particular in the human intestine.
Sequence Mass (Da): 36878
Sequence Length: 326
Subcellular Location: Periplasm
EC: 3.1.1.-
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Q8FD59 | MSTTTQNIPWYRHLNRAQWRAFSAAWLGYLLDGFDFVLIALVLTEVQGEFGLTTVQAASLISAAFISRWFGGLMLGAMGDRYGRRLAMVTSIVLFSAGTLACGFAPGYITMFIARLVIGMGMAGEYGSSATYVIESWPKHLRNKASGFLISGFSVGAVVAAQVYSLVVPVWGWRALFFIGILPIIFALWLRKNIPEAEDWKEKHGGKAPVRTMVDILYRGEHRIANIVMTLAAATALWFCFAGNLQNAAIVAVLGLLCAAIFISFMVQSTGKRWPTGVMLMVVVLFAFLYSWPIQALLPTYLKTDLAYDPHTVANVLFFSGFGAAVGCCVGGFLGEWLGTRKAYVCSLLASQLLIIPVFAIGGANVWVLGLLLFFQQMLGQGISGILPKLIGGYFDTDQRAAGLGFTYNVGALGGALAPILGALIAQRLDLGTALGSLSFSLTFVVILLIGLDMPSRVQRWLRPEALRTHDAIDGKPFSGAVPFGSAKNDLVKTKS | Function: Catalyzes the proton-dependent transport of sialic acid.
Catalytic Activity: H(+)(in) + N-acetylneuraminate(in) = H(+)(out) + N-acetylneuraminate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53584
Sequence Length: 496
Subcellular Location: Cell inner membrane
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Q8FDU9 | MYYKSAIIVRFNMDSCIQKKQVWYKHLSPRQWKIFGAAWTGYLLDGFDFVLISLVLTEVQHEFGLTTIEAASLISAAFISRWFGGLAIGALSDKMGRRMAMVLSIVLFSLGTLACGLAPGYAVMFIARIVIGLGMAGEYGSSVTYVIESWPVHLRNKASGFLISGFSIGGGLAAQVYSIVVPLWGWRSLFFVGMLPILFAFYLRKNLPESDDWQKRQQENKPVRTMVDILYREKNKYINILLSCIAFACLYVCFSGVTANAALITVMALCCAAVFISFIYQGMGKRWPTGIMLMLVVMFCFLYGWPLQAFLPTWLKVDMQYSPETVALIFMLAGFGSAAGSCIGGFMGDWLGTRKAYVISLLIGQLVIIPVFLVDRDYVWLLGLLIFTQQVFGQGIGALVPKIISGYFNVEQRAAGLGFIYNVGSLGGACAPILGAVVASHTSLGTAMCSLAFILTFVVLVLIGFDMPSRVQRWIHPEAALEYDTVDGKPFYGARKKNVAEE | Function: Catalyzes the proton-dependent transport of sialic acid.
Catalytic Activity: H(+)(in) + N-acetylneuraminate(in) = H(+)(out) + N-acetylneuraminate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55355
Sequence Length: 502
Subcellular Location: Cell inner membrane
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Q5E733 | MEAQSFGTLNYIALFAYLGAIMAVGVYFARRQKSADDYFKAGGRIPGWAAGFSVFATTLSSITFMSIPAKAYTSDWTFLIGQYVAIAILPIVFWFYIPFFRKLNLTSVYEYLERRFDVRMRLFGSISFMLFHIGRIAIVTYLTALALMPFIDISPLMIVFLIGVLCIIYTFLGGIEGVIWTDVIQGVMLSVAAILIFVVICFNVDGGIVEVFSMSNQADKYFPAEQFSWSWTDSTIPVLMIGFFFASLQQFTASQDVVQRYIVTDNIDETKKALITNAKLVACVPIFFFAVGSALFAYYTQNPELLPENFNTGGILPFYVISQMPVGVAGLIIAAIFAASQSSISSSLNSIAACFTSDIYEKVSKNPTSEQKLRIGRTLTVVAGLLGVVASTYLIMSNESEIWDAFNSLLGLMGGPMTGLFMLGIFVRRANANSALLGVVASIATVLWVRSATDLNFFFYGVIGTLMVVIVGYLTAPMFKNNLNSDEIDELSATKEKRSTTAEKA | Function: Seems to be involved in N-acetylneuraminate transport. Complements an E.coli nanT deletion mutant.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55564
Sequence Length: 505
Subcellular Location: Cell inner membrane
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P26235 | MEFIGILCLILVATTIGSHISRRFGIPAVIGQLLVGVLLGQAGLGWVHPNILVHDFSEIGVILLMFLAGLESDLSLLKKYFKPGMFVALLGILFPVFFGWLTGEAFQVANNEAIFFGIILAATSVSISVEVLKELNVVNTKEGSTILGASVVDDILVVLVLSFSLSFLTGKSTSNLPLPLLLLEQLFYFLFIFLLVKWIAPFLMSLAEKIYANSAIIIMSLVICLGMSYLADLIGLSSVIGAFFAGIAVSQTKVKHEVYNNVEALGYAVFIPVFFVSVGLEVDFSKFSEQILFILILTLVAILTKLIGGYIGAKFSSFSSNSALMVGAGMISRGEMALIILQIGQQSNLIENHYYSPLVIVVLLSTLISPLILKYFTKKVYAN | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Can also transport lithium.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41555
Sequence Length: 383
Subcellular Location: Cell membrane
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A2YQ58 | MTVEVEAVTMAKEEQPEEEEVIEKLVEKITGLAAAIGKLPSLSPSPEVNALFTELVMTCIPPSSVDVEQLGAEAQDMRGRLIRLCADAEGHLEAHYSDVLAAHDNPLDHLALFPYFNNYIQLAQLEYALLARHLPAAPPPSRLAFLGSGPLPLSSLVLAARHLPAASFHNYDICADANRRASRLVRADRDLSARMAFHTSDVAHVTTDLAAYDVVFLAALVGMAAEEKARMVEHLGKHMAPGAALVVRSAHGARGFLYPVVDPEEIRRGGFDVLAVHHPEGEVINSVIIARKPPVAAPALEGGDAHAHGHGAVVSRPCQRCEMEARAHQKMEDMSAMEKLPSS | Function: Synthesizes nicotianamine, a polyamine that is the first intermediate in the synthesis of the phytosiderophores of the mugineic acid type found in gramineae which serve as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
Catalytic Activity: 3 S-adenosyl-L-methionine = 3 H(+) + nicotianamine + 3 S-methyl-5'-thioadenosine
Sequence Mass (Da): 36983
Sequence Length: 343
EC: 2.5.1.43
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P55112 | MMTIQRYSLVFCAIFATCWTASVVNNKQVIDTSVPQTETTLNDADFHSDLHQRYDLQTLGIKVKDDPTIGNYSEGDILLESPKKFVEENNKLGRNAIKQIYRRWPNNEIPYTLSSQYGSYARSVIANAMNEYHTKTCVKFVARDPSKHHDYLWIHPDEGCYSLVGKTGGKQPVSLDSGCIQVGTIVHELMHAVGFFHEQSRQDRDSYIDVVWQNVMNGADDQFEKYNLNVISHLDEPYDYASIMHYGPYAFSGSGKKTLVPKKSGSERMGQRVKFSDIDVRKINKLYNCPGVSGNNNNNNNNQINSNSIVNHPQV | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease (By similarity). May be involved in digestion.
Sequence Mass (Da): 35743
Sequence Length: 315
Subcellular Location: Secreted
EC: 3.4.24.-
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P91828 | MDIKQLLLSIILTVSVVNGRGRRINIYGAENGKSDIVQLRGPAEQLVYSSPIRERRPIFRNALLSNSPLRWSKMQDLDGNYLIPYVISGNYDTVERDTIKTAMEKIANNTCIRLIPRTNQPDYAEINNKKGQGCYASIGRFPGKNVVMLESNDDQSCIQEDTVIHELFHVIGLWHEHMRADRDAFINVLYKNIEPAQYPQFEKLSSRDATTYSVPYDYNSVMHYDENAFAKPGKISMMTKDSKFQKVIGHPKDASSNDYKKVCAIYHCSKCMHQDFQQIVEQEHIELNNPIITNAPVQQGDSCTDRLGICPMLKSREMLNCKVMATFCCSSCSAPTSTTTTTSGTPSDGSLWQRIKSIFQ | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Sequence Mass (Da): 40772
Sequence Length: 360
Subcellular Location: Secreted
EC: 3.4.24.-
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Q9U3S9 | MLDHVLLLTYCLVSTVVRSQPSADVFRSFAGYIPEDHRVTHHEWQNSGKFQGDIDGVDPNLLKLPEGPVLFNALKNKQLTWEGGVIPYEMDTAFSPNEIKILEKAFDSYRRTTCIRFEKREGQTDYLNIVKGYGCYSQVGRTGGKQEISLGRGCFFHEIIVHELMHSVGFWHEHSRADRDDHIKINWDNILPGMKSQFDKISAVLQDLQGENYDYKSIMHYDSTAFSRNGRNTIETVENGFTQVIGTAMDLSPLDIVKINKLYSCKTKKKEKVKPATTEEPHQLIPQVVDKNSVDSGEKCVDHFADCPHFAQYCTRASFFFVMKSYCPFTCKHCPGDRKLKKSG | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Sequence Mass (Da): 39278
Sequence Length: 344
Subcellular Location: Secreted
EC: 3.4.24.-
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P55113 | MLLPWIITIVTVIPATLGHRNRVQDDEMLVISDSTDSLNLEDFEFADKLTREELFGKHIPVEVVNDFKSDIRLPRRHKRNGVSRAAKLWPNARIPYAISPHYSPHERALLAKAVKQYHEKTCIRFVPRQTGEPDYLFIGKVDGCFSEVGRTSGVQVLSLDNGCMEYATIIHEMMHVVGFYHEHERWDRDNFIDIIWQNIDRGALDQFGKVDLSKTSYYGQPYDYKSILHYDSLAFSKNGFPTMLPKVKSATIGNARDFSDVDISKINRMYNCPVEKSVTAPFARARHVPIYSPQYHKYEDRPKIPLRSFDMQQGPINPPMAQIPSQSLVVSSSSGRVNYNSNKPSSQCEDRITVCWWTADRCRSPAIYQVMSSLCPKTCKFC | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Sequence Mass (Da): 43820
Sequence Length: 382
Subcellular Location: Secreted
EC: 3.4.24.-
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Q9XFB6 | MDAQNKEVDALVQKITGLHAAIAKLPSLSPSPDVDALFTDLVTACVPPSPVDVTKLGSEAQEMREGLIRLCSEAEGKLEAHYSDMLAAFDNPLDHLGMFPYYSNYINLSKLEYELLARYVPGRHRPARVAFIGSGPLPFSSYVLAARHLPDAMFDNYDLCSAANDRASKLFRADKDVGARMSFHTADVADLTGELAAYDVVFLAALVGMAAEDKTKVIAHLGAHMADGAALVVRSAHGHVGFLYPIVDPQDIGRGGFEVLAVCHPDDDVVNSVIIAHKSKDVHANERPNGVVDSTRGAVPVVSPPCRFGEMVADVTHKREEFTNAEVAF | Function: Synthesizes nicotianamine, a polyamine that is the first intermediate in the synthesis of the phytosiderophores of the mugineic acid type found in gramineae which serve as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
Catalytic Activity: 3 S-adenosyl-L-methionine = 3 H(+) + nicotianamine + 3 S-methyl-5'-thioadenosine
Sequence Mass (Da): 35480
Sequence Length: 329
EC: 2.5.1.43
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D2KBH9 | MMNRASLCRIAVLLCILHLSHLIDSTYAQSYLTEKDFLAPLYDDDAITLSDDDFDNARKLSTEMVNSQKKRRVLSHQKYYRGDIRGRAAWTSKLKSGVRRNGVTSVIKRWPNGRIPYVISSQYNERERAVLARAFQEYHSRTCIRFVPRTSFDQDYLYIGKIDGCYSDVGRAGGRQELSLDDGCLQYNTAIHELMHSVGFYHEHERWDRDQYITILWNNIDKDAYDQFGRVDLTESSYYGQAYDYYSVMHYDSLAFSKNGFETLVAKRPEMTAVIGSAIDFSPIDLLKINKLYNCPAPNTIDISQISGNGWQGGGMGPRAPLPQVNLPLPPPPPLPTNPAIAIVGECSDRTNLCWRWLDRCRSYFFEKIMKEFCALSCGYCVPTNAVSKAAPAIPLQPTLSIAEGPEGPMPPLYQRFG | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Catalytic Activity: Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'.
Sequence Mass (Da): 47458
Sequence Length: 418
Subcellular Location: Secreted
EC: 3.4.24.21
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P91137 | MIFLLFVVFPFVYAQLLPELLAGFQNGRFRGGPDGFNRGPGGFHRGPDGFGGDPRGGVDLGHLIGNIAANVGQEMGLNDADVIGDLRGISRGPRPSSMEWGRRARHFCRRYPGHPKCQRGQLPQFTDVPTIINTIIYNAGDLLPRVPTLNIHDPLAGLNSELVGFIKSLQSQFGQLSSQQRNEIHDSCRSFKCDQQSPQNTQAKQELLTKMLAFDQAVGGKAAPAHDKVNLRFDRTQQVKQALLKRANLSHIIVPADNGVFDRDVLLTEHQANFLLNELGEAGRGADVGAGGGGGGRVPRSGVFFQESAVQKWDIWKPIQYTLDDSLEESDKKDIRDALHEISINTCILFRYNATPKGYHLNYMKVDSTTFCGLSYVGRTDPANPIYLSFQCGDNRGVAMHETMHALGVSHQHLRLDRDKYIKIDWSNIDPQHYDTFAISDAKLYTSYGTKYAYDSIMHYNAYLGAKDPNKPTMIPLVNPQENTPKLGQRAKLTRGDIRLLKKMYCRPGCDDQNVHCGTWALHGYCKMKEQMKWMNENCKASCDKC | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Sequence Mass (Da): 60977
Sequence Length: 546
Subcellular Location: Secreted
EC: 3.4.24.-
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Q9XFB7 | MGMEGCCSNKKVMEEEALVKKITGLAAAIGELPSLSPSPEVNALFTELVTSCIPPSTVDVDALGPDAQEMRARLIRLCADAEGHLEAHYSDLLAAHDNPLDHLTLFPYFNNYIKLSQLEHGLLARHVPGPAPARVAFLGSGPLPLSSLVLAARHLPDASFDNYDISGEANERASRLVRADADAGARMAFRTADVADVTTELEGYDVVFLAALVGMAAEEKARLVEHLGRHMAPGAALVVRSAHGARGFLYPVVDPEEIRRGGFEVLTVHHPEDEVINSVIIARKAAAPPPVAADRDVPVNMPMPAQCAVAVSRPCLGCACELGARAHQKMKEIAMEEMEA | Function: Synthesizes nicotianamine, a polyamine that is the first intermediate in the synthesis of the phytosiderophores of the mugineic acid type found in gramineae which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
Catalytic Activity: 3 S-adenosyl-L-methionine = 3 H(+) + nicotianamine + 3 S-methyl-5'-thioadenosine
Sequence Mass (Da): 36313
Sequence Length: 340
EC: 2.5.1.43
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P42432 | MKLSELKTSGHPLTLLCSFLYFDVSFMIWVMLGALGVYISQDFGLSPFEKGLVVAVPILSGSVFRIILGILTDRIGPKKTAVIGMLVTMIPLLWGTFGGRSLTELYAIGILLGVAGASFAVALPMASRWYPPHLQGLAMGIAGAGNSGTLFATLFGPRLAEQFGWHIVMGIALIPLLIVFILFVSMAKDSPAQPSPQPLKSYLHVFGQKETWFFCLLYSVTFGGFVGLSSFLSIFFVDQYQLSKIHAGDFVTLCVAAGSFFRPVGGLISDRVGGTKVLSVLFVIVALCMAGVSSLPSLSMVIVLLFVGMMGLGMGNGAVFQLVPQRFRKEIGMVTGIVGAAGGIGGFFLPNILGSLKQMTGTYAIGFITFSCIALLAFALVLAAGYYWRKSWSAESSPADV | Function: May function as a nitrate transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42712
Sequence Length: 401
Subcellular Location: Cell membrane
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I3R634 | MPRNLRFLSVVNHVTKQVPTTCMRCAVGCGHVHLGSENAYGLETVRGDPSHPVNNGLACGRGIRESADPAGEWLTRPLVREDGELVQTSWSDAMARVGATIRTAVATDPDEVAVLGSGQQTNEAAYALGKLARAGIGTRNYDANTTLCMASAVTAYYRAFGSDAPPPTYDDIPNAETHLVWGANPAVAHPVMFRWIRQSATDGRLVVVDPVETKTAAVADDHVSVAPGGDLALARAILRHLVDTDQIDESFVRSNTEGFDDVVSALPSVTDAAARAGVSLDTVEELAALLDAPTLIYWGMGVNQSVRGTATAGALVNLCLASGNLGPGTGPFSLTGQANSMGTRVCSSKGTWSGHRPFEHPDHRRAVAEAWDVPVSRLPDDSGPGPVGILDSSPSVVWTVATNPLAGFPDATAAREVLRDSFLVVQDAFRSDTVELADVVLPAATWGESEGTAMNMERTVSRIRAATETPPGVRQDLDIIADVAARVAPGLLPRPPVSPSAIFDEFAALTEGTDADCSGISYTRLDGERAVRWPAPEPNSDAGYRYYDPSTSRWTFPTPSGKARFSTLDGEPLPEPVDGDYPLTLTTGREADGYNTGVRSRSDTPEEPVARVNPETVDTYHDAVADTDGELRTTVVSRRASVSVTLDRDDAVPPGLVWLSIHHPMTNQLTSPAVDPQSNEPNFKQCAVRFVHPDAPAKADFLAAEVSD | Cofactor: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.
Function: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation. Catalyzes the reduction of nitrate to nitrite, using ferredoxin as the electron donor. Can use reduced methyl viologen but neither NADPH nor NADH as electron donors.
Catalytic Activity: H2O + nitrite + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 H(+) + nitrate + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 75211
Sequence Length: 708
Pathway: Nitrogen metabolism; nitrate reduction (assimilation).
Subcellular Location: Cytoplasm
EC: 1.7.7.2
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P86702 | IPDLASSRSTLPVLTKGPTGLLGPRGPYGPLQRFNIELSARGPAAVVGVLGKSFDSWLTKLGLPGPQGRPGPPGPGCRFALSNQCIKLAVEFAGQSKFSSFLANEGKKEGPEGEEGPRTEFDGAYFAGGKFPVVGKPFPQLKVFHAEPPFPTSRSTYGPSGSQPGKKGVVTPFKGNQPLKFNDFLVESDSRCPPDDSSFERSPAVSGHSSPATLNSRMKPAGFPGKGNGAPLKNGIASDPLENLKNRLGSCFPDVLDEPPTSPFFTGPSGYTSDGLNKTPTVSKTLTAAGDPGPGAGKVLESSKTDLVALQGEFQR | Function: Involved in nacre formation. Affects morphology of calcite crystals in vitro but does not inhibit their formation. Binds chitin.
PTM: Glycosylated; contains mainly glucose, galactose, galactosamine, glucosamine and glucuronic acid.
Sequence Mass (Da): 32939
Sequence Length: 316
Subcellular Location: Secreted
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A0QAU0 | MTSPESSSAAGSGDRAVAAAAERAKLTAGRNIPSFDDLPLPADTANLREGADLSDALLALLPLVGVWRGEGEGRGHDGDYRFGQQIVVSHDGGDYLNWEARSWRLNETGDYQERGLRETGFWRFVRDPDDPSESQAIELLLAHSAGYVELFYGRPRTQSSWELVTDALARSRSGVLVGGAKRLYGIVEGGDLAYVEERVDADGGLVPHLSARLSRFAG | Cofactor: Binds 1 heme b group per subunit, that coordinates a highly solvent-exposed Fe(III) atom.
Function: Heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts peroxynitrite to nitrate. Therefore, this protein likely plays a role in peroxynitrite sensing and in the detoxification of reactive nitrogen and oxygen species (RNS and ROS, respectively). Is able to bind nitric oxide (NO) in vitro, but may act as a sensor of peroxynitrite levels in vivo.
Catalytic Activity: peroxynitrite = nitrate
Sequence Mass (Da): 23561
Sequence Length: 218
Domain: Forms a 10-stranded antiparallel beta-barrel structure able to accommodate a hydrophobic ligand in its interior. In fact, this fold hosts the heme group, which is located in a wide surface cleft.
Pathway: Nitrogen metabolism.
EC: 5.99.-.-
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A0R6J8 | MIDLHPNIAPLAPLLGTWAGPGAGEYPTIQSFEYLEEITFGHVGKPFLTYQQRTKARDDGRPLHAEVGYIRVPAPDRVEWVLAHPTGITEIQEGTLTVGGDRITMDVKATTIGLTASAKNVTALARSFRITGDELTYTLQMGAVGQPLQHHLAATLRRTPA | Cofactor: Binds 1 heme b group per subunit, that coordinates a highly solvent-exposed Fe(III) atom.
Function: Heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts peroxynitrite to nitrate. Therefore, this protein likely plays a role in peroxynitrite sensing and in the detoxification of reactive nitrogen and oxygen species (RNS and ROS, respectively). Is able to bind nitric oxide (NO) in vitro, but may act as a sensor of peroxynitrite levels in vivo.
Catalytic Activity: peroxynitrite = nitrate
Sequence Mass (Da): 17482
Sequence Length: 161
Domain: Forms a 10-stranded antiparallel beta-barrel structure able to accommodate a hydrophobic ligand in its interior. In fact, this fold hosts the heme group, which is located in a wide surface cleft.
Pathway: Nitrogen metabolism.
EC: 5.99.-.-
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O36307 | MSTLQELQENITAHEQQLVTARQKLKDAEKAVEVDPDDVNKSTLQSRRAAVSTLETKLGELKRQLADLVAAQKLATKPVDPTGLEPDDHLKEKSSLRYGNVLDVNSIDLEEPSGQTADWKAIGAYILGFAIPIILKALYMLSTRGRQTVKDNKGTRIRFKDDSSFEEVNGIRKPKHLYVSMPTAQSTMKAEEITPGRFRTIACGLFPAQVKARNIISPVMGVIGFGFFVKDWMDRIEEFLAAECPFLPKPKVASEAFMSTNKMYFLNRQRQVNESKVQDIIDLIDHAETESATLFTEIATPHSVWVFACAPDRCPPTALYVAGVPELGAFFSILQDMRNTIMASKSVGTAEEKLKKKSAFYQSYLRRTQSMGIQLDQKIIILYMLSWGKEAVNHFHLGDDMDPELRQLAQSLIDTKVKEISNQEPLKL | Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state . Inhibits IFN signaling responses directed by the dsRNA sensors RIGI and IFIH1/MDA5, probably by interacting with host E3 ubiquitin ligase TRIM21 . As a consequence, TBK1-directed IRF3 phosphorylation and TBK1 autophosphorylation are inhibited . Also displays sequence-unspecific DNA endonuclease activity (By similarity).
Sequence Mass (Da): 48042
Sequence Length: 428
Domain: The N-terminus is required for chaperone activity and, in trimeric form, this region likely serves in high affinity vRNA panhandle recognition (By similarity). The N-terminus also contains a coiled coil region, which probably participates in but is insufficient to initiate N trimerization . The YxxL motif is indispensable for the interaction with host MAP1LC3B (By similarity). The central region is involved in specific RNA-binding (By similarity). Has distinct cap- and RNA-binding sites so it can bind simultaneously both the vRNA and mRNA cap (By similarity).
Subcellular Location: Virion
EC: 3.1.-.-
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A3EXH0 | MSGRNRSRSGTPSPKVTFKQESDGSDSESERRNGNRNGARPKNNNSRGSAPKPEKPKAAPPQNVSWFAPLVQTGKAELRFPRGEGVPVSQGVDSTYEHGYWLRTQRSFQKGGKQVLANPRWYFYYTGTGRFGDLRFGTKNPDIVWVGQEGANINRLGDMGTRNPSNDGAIPVQLAGGIPKGFYAEGRGSRGNSRSSSRNSSRASSRGNSRASSRGASPGRPAANPSTEPWMAYLVQKLERLESQVSGTKPATKNPVQVTKNEAAANAKKLRHKRTAHKGSGVTVNYGRRGPGDLEGNFGDREMIKLGTDDPRFAAAAQMAPNVSSFLFMSHLSTRDEDDALWLHYKGAIKLPKDDPNYEQWTKILAENLNAYKDFPPTEPKKDKKKKEETAQDTVIFEDASTGTDQTVVKVWVKDQDAQTDDEWLGGDETVYEDEDDRPKTQRRHKKRGSTASRVTIADPTNAGAERS | Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.
PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion during infection.
Sequence Mass (Da): 51547
Sequence Length: 468
Subcellular Location: Virion
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P16285 | MDADKIVFKVNNQVVSLKPEIIVDQYEYKYPAIKDLKKPCITLGKAPDLNKAYKSVLSGMSAAKLNPDDVCSYLAAAMQFFEGTCPEDWTSYGIVIARKGDKITPGSLVEIKRTDVEGNWALTGGMELTRDPTVPEHASLVGLLLSLYRLSKISGQNTGNYKTNIADRIEQIFETAPFVKIVEHHTLMTTHKMCANWSTIPNFRFLAGTYDMFFSRIEHLYSAIRVGTVVTAYEDCSGLVSFTGFIKQINLTAREAILYFFHKNFEEEIRRMFEPGQETAVPHSYFIHFRSLGLSGKSPYSSNAVGHVFNLIHFVGCYMGQVRSLNATVIAACAPHEMSVLGGYLGEEFFGKGTFERRFFRDEKELQEYEAAELTKTDVALADDGTVNSDDEDYFSGETRSPEAVYTRIMMNGGRLKRSHIRRYVSVSSNHQARPNSFAEFLNKTYSSDS | Function: Encapsidates the genome in a ratio of one protein N per nine ribonucleotides, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases.
PTM: Phosphorylated by host CK2. Unphosphorylated protein N seems to have a better affinity for leader viral promoter encapsidation. Phosphorylation of protein N in ribonucleocapsid may stabilize the interaction with protein P, thereby playing an important role in viral transcription/replication.
Sequence Mass (Da): 50603
Sequence Length: 450
Subcellular Location: Virion
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P0DTC9 | MSDNGPQNQRNAPRITFGGPSDSTGSNQNGERSGARSKQRRPQGLPNNTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANKDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRNSSRNSTPGSSRGTSPARMAGNGGDAALALLLLDRLNQLESKMSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYTGAIKLDDKDPNFKDQVILLNKHIDAYKTFPPTEPKKDKKKKADETQALPQRQKKQQTVTLLPAADLDDFSKQLQQSMSSADSTQA | Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M . Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.
PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion during infection.
Sequence Mass (Da): 45626
Sequence Length: 419
Subcellular Location: Virion
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Q9YDY1 | MAVTVAVGTSNPIKYRAVLRAFSRYYDVRVVMVSVDSGVGPQPSGVADVVGGALARAVRAVEKADSYFGVGVEAGPIEFPASGGYVETQVAAIVDRDCRATIGMSPSFEVDRRVLALMLDGVEMEKAVGVERHGGLGESVGFVGVATSGAVTRQDLTEHAVIMALIPRLMGYGSIATVEEIAAQAGASVECRSTRAI | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = H(+) + phosphate + XDP
Sequence Mass (Da): 20449
Sequence Length: 197
EC: 3.6.1.73
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O29361 | MGSKNPTKIEGARRAFEQYFDDVEIVGVEVSTSAPPQPFDAETVRGAIERAKKAYSPDFDFSVGIEAGLFRSECTITGYLDFQVAAVYDGERCTIGFGPGFEYPKLVVEEVLKGKEVGEVMEKVSGIKNLGKKVGAVHYLSKGAISRTDLSRISVTMALIPFINREMYL | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = H(+) + phosphate + XDP
Sequence Mass (Da): 18543
Sequence Length: 169
EC: 3.6.1.73
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A8MA42 | MKVALASRNPSKVKAVEEALRILNINGTVEAVDPPPGIPPEPMGLEATVNGAVVRARHALSSIKDSTYGIGIEAGVLMLSAFNVNFDVTVAAVIDRKGLITLGLSPAFMIPPAFMRELMTGKELNDVVEKYYGVPNAGKGIGFIGLLSRGLIKRINLNTEAVYMALLPRMPWNKDLYELSD | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = H(+) + phosphate + XDP
Sequence Mass (Da): 19477
Sequence Length: 181
EC: 3.6.1.73
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Q94BV7 | MRNFSVFERFSKAFKDHPSLTRILVVSTISGGGLIAYSEANASYGANGGAVVETGTKKKKVVLLGTGWAGTSFLKNLNNSQYEVQIISPRNYFAFTPLLPSVTCGTVEARSVVEPIRNIGRKNVDTSYLEAECFKIDPASKKVYCRSKQGLSSNGKKEFSVDYDYLVIATGAQSNTFNIPGVEENCHFLKEVEDAQRIRKTVIDSFEKASLPELSDEERKRILHFVVVGGGPTGVEFAAELHDFVTEDLVSLYPRAKGSVRITLLEAADHILTMFDKRITEFAEEKFSRDGIDVKLGSMVTKVNEKDISAKTKGGEVSSIPYGMIVWSTGIGTRPVIKDFMKQIGQGNRRALATDEWLRVEGTDNIYALGDCATINQRKVMEDVSAIFSKADKDKSGTLTLKEFQEAMDDICVRYPQVELYLKSKRMRGIADLLKEAETDDVSKNNIELKIEEFKSALSQVDSQVKFLPATAQVAAQQGAYLAKCFDRMEECEKSPEGPIRMRGEGRHRFRPFRYRHLGQFAPLGGEQTAAQLPGDWVSIGHSSQWLWYSVYASKQVSWRTRVLVVSDWMRRFIFGRDSSSI | Cofactor: Binds 1 FAD per subunit.
Function: Alternative NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH does not translocate protons across the inner mitochondrial membrane (By similarity). Calcium-dependent NAD(P)H dehydrogenase; more efficient on NADH. Binds calcium ions.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65059
Sequence Length: 582
Subcellular Location: Mitochondrion inner membrane
EC: 1.6.5.9
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O64725 | MAKPLGTTGEFFRRRDEWRKHPMLSNQMRHALPGIGIGVGAFCVYLVGEQIYSKLMAPSSQSSHQKQPAPSH | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8051
Sequence Length: 72
Subcellular Location: Mitochondrion inner membrane
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Q9M9R9 | MAKPLGTTGEFFRRRDEWRKHPMLSNQMRHALPGLGIGVAAFCVYLVGEQIYNKALAPSKSSHHHQEQTAPSH | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8224
Sequence Length: 73
Subcellular Location: Mitochondrion inner membrane
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Q8MMJ7 | MKTQFAILLVALVLFQMFAQSDAILGKIWEGIKSLFGKRGLSDLDGLDELFDGEISKADRDFLRELMR | Function: Shows weak hemolytic activity and antibacterial activity against both Gram-positive and Gram-negative bacteria probably by forming pores in the cell membrane. IsCT adopts an amphipathic alpha-helical structure.
PTM: IsCTf is an enzymatic proteolytic cleavage product of IsCT by the proteases present in the venom.
Sequence Mass (Da): 7722
Sequence Length: 68
Subcellular Location: Secreted
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Q0QLF4 | MKDFEFFAPKTLEEAKGLLHQYKDVPPAIIAGGTDLVIEINDRWEKPDVVIDIKKLKELEYIRVEENTIHIGALSTFTQIENHPFIRSHVRALYKAASQVGSPQIRNLGTIGGNLSTSSVAGDGVSAMTTLDATVVLESVRGTRQMKLTDFFDGEGFKRRNALEADEIMTEVIIDRPDAHSASAFYKLAKRKSLAISVIGGGMAVKVDDAGVCTWASMRGGCIGRYPLHFKQAEEMLVGAPLTMETMEATLPILHDTVYDMARARPSVLYKKESVQGVFKKLFVDILDQLEGGCNE | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the hydroxylation of nicotinate to 6-hydroxynicotinate. Also active against 2-pyrazinecarboxylic acid, but inactive against other nicotinate analogs.
Catalytic Activity: H2O + NADP(+) + nicotinate = 6-hydroxynicotinate + H(+) + NADPH
Sequence Mass (Da): 32622
Sequence Length: 296
Pathway: Cofactor degradation; nicotinate degradation; 6-hydroxynicotinate from nicotinate: step 1/1.
EC: 1.17.1.5
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O14121 | MLFSRSILRGMPKAGIPKSPLALSASRNLRLANSVRFASDAASSPKSTTSKWKILKRTTLGLFATAVVLYGANVYRFRHPDPHQPLPDPSKKTLVVLGAGWGATSILRTIDTSLFNVIVVSPRNYFLFTSLLPSTATGSVHTRSIVQPIRYMLRHKSCYVKFYEAECTDVDADKKVIHIKKTTTDGVDLEQEIKYDYLVCSHGAETQTFNIPGIAEYGCFLKEIWDAQKIRARILHCLEQAQFKDLPAETRRRYVHTVVVGGGPTGMEFAGEMADFIEDDLKSWYPELADDFAVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRTNTALKKVTAENIHVEVKNPDGSKQEEVIPYGLLVWAGGNRARPLTKKLMEGSEEQNNRRGLVVDEYLKLKGYKDIFALGDCTHTAYAPTAQVASQQGAYLGQLFNKLGSLNFEKPSEDRHIALGDEMDSSTLISLANEKHASTKVFLPFKYSHQGSLAYVGHEKAIADIEVPWFGKQLHASGALAFYFWRSVYLSELYSLRNRTNVTLDWIRVKLFGRDISSL | Function: Catalyzes the oxidation of NADH.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Sequence Mass (Da): 61675
Sequence Length: 551
Subcellular Location: Mitochondrion
EC: 1.6.5.9
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P40215 | MIRQSLMKTVWANSSRFSLQSKSGLVKYAKNRSFHAARNLLEDKKVILQKVAPTTGVVAKQSFFKRTGKFTLKALLYSALAGTAYVSYSLYREANPSTQVPQSDTFPNGSKRKTLVILGSGWGSVSLLKNLDTTLYNVVVVSPRNYFLFTPLLPSTPVGTIELKSIVEPVRTIARRSHGEVHYYEAEAYDVDPENKTIKVKSSAKNNDYDLDLKYDYLVVGVGAQPNTFGTPGVYEYSSFLKEISDAQEIRLKIMSSIEKAASLSPKDPERARLLSFVVVGGGPTGVEFAAELRDYVDQDLRKWMPELSKEIKVTLVEALPNILNMFDKYLVDYAQDLFKEEKIDLRLKTMVKKVDATTITAKTGDGDIENIPYGVLVWATGNAPREVSKNLMTKLEEQDSRRGLLIDNKLQLLGAKGSIFAIGDCTFHPGLFPTAQVAHQEGEYLAQYFKKAYKIDQLNWKMTHAKDDSEVARLKNQIVKTQSQIEDFKYNHKGALAYIGSDKAIADLAVGEAKYRLAGSFTFLFWKSAYLAMCLSFRNRVLVAMDWAKVYFLGRDSSI | Function: External NADH dehydrogenase required for optimum cellular growth with a number of nonfermentable carbon sources, including ethanol. With NDE2, performes the mitochondrial oxidation of cytosolic NADH under these growth conditions. Regulates the mitochondrial glycerol-3-phosphate dehydrogenase, GUT2, also involved in cytosolic NADH oxidation.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Sequence Mass (Da): 62774
Sequence Length: 560
Subcellular Location: Mitochondrion intermembrane space
EC: 1.6.5.9
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O43090 | MSVSKARLQSVVRLSRTVPYSKTMVRSFHVSCAVKNSGNVPTPRNKSFFSRALEMAEVTSSLSMLGAVALFQSLRRLNNSSPKGKSGVPKKNIVVLGSGWGAVAAIKNLDPSLYNITLVSPRDHFLFTPMLPSCTVGTLRLPSITEPIVALFKGKIDPSNIHQAECTAIDTSAKKVTIRGTTEANEGKEAVIPYDTLVFAIGAGNQTFGIQGVRDHGCFLKEAGDAKKVFNRIFEILEQVRFNKDLSPEERARLLHITVVGGGPTGMEFAAEMQDFIDNDVKDMFPELQKDIHVTLIEAAPGVLPMFTKSLITYTENLFKNLNIKIMTKTVVKDVNEKNLIVQKTNPDGSKAMQEIPYGMLVWAAGITARPLTRTLMSSIPEQSGARKGLIVDEFFRVKGVPEMYAVGDCAFSGLPATAQVANQQGAWLAKNLNVEGKKFALHERIQALEKQLGEKEAPSQVAGLKQQVEQLKLEPFKYHHQGALAYVGDEKAIADLKLPFMKKMLPLQGIVGHTFWRLAYLNELISARSQFMVLIDWLKTRLFGRYDAKV | Function: Catalyzes the oxidation of NADH.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Sequence Mass (Da): 60781
Sequence Length: 551
Subcellular Location: Mitochondrion
EC: 1.6.5.9
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F2Z699 | MLRLRPAVRAVSVARSVALTRSLHVSVAKFNKIEGTAPAGLPKEVKQTAGHQGHHQEIPKPDENHPRRKKFHFWRSLWRLTYLSAIASLGYIGYRIYVIRNPSDQLPADPSKKTLVVLGSGWGSVSFLKKLDTSNYNVIVVSPRNYFLFTPLLPSCPTGTIEHRSIMEPIRGIIRHKQAECQYLEADATKIDHEKRIVTIRSAVSENSKEEVIKEIPFDYLVVGVGAMSSTFGIPGVQENACFLKEIPDAQQIRRTLMDCIEKAQFEKDPEVRKRLLHTVVVGGGPTGVEFAAELQDFFEDDLRKWIPDIRDDFKVTLVEALPNVLPSFSKKLIDYTEKTFSDEKISILTKTMVKSVDENVIRAEQTKGDGTKETLEMPYGTLVWATGNTVRPVVRELMSKIPAQKGSRRGLLVNEYLVVEGTEGIWALGDCSATKYAPTAQVASQEGSYLANLLNGIAKTEDLNNEITNLEKQSEHTFDEQERKNIFAQLESKSRKLRRSRAMLPFEYSHQGSLAYIGSDRAVADLSFNFWGIMNWSSGGTMTYYFWRSAYVSMCFSMRNKILVCIDWMKVRVFGRDISRE | Cofactor: Binds 1 FAD per subunit.
Function: Alternative NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH does not translocate protons across the inner mitochondrial membrane.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65815
Sequence Length: 582
Subcellular Location: Mitochondrion inner membrane
EC: 1.6.5.9
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P95200 | MTLSSGEPSAVGGRHRVVIIGSGFGGLNAAKALKRADVDITLISKTTTHLFQPLLYQVATGILSEGDIAPTTRLILRRQKNVRVLLGEVNAIDLKAQTVTSKLMDMTTVTPYDSLIVAAGAQQSYFGNDEFATFAPGMKTIDDALELRGRILGAFEAAEVSTDHAERERRLTFVVVGAGPTGVEVAGQIVELAERTLAGAFRTITPSECRVILLDAAPAVLPPMGPKLGLKAQRRLEKMDVEVQLNAMVTAVDYKGITIKEKDGGERRIECACKVWAAGVAASPLGKMIAEGSDGTEIDRAGRVIVEPDLTVKGHPNVFVVGDLMFVPGVPGVAQGAIQGARYATTVIKHMVKGNDDPANRKPFHYFNKGSMATISRHSAVAQVGKLEFAGYFAWLAWLVLHLVYLVGYRNRIAALFAWGISFMGRARGQMAITSQMIYARLVMTLMEQQAQGALAAAEQAEHAEQEAAG | Cofactor: Binds 1 FAD per subunit.
Function: Alternative, nonproton pumping NADH:quinone oxidoreductase that delivers electrons to the respiratory chain by oxidation of NADH and reduction of quinones.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 50385
Sequence Length: 470
Subcellular Location: Cell inner membrane
EC: 1.6.5.9
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Q2MI46 | MLPMITEFINYGQQTIRAARYIGQGFMITLSHANRLPVTIQYPYEKLITSERFRGRIHFEFDKCIACEVCVRVCPIDLPVVDWKLETDIRKKRLLNYSIDFGICIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQIALGRLPMSVIDDYTIRTISNLPQINNE | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19538
Sequence Length: 167
Subcellular Location: Plastid
EC: 7.1.1.-
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Q2PMN6 | MFLMVSGFINYSQQTVRAARYIGQGFTITLSHANRLPVTIQYPYEKIISSERFRGRIHFEFDKCIACEVCVRVCPIDLPVVDWKLETDIRKKQLLNYSIDFGICIFCGNCIEYCPTNCLSMTEEYELSTYDRHELNYNQIALGRLPVSVIDDYTIRTIQIKFN | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19034
Sequence Length: 163
Subcellular Location: Plastid
EC: 7.1.1.-
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P56756 | MNSIKFPILDRTTKNSVISTTLNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDAITKLRKKIAREIYKDRIRPQQGNRCFTTNHKFFVVRSPHIGNYDQELLYPPSSTSEISTETFFKYKSPVSSHELVN | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25366
Sequence Length: 225
Subcellular Location: Plastid
EC: 7.1.1.-
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Q7YJW8 | MNSTEFPLLDRTTQNSVISTTLNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDAITKLRKKVSREIYQDRIGSQQENRCFTTNHKFHIERSTHTGNYGQGLLYQSPSTSEIPSETFFKYKSSVSSHELMN | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25265
Sequence Length: 225
Subcellular Location: Plastid
EC: 7.1.1.-
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Q9S829 | MAFSATVSQLSSLSTISSSLPISSRRLPHRSLPQFTVKAEAEKEKQSTQGKSDGEASPAATKTPKTLPKKPVYSMKKGQIVRVEKEKYLNSINYLSVGHPPFYKGLDYIYEDRGEVLDLRVFETGEYALVGWVGIPTAPAWLPTDMLIKCEKLVYERM | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17657
Sequence Length: 158
Subcellular Location: Plastid
EC: 7.1.1.-
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B0JRM7 | MAATIKKGALVRVVTGNLENSLEALASDRRLPSYMFNSTAEVLDVKDDYALIKFYVPTPSVWLKLEQLEPV | Function: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7927
Sequence Length: 71
Subcellular Location: Cellular thylakoid membrane
EC: 7.1.1.-
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B1X470 | MNEFQTESFVSLKPYDLVKVNRGAYVGSLEARASDPIPPAYIFEGPGTLITTAGQYSLVRWHLIPAPDVWLATAQLEAYSED | Function: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 9074
Sequence Length: 82
Subcellular Location: Plastid
EC: 7.1.1.-
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Q7VE72 | MSVTPSPIETNAPKPLKKGSLVRVNPEAYKNSLESLASDQSSPEYIFEGPGELVAIKQDYGQVRWRRPVPDVWLRLDQLQAWTEGS | Function: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 9654
Sequence Length: 86
Subcellular Location: Cellular thylakoid membrane
EC: 7.1.1.-
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O51419 | MLLQKTLCIVKPDGVRRGLIGDVVSRFERVGLKMVAAKMLIVDESLAKKHYLYDDIVFRHSEAVWNSLIKFISNSPVFTFVVEGVESIEVVRKLCGATEPKLAIPGTIRGDFSYHSFKYSNEKGFSIYNVIHASANEADAMREIPIWFKDNEILNYKRDDECEHYYC | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 19159
Sequence Length: 167
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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Q89MS3 | MAIERTFSIIKPDATARNLTGAVNAVIEKAGLRIVAQKRIRMTKEQAETFYAVHKARPFFGELVEFMTSGPVVVQVLEGENAVAKYRDAMGATDPSKAAEGTIRKLYAKSIGENSAHGSDAPETAAIEIAQFFSGNEIVG | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 15059
Sequence Length: 140
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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P48817 | MSNTKERTFICIKPDAVQRGLIGKIFERFEQRGYKLVAMKMLKATKSHLEIHYQELQGKPFFNDLVGYMSSGPVIAMVWEGLDVVKQARQMLGATNPLNSMPGTIRGDFSIQTGRNIVHGSDSLPSAEREITHWFKPEELCEWSSATATWVYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 17383
Sequence Length: 153
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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B9M699 | MERTFAIIKPDAVERNISGKVLDRIEGAGFKIVGMKKIHLTKKEAEGFYYVHKERPFFNDLCTFMSRNPVIVLALEKDNAIAAWRELMGATNPANADAGTIRKDLGVSIEENTVHGSDSPESAAFEIPYFFSSLELV | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 15265
Sequence Length: 137
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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Q74E54 | MERTFAIIKPDAVERNIIGKILEKVETAGFRIVGMKKILLSKCEAEGFYYVHKERPFFNDLCSFMSRSPVVVMVLERENAINTWREVMGATNPANAEAGTIRKDFGLSIEENSVHGSDSPESAAYEIPYFFSQLELL | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 15498
Sequence Length: 137
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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B8F3E4 | MIQQTLAIIKPDATKRHLIGEILSYMEKNGLAIKALKMLHLTKEQTEGFYAEHQGKDFFDPLVAFMISEPIVVAVLEGENAVENYRLLMGATKPEERKLGTIRKMFGLGYRENAVHGSDSETSAKREIAYFFTPSEIV | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 15563
Sequence Length: 138
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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Q0BQG5 | MAIERTFSIIKPDATRRNLTGRINAVFEENGLRIVAQKRVQLSQAQAEAFYGVHRERPFFNDLVSFMISGPVVVQVLEGENAVARNRELMGATDPKKADAGTIRAQFAESIEANSVHGSDSAENAAIEIAYFFAGSEIVA | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 15300
Sequence Length: 140
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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Q7VMD0 | MLQQTLCLIKPDATQRNLIGKIISYLENAGLKIKAIKKLQLTQAQAEKFYLEHQDKPFFASLVGFMISAPIVAIVLEGENAIAHYRELMGATNPEQREAGTIRALYAISNQENSVHGSDSETSAKREIDYFFSKEEIC | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 15464
Sequence Length: 138
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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Q7UJK7 | MQRTLVLLKPDCVQRRLIGDVLSRFEAKGLHIVAMKLLQVTPELSKQHYAEHVEKPFYPSLEEFITSAPVVAIALEGLEVIRVVRDMLGATNGLQAAPGTLRGDYSSSRQMNLVHASDSEESAQRELDLYFNADEFCDYSLVLTPFMRADDE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 17085
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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Q8C119 | MELFYWCLLCLLLPLTSRTQKLPTRDEELFQMQIRDKEFFHDSSVIPDGAEVSSYLFRDTPRRYFFMVEEDNTPLSVTVTPCDAPLEWKLSLQELHEGSSADGSGDPELLDQQKQQMTDVEGTELFSYKGNDVEYFLSSSSPSGLYQLELLSTEKDTHFKVYATTTPESDQPYPELPYDPRVDVTSFGRTTVTLAWKPSPTASILKQPIEYCVVINKEHNFKSLCAAETKMNADDAFMVAPKPGLDFNPFDFAHFGFPTDNLGKDRSLLAKPSPKVGRHVYWRPKVDIQKICIGNKNIFTVSDLKPDTQYYFDVFMVNTNTNMSTAYVGAFVRTKEEAKQKTVELKDGRVTDVFVKRKGKKFLRFAPVSSHQKVTFFIHSCMDAVQVQVRRDGRLLLSQNVEGIRQFQLRGKPKGKYLIRLKGNRKGASKLKILATTRPSKHAFPSLPEDTRIKAFDKLRTCSSVTVAWLGTQERRKFCIYRKEVDGNYSEDQKRREQNQCLGPDTRKKSEKVLCKYFHSQNLQKAVTTETIRDLQPGKSYLLDVYVVGHGGHSVKYQSKIVKTRKVC | Function: Secretory protein that plays a role in various cellular processes. Acts as a chemorepellent acting on gonadotropin-releasing hormone (GnRH) expressing neurons regulating their migration to the hypothalamus . Also promotes neuron migration, growth and survival as well as neurite outgrowth and is involved in the development of the olfactory system . May also act through the regulation of growth factors activity and downstream signaling (By similarity). Also regulates extracellular matrix assembly and cell adhesiveness . Promotes endothelial cell survival, vessel formation and plays an important role in the process of revascularization through NOS3-dependent mechanisms .
PTM: O-glycosylated; contains heparan sulfate and chondroitin sulfate.
Sequence Mass (Da): 65027
Sequence Length: 568
Subcellular Location: Secreted
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P0A185 | MTVKWIEAVALSDILEGDVLGVTVEGKELALYEVEGEIYATDNLCTHGSARMSDGYLEGREIECPLHQGRFDVCTGKALCAPVTQNIKTYPVKIENLRVMIDLS | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene . Functions as an intermediate electron transfer protein via a specific interaction with iron sulfur protein components (ISP) (NdoB and NdoC) . Also able to catalyze the cis-dihydroxylation of biphenyl and phenanthrene .
Sequence Mass (Da): 11446
Sequence Length: 104
Pathway: Aromatic compound metabolism; naphthalene degradation.
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P0A110 | MNYNNKILVSESGLSQKHLIHGDEELFQHELKTIFARNWLFLTHDSLIPAPGDYVTAKMGIDEVIVSRQNDGSIRAFLNVCRHRGKTLVSVEAGNAKGFVCSYHGWGFGSNGELQSVPFEKDLYGESLNKKCLGLKEVARVESFHGFIYGCFDQEAPPLMDYLGDAAWYLEPMFKHSGGLELVGPPGKVVIKANWKAPAENFVGDAYHVGWTHASSLRSGESIFSSLAGNAALPPEGAGLQMTSKYGSGMGVLWDGYSGVHSADLVPELMAFGGAKQERLNKEIGDVRARIYRSHLNCTVFPNNSMLTCSGVFKVWNPIDANTTEVWTYAIVEKDMPEDLKRRLADSVQRTFGPAGFWESDDNDNMETASQNGKKYQSRDSDLLSNLGFGEDVYGDAVYPGVVGKSAIGETSYRGFYRAYQAHVSSSNWAEFEHASSTWHTELTKTTDR | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The alpha subunit has a catalytic role in the holoenzyme. Also able to catalyze the cis-dihydroxylation of biphenyl and phenanthrene .
Catalytic Activity: H(+) + NADH + naphthalene + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD(+)
Sequence Mass (Da): 49608
Sequence Length: 449
Pathway: Aromatic compound metabolism; naphthalene degradation.
EC: 1.14.12.12
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Q6NPS8 | MGEKQRKLLVLYASQTGNALDAAERIGREAERRGLPASVVSTDEFDTSSLPHHEEAVVFVVSTTGQGDSPDSFKAFWRFLLQRNLGNYWLQQVRYAVFGLGDSGYQKYNFVAKKLDKRLSDLGATTIIEKGLGDDQHPSGYEGTLDPWMLSLWRTLYQINPKYFPKGPDVKIPQDEVIDKPKYRILFHKQEKLEPKLLSDSDIIQRARGMSPGKLFKDKSKPDCFLKMTRNEVLTKAESTKDVRHFEFQFVSSTIEYEVGDVVELLPSQNSSVVDAFIERCGLDPESFITVGPRETENSSFSEEMITQIPIKLKTFVELTMDVTSASPRRYFFEIMSFYATAEHEKERLQYFASPEGRDDLYNYNQKERRSILEVLEDFPSVQIPFDWLVQLVPPLKPRAFSISSSPLAHPAAVHLTVSIVSWITPYKRTRKGLCSSWLASLAPEQEVNIPVWFHKGSLPAPSQSLPLILVGPGTGCAPFRGFIAERAVQAQSSPVAPVMFFFGCRNKDTDFLYRDFWESHAREGGMLSEGKGGGFYTAFSRDQPKKVYVQHKIREMSKRVWDLLCDGAAVYVAGSSTKMPCDVMSAFEDIVSEETGGGSKEVASRWLKALEKTGRYNVEAWS | Function: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of the anamorsin/DRE2 homolog, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins (By similarity). Catalyzes the NADP-dependent reduction of cytochrome c, but not cytochrome P450 in vitro. Required for embryo development .
Catalytic Activity: NADPH + 2 oxidized [2Fe-2S]-[protein] = H(+) + NADP(+) + 2 reduced [2Fe-2S]-[protein]
Sequence Mass (Da): 70412
Sequence Length: 623
Subcellular Location: Cytoplasm
EC: 1.18.1.-
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Q86IZ2 | MVGYRQKWVQDLPPAGGFPKLKYARTSTSPIPGAYIFAGVFSIMAVGTYIFFSDKVERNAREEEEKRRLSMILPILQAENDINFLASPHQNVYFTRWMPPQTGKRAAALLRDL | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12894
Sequence Length: 113
Subcellular Location: Mitochondrion inner membrane
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Q9P0J0 | MAASKVKQDMPPPGGYGPIDYKRNLPRRGLSGYSMLAIGIGTLIYGHWSIMKWNRERRRLQIEDFEARIALLPLLQAETDRRTLQMLRENLEEEAIIMKDVPDWKVGESVFHTTRWVPPLIGELYGLRTTEEALHASHGFMWYT | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis . Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone . Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16698
Sequence Length: 144
Subcellular Location: Mitochondrion inner membrane
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Q9ERS2 | MAASKVKQDMPPPGGYGPIDYKRNLPRRGLSGYSMFAVGIGALIFGYWRMMRWNQERRRLLIEDLEARIALMPLFQAEKDRRTLQILRENLEEEAIIMKDVPNWKVGESVFHTTRWVPPLIGEMYGLRTKEEMSNANFGFTWYT | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16860
Sequence Length: 144
Subcellular Location: Mitochondrion inner membrane
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Q02378 | MNLLQVVRDHWVHVLVPMGFVFGYYLDRKNDEKLTAFRNKSLLYKRELKPNEEVTWK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6966
Sequence Length: 57
Subcellular Location: Mitochondrion inner membrane
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O75438 | MVNLLQIVRDHWVHVLVPMGFVIGCYLDRKSDERLTAFRNKSMLFKRELQPSEEVTWK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6961
Sequence Length: 58
Subcellular Location: Mitochondrion inner membrane
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P0DN34 | MTLFQLLREHWVHILVPAGFVFGCYLDRKDDEKLTAFRNKSMLFQRELRPNEEVTWK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6954
Sequence Length: 57
Subcellular Location: Mitochondrion inner membrane
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Q8LDK3 | MGGGGHGGGITYKGVTVHTPKTWHTVTGKGLCAVMWFWILYRAKQDGPVVMGWRHPWDGHGDHGHGDHH | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7568
Sequence Length: 69
Subcellular Location: Mitochondrion inner membrane
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Q20412 | MLGNKFVAQLALQHLRNRGLVNSPSRLTFVRNRFAWGSDAVGPNVPVGGKMGASENPELHTYDGDYRGTISKGDKPIPDYFYRTPTTGRTYIDRCVTYFISAVIWAWFSYHMYYHSGHLLGHWYMPYLSEFTDEELGIPKDSAEDPEYWGNHKKEYGTYR | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18486
Sequence Length: 160
Subcellular Location: Mitochondrion inner membrane
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Q9VWI0 | MSALRQVMCRSTASLQLYQANRAAAARWASTATDGGPLDPKTALARPEELEQRNKLSGKITVPTAVNLSPISGVPEEHIRERRVRIHIPPKNAMQSGTDNVNTWQIEFDNRERWENPLMGWASSGDPLSNMNVQFGSPEEAITFCERNGWRWYVDGAAKPKKERVKNYGINFAWNKRTRVSTK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20681
Sequence Length: 183
Subcellular Location: Mitochondrion inner membrane
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O43181 | MAAVSMSVVLRQTLWRRRAVAVAALSVSRVPTRSLRTSTWRLAQDQTQDTQLITVDEKLDITTLTGVPEEHIKTRKVRIFVPARNNMQSGVNNTKKWKMEFDTRERWENPLMGWASTADPLSNMVLTFSTKEDAVSFAEKNGWSYDIEERKVPKPKSKSYGANFSWNKRTRVSTK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20108
Sequence Length: 175
Subcellular Location: Mitochondrion inner membrane
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Q9CXZ1 | MAAVSISVSLRQAMLGRRAMATAAVSVCRVPSRLLSTSTWKLADNQTRDTQLITVDEKLDITTLTGVPEEHIKTRKVRIFVPARNNMQSGVNNTKKWKMEFDTRERWENPLMGWASTADPLSNMVLTFSAKEDAIAFAEKNGWSYDVEEKKVPKPKSKSYGANFSWNKRTRVSTK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19785
Sequence Length: 175
Subcellular Location: Mitochondrion inner membrane
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Q5XIF3 | MAAVSMSVSLRQALLRQRAVATAAVSVCRVPSRLLNTSTWKLADGQTRDTQLITVDEKLDVTPLTGVPEEHIKTRKVRIFVPARNNMQSGVNNTKKWKMEFDTRERWENPLMGWASTADPLSNMVLTFSAKEDAVAFAEKHGWSYDVEGRKVPKPKSKSYGANFSWNKRTRVSTK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19741
Sequence Length: 175
Subcellular Location: Mitochondrion inner membrane
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Q02379 | MPFFDVQKRLGVDLDRWMTIQSAEQPHKIPSRCHAFEKEWIECAHGIGSIRAEKECKIEFEDFRECLLRQKTMKRLHAIRRQREKLIKEGKYTPPPHHSGQEEPRS | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12668
Sequence Length: 106
Domain: Contains two C-X9-C motifs that are predicted to form a helix-coil-helix structure, permitting the formation of intramolecular disulfide bonds.
Subcellular Location: Mitochondrion inner membrane
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O43920 | MPFLDIQKRFGLNIDRWLTIQSGEQPYKMAGRCHAFEKEWIECAHGIGYTRAEKECKIEYDDFVECLLRQKTMRRAGTIRKQRDKLIKEGKYTPPPHHIGKGEPRP | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12518
Sequence Length: 106
Domain: Contains two C-X9-C motifs that are predicted to form a helix-coil-helix structure, permitting the formation of intramolecular disulfide bonds.
Subcellular Location: Mitochondrion inner membrane
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Q4R3M6 | MPFLDIQKRFGLNIDRWWTIQSAEQPYKLAPRCHAFEKEWIECAHGIGAIRAEKECKIEYDDFIECLLRQKTMRRVNAIRRQRDKLIKEGKYTPPPHHIGKGEPRP | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12644
Sequence Length: 106
Domain: Contains two C-X9-C motifs that are predicted to form a helix-coil-helix structure, permitting the formation of intramolecular disulfide bonds.
Subcellular Location: Mitochondrion inner membrane
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Q99LY9 | MPFLDIQKKLGISLDRHFMFLSAEQPYKNAARCHAFEKEWIECAHGIGGTRAKKECKIEFDDFEECLLRYKTMRRMHDIKKQREKLMKEGKYTPPPHHSGREEPRP | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12648
Sequence Length: 106
Domain: Contains two C-X9-C motifs that are predicted to form a helix-coil-helix structure, permitting the formation of intramolecular disulfide bonds.
Subcellular Location: Mitochondrion inner membrane
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P0CB87 | MPFLDIQKRFGLNIDRWLTTQSAEQPYKMASRCHAFEKEWIECAHGIGYTRAEKECKIEYDDFIECLLRQKTMRRTGTIRKQRDKLIKEGKYTPPPHHIGKGEPRP | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12594
Sequence Length: 106
Domain: Contains two C-X9-C motifs that are predicted to form a helix-coil-helix structure, permitting the formation of intramolecular disulfide bonds.
Subcellular Location: Mitochondrion inner membrane
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Q9M9M6 | MASNLLKALIRSQILPSSRRNFSVATTQLGIPTDDLVGNHTAKWMQDRSKKSPMELISEVPPIKVDGRIVACEGDTNPALGHPIEFICLDLNEPAICKYCGLRYVQDHHH | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12234
Sequence Length: 110
Subcellular Location: Mitochondrion inner membrane
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P23934 | MAAVLTFLRFLGRGGAVTRGLPGGARCFGVRTSPTGEKVTHTGQVYDDGDYRKVRFVGRQKEVNENFAIDLIAEQPVSQVGSRVISCDGGGGALGHPRVYINLDKETKTGTCGYCGLQFRQQHH | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13413
Sequence Length: 124
Subcellular Location: Mitochondrion inner membrane
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Q8NHV4 | MQENLRFASSGDDIKIWDASSMTLVDKFNPHTSPHGISSICWSSNNNFLVTASSSGDKIVVSSCKCKPVPLLELAEGQKQTCVNLNSTSMYLVSGGLNNTVNIWDLKSKRVHRSLKDHKDQVTCVTYNWNDCYIASGSLSGEIILHSVTTNLSSTPFGHGSNQSVRHLKYSLFKKSLLGSVSDNGIVTLWDVNSQSPYHNFDSVHKAPASGICFSPVNELLFVTIGLDKRIILYDTSSKKLVKTLVADTPLTAVDFMPDGATLAIGSSRGKIYQYDLRMLKSPVKTISAHKTSVQCIAFQYSTVLTKSSLNKGCSNKPTTVNKRSVNVNAASGGVQNSGIVREAPATSIATVLPQPMTSAMGKGTVAVQEKAGLPRSINTDTLSKETDSGKNQDFSSFDDTGKSSLGDMFSPIRDDAVVNKGSDESIGKGDGFDFLPQLNSVFPPRKNPVTSSTSVLHSSPLNVFMGSPGKEENENRDLTAESKKIYMGKQESKDSFKQLAKLVTSGAESGNLNTSPSSNQTRNSEKFEKPENEIEAQLICEPPINGSSTPNPKIASSVTAGVASSLSEKIADSIGNNRQNAPLTSIQIRFIQNMIQETLDDFREACHRDIVNLQVEMIKQFHMQLNEMHSLLERYSVNEGLVAEIERLREENKRLRAHF | Function: Required for mitosis progression. Promotes the nucleation of microtubules from the spindle.
PTM: During mitosis, prior phosphorylation on Thr-550 by CDK1 promotes subsequent phosphorylation by PLK1 on Thr-382, Ser-397, Ser-426 and Ser-637. Phosphorylated NEDD1 can interact with gamma-tubulin for targeting the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation.
Sequence Mass (Da): 71966
Sequence Length: 660
Subcellular Location: Cytoplasm
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Q9VVI3 | MSARSSGLVAAAALPVPSSSSSVAGGDVPRPPPRRRAASVAGQQQTRQEFGNGYTPRRSLAAVNDSGDSCHLRIVVLTGQSLAKKDIFGASDPYVRIDLNTINGDINIDSVLTKTKKKTLNPTWNEEFIFRVKPSEHKLVFQVFDENRLTRDDFLGMVELTLVNLPTEQEGRTIGEQSYTLRPRRSVGAKSRIKGTLRIYHAFIRETREQSEPSSGNSDGEWEHVEATNAGETSAQPHPFPTGGHDALPAGWEERQDANGRTYYVNHTARTTQWDRPTVLNSHSSQSTDDQLASDFQRRFHISVDDTESGRSADSISHNSIEDNNNAAGLAYTPKTAATSSAPPNTPTNNNGILAQIAMQYRAEEDQDPTVDHTSFVYNSLRHPVAHRQPEISATSLQNDLRPVREAPGVPDIAITNPFTRRAAGNMAGGAGWQQERRRQQMQLHIQQHQQRQQQQQQNRILLDVDHRQQEPQHRGQRHQQQHRPSNEDTDHTDSHNPSDISAPSTRRNSEEDNAAVPPMEQNTGGEEEPLPPRWSMQVAPNGRTFFIDHASRRTTWIDPRNGRASPMPNQTRRVEDDLGPLPEGWEERVHTDGRVFYIDHNTRTTQWEDPRLSNPNIAGQAVPYSRDYKQKYEYFKSHIRKPTNVPNKFEIRIRRTSILEDSYRIISSVTKTDLLKTKLWVEFEGETGLDYGGLAREWFYLLSKEMFNPYYGLFEYSAMDNYTLQINNGSGLCNEEHLSYFKFIGRIAGMAVYHGKLLDAFFIRPFYKMMLQKPIDLKDMESVDTEYYNSLMWIKENDPRILELTFCLDEDVFGQKSQHELKPGGANIDVTNENKDEYIKLVIEWRFVARVKEQMSSFLDGFGSIIPLNLIKIFDEHELELLMCGIQNIDVKDWRENTLYKGDYHMNHIIIQWFWRAVLSFSNEMRSRLLQFVTGTSRVPMNGFKELYGSNGPQMFTIEKWGTPNNFPRAHTCFNRLDLPPYEGYLQLKDKLIKAIEGSQGFAGVD | Function: Essential E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Down-regulates Notch/N signaling pathway by promoting Notch ubiquitination, endocytosis and degradation.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 114875
Sequence Length: 1007
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.26
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Q93725 | MLIKVKTLTGKEIELDIEPNDRVERIKEKVEEKEGIPPPQQRLIFAGKQMNDDKTAADYKVLGGSVLHLVLALRGGF | Function: Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex uba-3-ula-1 and linkage to the E2 enzyme ubc-12. Attachment of ned-8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins.
PTM: Cleavage of precursor form is necessary for function.
Sequence Mass (Da): 8629
Sequence Length: 77
Subcellular Location: Nucleus
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Q54XV3 | MLIKVKTLTGKEIEIDIDPTDKIQRIKERVEEKEGIPPSQQRLIFGGKQMGDDKPASEYSIEGGSVLHLVLALRGGL | Function: Ubiquitin-like protein which plays an important role in cell cycle control. Attachment of nedd8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins (By similarity).
PTM: Cleavage of precursor form is necessary for function.
Sequence Mass (Da): 8515
Sequence Length: 77
Subcellular Location: Nucleus
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Q9VJ33 | MLIKVKTLTGKEIEIDIEPTDKVDRIKERVEEKEGIPPQQQRLIFSGKQMNDDKTAADYKVQGGSVLHLVLALRGGDSILTPCV | Function: Ubiquitin-like protein which plays an important role in cell cycle control, embryogenesis and neurogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex Uba3-Ula1 and linkage to the E2 enzyme UbcE2M. Attachment of Nedd8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins.
PTM: Cleavage of precursor form is necessary for function.
Sequence Mass (Da): 9346
Sequence Length: 84
Subcellular Location: Nucleus
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Q15843 | MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGGGGLRQ | Function: Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis via its conjugation to a limited number of cellular proteins, such as cullins or p53/TP53 . Attachment of NEDD8 to cullins is critical for the recruitment of E2 to the cullin-RING-based E3 ubiquitin-protein ligase complex, thus facilitating polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins . Attachment of NEDD8 to p53/TP53 inhibits p53/TP53 transcriptional activity . Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M .
PTM: Cleavage of precursor form by UCHL3 or SENP8 is necessary for function.
Sequence Mass (Da): 9072
Sequence Length: 81
Subcellular Location: Nucleus
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Q9W436 | MSQQHEATAAAAEKPLNNGYLQANAPLEELSATVVSPLLGQQQVQHQAPHQMQQQQQQQQQNKLPTVVFLAPDGSGGVGIQRGNPAQGNPGMVTGTGSHSDWLLKESQQRRRLLVLAIAFTVLGAAIGALAIYFASVHQRCHLYRLEPDNDDRPNGRWNQDSGSAHEGQDNICMTQECVRTAASLLSAMDLNSDPCEDFFQYACGTWNKMHPIPEDRSSISTFEVLSDQQQVILRAVLEEPIDERDNKATIKAKTFFKSCMDIPQIRKIGTGRLKQVLQSLGGWPVIERNWSPPADLSVERLMGQLRLNYSEPVMIELYVGADDKNSSVNILQMDQLQYALPSRDYYLKESSANDRRAYHRYMTQVALLLGADPATAAAELEKVVLFETQLVNVSLPEADRHDTSLVYRKMLLPELQELVPEVQWQEYLQAALGPGIPLQEDEPLVTYGLHYLTEMGKILAHTDRRVVHNYMLWRLVMSLMSHMIDEYQRERVEFRKILMGIQSERTRWSQCVEWTNKKLGVAVGALFIRDNFNQESKEVALEMIHTIRAAFNELLAENDWMDDETRAVAKEKADSMNERIGYPELLTNATELEQEYVNLTIVPDNFINNVLSILQWESEKMLRLLRQPVDKEKWTTEPAVVNAFYNPNKNDIVFPAGILQPLFYSQHFPKSLNYGGIGVVIGHEITHGFDDKGRQFDKEGNMMQWWNNATIEAFRERTQCVIDQYSRYKINEVDMFMDGRMTQGENIADNGGLKQAFRAYKKWETLHGREQQLPGLNMTHDQLFFLNYAQIWCGSMRPEDALTKIRSAVHSPGFVRVLGPLSNSRDFASAYKCPLGSTMNPAEKCSVW | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloendoprotease which functions in fertility and memory formation . Required in the dorsal paired medial neurons and alpha/beta mushroom body neurons for the proper formation of long-term and middle-term memories . Required in males to maximise egg-laying in female mates and is also required in females for their fertility .
Catalytic Activity: Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 96534
Sequence Length: 849
Subcellular Location: Cell membrane
EC: 3.4.24.11
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P08473 | MGKSESQMDITDINTPKPKKKQRWTPLEISLSVLVLLLTIIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQKAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLYNKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWRFIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSASNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGLGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW | Cofactor: Binds 1 zinc ion per subunit.
Function: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids . Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond . Catalyzes cleavage of bradykinin, substance P and neurotensin peptides . Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 . Involved in the degradation of atrial natriuretic factor (ANF) and brain natriuretic factor (BNP(1-32)) . Displays UV-inducible elastase activity toward skin preelastic and elastic fibers .
Catalytic Activity: Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.
PTM: Myristoylation is a determinant of membrane targeting.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 85514
Sequence Length: 750
Subcellular Location: Cell membrane
EC: 3.4.24.11
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Q9AFG9 | MKPICIIPARSGSKGLPDKNMLFLSGKPMIFHTIDAAIESGMFDKKDIFVSTDSELYREICLERGISVVMRKPELSTDQATSYDMLKDFLSDYEDNQEFVLLQVTSPLRKSWHIKEAMEYYSSHDVDNVVSFSEVEKHPSLFTTLSDEGYAIDMVGADKGYRRQDLQPLYYPNGAIFISNKETYLREKSFFTSRTYAYQMAKEFSLDVDTRDDFIHVIGHLFFDYAIREKENKVFYKEGYSRLFNREASKIILGDSKTISTSLESYHNYSQGGVTLATMLENLPNFLTANVTEAFVSIGVNDLITGYSVEEIFSNFQKLYSLLAENKIKMRLTTIAYTLFRETVNNADIEKINQWLTEFCYQNQIPLLDINRFLSKDGNLNYHLTSDGLHFTQEANDLLQSQYQLFVDEVKTL | Function: Catalyzes the formation of CMP-N-acetylneuraminic acid (CMP-NeuNAc), which is essential for the formation of the capsule.
Catalytic Activity: an N-acylneuraminate + CTP = a CMP-N-acyl-beta-neuraminate + diphosphate
Sequence Mass (Da): 47644
Sequence Length: 413
Subcellular Location: Cytoplasm
EC: 2.7.7.43
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Q0P8T1 | MKKTLIIAEAGVNHNGDLNLAKKLIEIAADSGADFVKFQSFKAKNCISTKAKKAPYQLKTTANDESQLQMVQKLELDLKAHKELILHAKKCNIAFLSTPFDLESVDLLNELGLKIFKIPSGEITNLPYLKKIAKLNKKIILSTGMANLGEIEEALNVLCKNGAKRQNITLLHCTTEYPAPFNEVNLKAMQSLKDAFKLDVGYSDHTRGIHISLAAVALGACVIEKHFTLDKNMSGPDHKASLEPQELKMLCTQIRQIQKAMGDGIKKASKSEQKNINIVRKSLVAKKDIKKGEIFSEGNLTTKRPANGISAMRYEEFLGKIATKNYKEDELIRE | Function: Involved in biosynthesis of legionaminic acid (5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonic acid)(Leg), a sialic acid-like derivative that is incorporated into flagellin via O-linkage to Ser/Thr. Catalyzes the condensation of 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate (PEP) to give N,N'-diacetyllegionaminic acid.
Catalytic Activity: 2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + H2O + phosphoenolpyruvate = N,N-diacetyllegionaminate + phosphate
Sequence Mass (Da): 37091
Sequence Length: 334
EC: 2.5.1.101
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Q5ZXH9 | MGSNRKINGIKPRGSSMTCFIIAEAGVNHNGDLQLAKELVYAAKESGADAVKFQTFKADTLVNKTVEKAEYQKNNAPESSTQYEMLKALELSEEDHYLLSELANSLGIEFMSTGFDEQSIDFLISLGVKRLKIPSGEITNVPYLQHCASKKLPLIISTGMCDLQEVRVAIDTVKPYYGNSLSDYLVLLHCTSNYPASYQDVNLKAMQTLADEFQLPVGYSDHTLGILVPTLAVGMGACVIEKHFTMDKSLPGPDHLASMDPEEMKNLVQSIRDAETVLGSGEKKPSDNELPIRALVRRSITLRRDLVKGAQISKEDLILLRPGTGIAPSEISNIVGSRLSMNLSAGTTLLWEHIEA | Function: Involved in biosynthesis of legionaminic acid (5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonic acid)(Leg), a sialic acid-like derivative that is incorporated into virulence-associated cell surface glycoconjugates such as lipopolysaccharide (LPS) which could be a key determinant in the ability of L.pneumophila to inhibit the fusion of phagosomes with lysosomes. LPS contains a majority alpha2,4-linked homomer of legionaminic acid. Catalyzes the condensation of 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate (PEP) to give N,N'-diacetyllegionaminic acid.
Catalytic Activity: 2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + H2O + phosphoenolpyruvate = N,N-diacetyllegionaminate + phosphate
Sequence Mass (Da): 38991
Sequence Length: 356
EC: 2.5.1.101
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Q0P8T0 | MSKRKICIVSATRAEWYLLRNLCHEIQNDKDLSLQIIATGAHLSPEFGLTYKEIEKEFKITKKIPILLANDDKISLCKSMSLAFSAFSDAFEDLKPDMVVILGDRYEMLSVASVCLLMHIPLVHLCGGELTLGAIDDSIRHSISKMSHLHFVSHEIYKKRLLQLGEEEKRVFNIGSLASTIIKNMNFLNKKDLEKALEMKLDKELYLITYHPLTLNVKNTQKEIKTLLKKLDTLKNASLIFTKANADENGLLINEILQNYCQKNSHKAKLFDNLGSQKYLSLMKIAKAMIGNSSSGISESPFFKTPCINIGDRQKGRLRTQNIIDSEINDLDQAFEKLESKEFKQNLKNFKNPYDNGKNPNKIIKTCLKNVNLDTILHKNFIDL | Function: Involved in biosynthesis of legionaminic acid (5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonic acid)(Leg), a sialic acid-like derivative that is incorporated into flagellin via O-linkage to Ser/Thr. Catalyzes the conversion of GDP-N,N'-diacetylbacillosamine (Bac2Ac4Ac) into 2,4-diacetamido-2,4,6-trideoxymannose and GDP. It can also use UDP-N,N'-diacetylbacillosamine however it generates small quantities of 2,4-diacetamido-2,4,6-trideoxymannose.
Catalytic Activity: GDP-N,N'-diacetylbacillosamine + H2O = 2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + GDP + H(+)
Sequence Mass (Da): 43766
Sequence Length: 384
EC: 3.2.1.184
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Q5ZXH8 | MIRKIIYVTGTRADYGLMREVLKRLHQSEDIDLSICVTGMHLDALYGNTVNEIKADQFSICGIIPVDLANAQHSSMAKAIGHELLGFTEVFESETPDVVLLLGDRGEMLAAAIAAIHLNIPVVHLHGGERSGTVDEMVRHAISKLSHYHFVATEASKQRLIRMGEKEETIFQVGAPGLDEIMQYKTSTRDVFNQRYGFDPDKKICLLIYHPVVQEVDSIKIQFQSVIQAALATNLQIICLEPNSDTGGHLIREVIQEYIDHPDVRIIKHLHRPEFIDCLANSDVMLGNSSSGIIEAASFNLNVVNVGSRQNLRERSDNVIDVDVTYDAILTGLREALNKPKIKYSNCYGDGKTSERCYQLLKTIPLHSQILNKCNAY | Function: Involved in biosynthesis of legionaminic acid (5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonic acid)(Leg), a sialic acid-like derivative that is incorporated into virulence-associated cell surface glycoconjugates such as lipopolysaccharide (LPS) which could be a key determinant in the ability of L.pneumophila to inhibit the fusion of phagosomes with lysosomes. LPS contains a majority alpha2,4-linked homomer of legionaminic acid. Catalyzes the conversion of UDP-N,N'-diacetylbacillosamine (Bac2Ac4Ac) into 2,4-diacetamido-2,4,6-trideoxymannose and UDP.
Catalytic Activity: H2O + UDP-N,N'-diacetylbacillosamine = 2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + H(+) + UDP
Sequence Mass (Da): 42110
Sequence Length: 377
EC: 3.2.1.184
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Q9XXA7 | MDKNRRRTDDAGLMTKTLAGIAALVFFLSFICSSYDITVTHVISTIDVILEESEYYRSAKEWTASSIDATWNEVSIPSRKAEHIQAINPEVDVAAGGKHVFTPEQLHFFDGTRDSKPIYLAILGRVYNVDGKKEYYGPGKSYHHFAGRDATRAFTTGDFQESGLIATTHGLSHDELLSIRDWVSFYDKEYPLVGVVADLYYDSEGQPTPELTDVLARVEKANEYRKAQAVEIEVFPPCNSEYNQNGGRVWCSTKSGGVERQWAGVPRKLIEPTTEKFRCACVKNFGPGVSGAEEVKSSSNRGDLDHPDLELFPDCSPTSNSCKIVS | Function: Heme-binding protein.
Sequence Mass (Da): 36242
Sequence Length: 326
Domain: The cytochrome b5 heme-binding domain was proven to bind heme, although it lacks the conserved iron-binding His residues at position 136 and 169.
Subcellular Location: Secreted
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A2CES0 | MLKYLVALISMVLAVWTVPEWLTFPIYGNVVTVLESWLRQRVSEVSASSPGLLLTKEQLSLYNGGKNSKGLYLAILGQVFDVEKGRKHYGPGGGYHFFTGKDASRAFITGDFTEAGLSNDVSDFSESQIVALYDWLSFYQRDYTPVGKLIGRFYTETGQPTDALLHVEAFLSDGLKKKAQAQSEMQLYPSCNSEWSEASGGRVWCSTMSGGIHRDWVGVPRMLFTPGSGHSRCVCIRLSDPVHSENRNLREYTDCPPRAESCQIAKD | Function: Heme-binding protein which promotes neuronal but not astrocyte differentiation.
Sequence Mass (Da): 29715
Sequence Length: 267
Domain: The cytochrome b5 heme-binding domain was proven to bind heme, although it lacks the conserved iron-binding His residues at position 90 and 114.
Subcellular Location: Secreted
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Q9W376 | MFGLLRHLFKFQFLFVVAAVLGGIYHTEIRQFLRRQTDNYLDQAGQDASIPLAFQAGDDIGTLFTPAELAKFNGEEEGRPLYLALLGSVFDVSRGIKHYGSGCSYNFFVGRDASVSFISGDFETYDPETADDVLTLKPDDLIGLAGWRDFYQKDYVYKGRVIGRFYDEKGALTTYHHKFLELLEQARDAKRQVEELRARYPGCNIEWSEERGTRVWCTTTSGDGKERSWIGYPRKLYSRGNKSFQCACVPDAELDEIDAGGKVAHGDAMLKPYDNCEPQARECFYRV | Function: Heme-binding protein.
Sequence Mass (Da): 32628
Sequence Length: 287
Domain: The cytochrome b5 heme-binding domain was proven to bind heme, although it lacks the conserved iron-binding His residues at position 99 and 126.
Subcellular Location: Secreted
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Q5SSH8 | MLRICGLGVVLSLAVAAVAVMAVWLMDWWGPRPGIRLFLPEELARYRGGPGDPGLYLALLGRVYDVSSGRRHYEPGAHYSGFAGRDASRAFVTGDYSEAGLVDDINGLSSSEILTLHNWLSFYEKNYVFVGRLVGRFYRKDGLPTSELTQVEAMVTKGMEANEQEQREKQKFPPCNSEWSSAKGSRLWCSQKSGGVHRDWIGVPRKLYKPGAKEPHCVCVRTTGPPSDQQDNPRHSNHGDLDNPNLEEYTGCPPLATTCSFPL | Function: Heme-binding protein which promotes neuronal but not astrocyte differentiation.
Sequence Mass (Da): 29162
Sequence Length: 263
Domain: The cytochrome b5 heme-binding domain was proven to bind heme, although it lacks the conserved iron-binding His residues at position 73 and 106.
Subcellular Location: Secreted
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Q28FI8 | MLGYLAAAALCLAAVLLMRLDHLPLVDIPGLGYIFPQQCELSEGRLMSKEELSVYDGGPGSSGIYLAILGQVFDVHKGSKHYGPGGSYSFFAGKDASRAYMTGDFTEKGLVDDVTELSPLQMLHLHNWLSFYQQNYITIGKLTGRFYDESGNPTKALEDALKVIDIGLKLKEEREEENKQFPPCNSEWSSESKRVWCSKNSGGIQRDWVGVPRKMYTAGTNGYRCVCVRNFGPPSEQPDSTEHNDRGDLDNPMLHEYEDCNPLFEWCFLKNGT | Function: Heme-binding protein which promotes neuronal but not astrocyte differentiation.
Sequence Mass (Da): 30527
Sequence Length: 273
Domain: The cytochrome b5 heme-binding domain was proven to bind heme, although it lacks the conserved iron-binding His residues at position 82 and 124.
Subcellular Location: Secreted
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P35722 | MDCCTESACSKPDDDILDIPLDDPGANAAAAKIQASFRGHMARKKIKSGERGRKGPGPGGPGGAGGARGGAGGGPSGD | Function: Acts as a 'third messenger' substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. Binds to calmodulin in the absence of calcium.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 7549
Sequence Length: 78
Domain: Neurogranin is intrinsically unstructured; however, upon binding with CaM, The IQ domain adopts a helical conformation.
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Q92686 | MDCCTENACSKPDDDILDIPLDDPGANAAAAKIQASFRGHMARKKIKSGERGRKGPGPGGPGGAGVARGGAGGGPSGD | Function: Acts as a 'third messenger' substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. Binds to calmodulin in the absence of calcium (By similarity).
PTM: Phosphorylated at Ser-36 by PHK and PKC, phosphorylation prevents interaction with Calmodulin and interrupts several learning- and memory-associated functions.
Sequence Mass (Da): 7618
Sequence Length: 78
Domain: Neurogranin is intrinsically unstructured; however, upon binding with CaM, The IQ domain adopts a helical conformation.
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P60761 | MDCCTESACSKPDDDILDIPLDDPGANAAAAKIQASFRGHMARKKIKSGECGRKGPGPGGPGGAGGARGGAGGGPSGD | Function: Regulates the affinity of calmodulin for calcium. Involved in synaptic plasticity and spatial learning.
PTM: Disulfide bond formation is redox-sensitive. The cysteine residues are readily oxidized by several nitric acid (NO) donors and other oxidants to form intramolecular disulfide. Cys-51 can form a disulfide with any other of the cysteine residues with an order of reactivity Cys-9 > Cys-4 > Cys-3 (By similarity).
Sequence Mass (Da): 7496
Sequence Length: 78
Domain: Neurogranin is intrinsically unstructured; however, upon binding with CaM, The IQ domain adopts a helical conformation.
Subcellular Location: Cytoplasm
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