ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q4UQV0 | MSTSLPLRDDGAVRASFALALFVLLGLGLGYSLVATGITSALMPDQAHGSLLRADGRVIGSSLVAQPFADARYFQPRPSAAKYDPTAAAGSNQARSNPELLARIATARAEIAQRDGIAPDAVPGELLTQSGSGLDPHLSPAGAQVQLRRVAAARGWPEQRVAALLQAATEQPQFGLLGQPRINVLALNLALDRAGDGVPGTENGVEQQR | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
P94608 | MDINYERPDPYYLLNKIDKEEKNKNRGKLKIFFGYAAGVGKTYAMLRAAHYMKELGKDIVIGYIEPHARMDTMSLTKGLPQIPVKNIDYKGVILREFDVDKALLRKPEIILVDELAHTNAKSQRNKKRWKDIEELLDAGIDVYTTLNVQHIESLNDIVANITHVSVRETIPDKVFDDADKVELIDIEPDELLKRFTDGKIYRKEQVKRAFNNFFTKNNLYALREIALRRTADRVNFEIEIARLSKGQITVMATSDQILACIGTSPSSARIIRTAARMAESYHSKWIALYVDTGRSLGKADKETLNANFNLVELLGGELVT... | Function: Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon. KdpD may function as a membrane-associated protein kinase that phosphorylates KdpE in response to environmental signals (By similarity).
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho... |
P21865 | MNNEPLRPDPDRLLEQTAAPHRGKLKVFFGACAGVGKTWAMLAEAQRLRAQGLDIVVGVVETHGRKDTAAMLEGLAVLPLKRQAYRGRHISEFDLDAALARRPALILMDELAHSNAPGSRHPKRWQDIEELLEAGIDVFTTVNVQHLESLNDVVSGVTGIQVRETVPDPFFDAADDVVLVDLPPDDLRQRLKEGKVYIAGQAERAIEHFFRKGNLIALRELALRRTADRVDEQMRAWRGHPGEEKVWHTRDAILLCIGHNTGSEKLVRAAARLASRLGSVWHAVYVETPALHRLPEKKRRAILSALRLAQELGAETATLS... | Function: Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon. KdpD may function as a membrane-associated protein kinase that phosphorylates KdpE in response to environmental signals.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Lo... |
P61656 | MKDNTCTKRDFLNGTKIGGDEPFFLISGPCVMENRDLLDRVCAEMIEVCGELKIPYIFKSSFDKANRSSVNSYRGPGLAEGIKNLEYIKNKYNVPVLTDIHETSQISPLKDVIDVYQIPAFLCRQTDLISQSAQTGKWVNVKKGQFLAPADTRHIAVKMNESGNNKLLVTERGTSFGYGNLIFDGRAIPIIHGFDIPLVFDATHSAQLPGAAGNSTGGQREFIPSILRSAVSFGIEGIFMEVHPDPPNALSDATTQYPLSQIKSLLKEMIGLDRYIKKEILISRSSL | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
Sequence Mass (Da): 31703
Sequence Length: 287
Pathway: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: s... |
Q604M5 | MSNVETSARPFELCGFPVGLEHPLFLIAGPCVIETEQLALDTAGALKEITDGLGIPFIYKSSFDKANRSSHASYRGPGMEEGLRILAEVKRQIGVPVLTDVHEDTPLQEVASVVDVLQTPAFLCRQTNFIQNVANTGKPVNLKKGQFLAPWDMKHVAAKALATGNRHIMVCERGVSFGYNNLVSDMRSLSIMRETGCPVVYDATHSVQLPGGQGTASGGQREFVPALARAAVAVGISGLFMETHPDPDRALSDGPNSWPLDRMKALLELLSTLDRTVKASPLL | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
Sequence Mass (Da): 30506
Sequence Length: 283
Pathway: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: s... |
Q9JZ55 | MDIKINDITLGNNSPFVLFGGINVLESLDSTLQTCAHYVEVTRKLGIPYIFKASFDKANRSSIHSYRGVGLEEGLKIFEKVKAEFGIPVITDVHEPHQCQPVAEVCDVIQLPAFLARQTDLVVAMAKTGNVVNIKKPQFLSPSQMKNIVEKFHEAGNGKLILCERGSSFGYDNLVVDMLGFGVMKQTCGNLPVIFDVTHSLQTRDAGSAASGGRRAQALDLALAGMATRLAGLFLESHPDPKLAKCDGPSALPLHLLEDFLIRIKALDDLIKSQPILTIE | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
Sequence Mass (Da): 30483
Sequence Length: 280
Pathway: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: s... |
Q3SRK0 | MNQPVSASPVVSVGSVTFGQDRPLSIIAGPCQMESRAHALEVAGALKDIAARLNVGLVFKTSFDKANRTSASGARGIGLKQALPVFADIRSSLGLPVLTDVHEAAQCAEVAQVVDVLQIPAFLCRQTDLLLAAAATGKVVNVKKGQFLAPWDMGNVVAKITGGGNRNILVTERGASFGYNTLVSDMRALPILARTTGAPVIFDATHSVQQPGGKGASTGGEREFVPVLARAAVAVGVAGVFIETHPDPDHAPSDGPNMVPLREFEALVRRLMAFDALAKAADPACPE | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
Sequence Mass (Da): 29822
Sequence Length: 287
Pathway: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: s... |
O66914 | MRRAVIIPARLGSTRLKEKPLKNLLGKPLIRWVVEGLVKTGERVILATDSERVKEVVEDLCEVFLTPSDLPSGSDRVLYVVRDLDVDLIINYQGDEPFVYEEDIKLIFRELEKGERVVTLARKDKEAYERPEDVKVVLDREGYALYFSRSPIPYFRKNDTFYPLKHVGIYGFRKETLMEFGAMPPSKLEQIEGLEQLRLLENGIKIKVLITENYYHGVDTEEDLKIVEEKLKNL | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27173
Sequence Length: 234
Pathway: Nucleotide-suga... |
Q9C920 | MSVCSSSSSSQKTWIVNGILAGTAIAAAIGARAYLGRSKKFRSRVVGIIPARYASSRFEGKPLVQILGKPMIQRTWERSKLATTLDHIVVATDDERIAECCRGFGADVIMTSESCRNGTERCNEALEKLEKKYDVVVNIQGDEPLIEPEIIDGVVKALQVTPDAVFSTAVTSLKPEDGLDPNRVKCVVDNRGYAIYFSRGLIPYNKSGKVNPDFPYMLHLGIQSFDSKFLKVYSELQPTPLQQEEDLEQLKVLENGYKMKVIKVDHEAHGVDTPDDVEKIESLMRERNMS | Function: Catalyzes the production of the sugar nucleotide CMP-3-deoxy-D-manno-octulosonate (CMP-KDO). CTP is the preferred nucleotide donor, but it can partially be replaced with UTP. Activates KDO during the biosynthesis of rhamnogalacturonan II (RG-II), a structurally complex pectic polysaccharide of the primary cel... |
A8IGU8 | MAFSASDVLVLIPARLAASRLPGKPLADVGGRPMIVEVARRAVAAGIGRVAVATDAVEIADAVRAAGFEAVMTRADHPSGSDRIFEALGVLDPDGAVQVVVNVQGDLPTIAPETIRAALVPLEEGPADIATLTAVITEEGERTDPNVVKVVGTPIGENRLRALYFTRATAPTGEGPLYHHIGLYAYRRAALERFVSLPPSPLEKRERLEQLRALEAGMRIDVAVVDAVPLGVDTPEHLERARALLASNDN | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 26436
Sequence Length: 250
Pathway: Nucleotide-suga... |
Q8A9S0 | MKFLGIIPARYASTRFPAKPLAMLGGKTVIQRVYEQVAGILDDAYVATDDERIEAAVKAFGGKVVMTSIDHKSGTDRCYEACTKIGGDFDVVVNIQGDEPFIQPSQLNAVKACFEDPTTQIATLVKPFTADEPFAVLENVNSPKVVLNKNWNALYFSRSIIPFQRNADKEDWLKGHTYYKHIGLYAYRTEVLKEITALPQSSLELAESLEQLRWLENGYKIKVGISDVETIGIDTPQDLKHAEEFLKNRS | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27994
Sequence Length: 250
Pathway: Nucleotide-suga... |
Q6G4U6 | MALEPIILIPARIGSTRLPQKALAEIAGKPMIVHVAEQAKKAAFGRIIVATDHNNIAKVVTAYGHECIITCRDHKSGSDRIYEALTHIDPERRYNVILNVQGDLPTITPHEIISALRPLENSLTDIATLGAKIVEENEKTDPNIVKIIGTPLSHNRFRALYFTRATAPYGDGPLYHHIGIYAYRREALEKFVALKPSPLEQREKLEQLRALEHNMRIDVEIVDTIPLGVDTQRDLERVRKILA | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27280
Sequence Length: 243
Pathway: Nucleotide-suga... |
Q6MPP1 | MKIVGVIPARFGSTRFPGKPLVNLKGRPLIQWTVEGAKKSKLLSEVIVATDHEGIKAAAEAVGVKVVMTDSDLPTGSDRINAAIKDVACDVVVNIQGDEPLVTGELIDRLAQVFVDDPKMDMATLAHPISAEELQSMNSVKVVVNCRDEALYFSRYPMPYSRMSAQEAGSMDGCLKHIGMYAYSRNFLKQFCEAPPALIEKAESLEQLRALYLGAKIKVIRVKEASVGVDTPEDLARLEKLLSSQGM | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 26921
Sequence Length: 247
Pathway: Nucleotide-suga... |
Q492T2 | MNFVVIIPVRFFSTRFPGKALADINGKPMIVRVMENALDSGANKVIIATDSSCIARVIESEQSESEVCLTRSTHQSGTERLAEVAINYKFSDDQIIVHLQGDEPLLSSTMIRQVASILCSMSSTISMATLATPLSSFKEARDDNVVKVVINMNSNALYFSRSMIPWNTGDFVNHLDSKFSKTLLRHIGIYAYRVKFLRRYIAWTKSPLEQIEHLEQLRVLWHGEAIHVSVIDDVFNISVDTPESLSRVNTVFKKNKYATVHN | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 29527
Sequence Length: 262
Pathway: Nucleotide-suga... |
Q129C7 | MRFTVLIPARLASTRLPNKPLADMGGAPMVVRVAQRAMQSTAARTVVATDSTDIIDKCAAFGVAAVLTRADHPSGSDRLAEACTALGLADDDIVVNVQGDEPLIDPALIDAVARLLNERPDCAMSTAAHSIDQMADLLNPNVVKVVLDARQTALYFSRSPIPAARDFAGKPWWEDGEKGCKLPKPLRHVGIYGYRVGFLRQFPTLPQAPLEQLESLEQLRALWHGHRIAVHITDEAPGPGVDTPEDLARARQFFP | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27656
Sequence Length: 255
Pathway: Nucleotide-suga... |
B2RLM4 | MNTEVIAIIPARFASSRFPGKPLADMLGKSMIQRVHERIAGVVPRAVVATDDERIRQAVEDFGGEVVMTSPECSSGTERCREAFDKVGRGEKIVLNLQGDEPFIQKEQIDLLISAFDKPETDIATLAEVFSSDASFERLNNPNSPKIVLDHGGYALYFSRSVIPYLRGVQPDSWCRRHTYYKHIGIYAFRPTVLRKITSLPQSTAEQAESLEQLRWLEYGYRIRVLQTQQSTIGIDTPEDMDKAIAYLRSQGME | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 28660
Sequence Length: 254
Pathway: Nucleotide-suga... |
Q9HZM5 | MTQAFTVVIPARYASTRLPGKPLQDIAGQPMIQRVWNQARKSAASRVVVATDDERILAACQGFGAEALLTRAEHNSGTDRLEEVASRLGLASDAIVVNVQGDEPLIPPALIDQVAANLAAHPEAAIATLAEPIHEVSALFNPNVVKVATDIDGLALTFSRAPLPWARDAFARDRDSLPEGVPYRRHIGIYAYRVGFLADFVAWGPCWLENAESLEQLRALWHGVRIHVADARENMLPGVDTPEDLERVRRVLGG | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27646
Sequence Length: 254
Pathway: Nucleotide-suga... |
Q4KFT3 | MSSAFTVVIPARYASTRLPGKPLQLIAGKPMIQWVWEQARKSSAERVVVATDDQRIVEACQGFGAEALLTREDHNSGTDRLAEVAAQLGLAADAIVVNVQGDEPLIPPSVIDQVAANLAAHTEARMATLAEPIEDVQTLFNPNVVKVVSDLNGLALTFSRATLPWARDAFAQSREQLPEGVPYRRHIGIYAYRAGFLHDFVSWGPCWLENTESLEQLRALWHGVRIHVADALEAPPTGVDTAEDLERVRRLLEA | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27862
Sequence Length: 254
Pathway: Nucleotide-suga... |
Q46222 | MMLRGVHRIFKCFYDVVLVCAFVIALPKLLYKMLVYGKYKKSLAVRFGLKKPHVPGEGPLVWFHGASVGEVRLLLPVLEKFCEEFPGWRCLVTSCTELGVQVASQVFIPMGATVSILPLDFSIIIKSVVAKLRPSLVVFSEGDCWLNFIEEAKRIGATTLVINGRISIDSSKRFKFLKRLGKNYFSPVDGFLLQDEVQKQRFLSLGIPEHKLQVTGNIKTYVAAQTALHLERETWRDRLRLPTDSKLVILGSMHRSDAGKWLPVVQKLIKEGVSVLWVPRHVEKTKDVEESLHRLHIPYGLWSRGANFSYVPVVVVDEIG... | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of three 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Thus generates the genus-specific LPS epitope of Chlamydia, composed of the trisaccharid... |
P0CE14 | MIRRWLTSRLYDAFLVCAFFVSAPRIFYKVFFHGKYIDSWKIRFGVQKPFVKGEGPLVWFHGASVGEVSLLAPLLNRWREEFPEWRFVVTTCSEAGVHTARRLYESLGATVFVLPLDLSCIIKSVVRKLAPDIVIFSEGDCWLHFLTESKRLGAKAFLINGKLSEHSCKRFSFLKRLGRNYFAPLDLLILQDELYKQRFMQIGISSDKIHVTGNMKTFIESSLATNRRDFWRAKLQISSQDRLIVLGSMHPKDVEVWAEVVSHFHNSSTKILWVPRHLEKLKEHAKLLEKAGILFGLWSQGASFRQYNSLIMDAMGVLKD... | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of three 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Thus generates the genus-specific LPS epitope of Chlamydia, composed of the trisaccharid... |
P0AC77 | MLELLYTALLYLIQPLIWIRLWVRGRKAPAYRKRWGERYGFYRHPLKPGGIMLHSVSVGETLAAIPLVRALRHRYPDLPITVTTMTPTGSERVQSAFGKDVQHVYLPYDLPDALNRFLNKVDPKLVLIMETELWPNLIAALHKRKIPLVIANARLSARSAAGYAKLGKFVRRLLRRITLIAAQNEEDGARFVALGAKNNQVTVTGSLKFDISVTPQLAAKAVTLRRQWAPHRPVWIATSTHEGEESVVIAAHQALLQQFPNLLLILVPRHPERFPDAINLVRQAGLSYITRSSGEVPSTSTQVVVGDTMGELMLLYGIAD... | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of two 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kd... |
P44806 | MWRFFYTSLLLICQPLILCFIGLLSVKSPRYRQRLAERYGFYGNASCPPPQGIFIHAASVGEVIAATPLVRQLQQDYPHLSITFTTFTPTGSERVKATFGDSVFHYYLPLDLPFSIHRFINFVQPKLCIVMETELWPNLIHQLFLRNIPFVIANARLSARSAHRYGKIKAHLQTMWSQISLIAAQDNISGKRYATLGYPKEKLNITGNIKYDLNTNDELLRKIDSLRTLWKQDRPIWIAASTHNGEDEIILKSHRALLAKYPNLLLLLVPRHPERFNVVADLLKKEKFQFIRRSTNELPNENTQVILGDSMGELMLMYGI... | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of a single 3-deoxy-D-manno-octulosonate (Kdo) residue from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Is strictly monofunctional, i.e. is capable of adding only a single Kdo residue to the... |
Q9ZE58 | MMLLYYTLSFILLPVYFIIIFIRLLIGKEDIRRIQERFAIGKQRQNSALDFIQMSVNKEGFTDHKTTSYVDMHRNASLMYKLSLERSYAHSLVWIHAASVGEVMTALTLIHNISKLAPNVRFLITSWTNASAKILSTKLPKIATHQFLPIDNVIFTRKFLRNWQPDLGIFIESELWPCTINEGAKYCKLLLINARISNKSFKAWLKRKRFFQLIIKNFSKIIVQSERDLQKFNALGISDAMNLGNIKFANEKLLVNQEKLSKLILHLDNRRVLVFASTHPEDEEVILPIINNLKEQFIDCYIILIPRHPERIKSIINNCK... | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-... |
P50842 | MGYLHDAFSLKGKTALVTGPGTGIGQGIAKALAGAGADIIGTSHTSSLSETQQLVEQEGRIFTSFTLDMSKPEAIKDSAAELFENRQIDILVNNAGIIHREKAEDFPEENWQHVLNVNLNSLFILTQLAGRHMLKRGHGKIINIASLLSFQGGILVPAYTASKHAVAGLTKSFANEWAASGIQVNAIAPGYISTANTKPIRDDEKRNEDILKRIPAGRWGQADDIGGTAVFLASRASDYVNGHILAVDGGWLSR | Function: Catalyzes the reduction of 2,5-diketo-3-deoxygluconate (DKII or 4,6-dihydroxy-2,5-dioxohexanoate) into 2-keto-3-deoxygluconate (KDG or 2-dehydro-3-deoxygluconate) with a concomitant oxidation of NADH.
Catalytic Activity: 2-dehydro-3-deoxy-D-gluconate + NAD(+) = 3-deoxy-D-glycero-2,5-hexodiulosonate + H(+) + N... |
P37769 | MILSAFSLEGKVAVVTGCDTGLGQGMALGLAQAGCDIVGINIVEPTETIEQVTALGRRFLSLTADLRKIDGIPALLDRAVAEFGHIDILVNNAGLIRREDALEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNGGKIINIASMLSFQGGIRVPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSAEILDRIPAGRWGLPSDLMGPIVFLASSASDYVNGYTIAVDGGWLAR | Function: Catalyzes the reversible reduction of 2,5-diketo-3-deoxygluconate (DKII or 4,6-dihydroxy-2,5-dioxohexanoate) into 2-keto-3-deoxygluconate (KDG or 2-dehydro-3-deoxygluconate) with a concomitant oxidation of NADH (Ref.4). To a lesser extent, can also reduce 5-keto-D-gluconate and oxidize D-gluconate and 1,2-pro... |
Q8A2S4 | MKTNYEIRYAAHPEDAKSYDTARIRRDFLIEKIFVPNEVNMVYSMYDRMVVGGALPVGEVLTLEAIDPLKAPFFLTRREMGIYNVGGPGVVKAGDAVFELDYKEALYLGSGDRVVTFESKDASNPAKFYFNSLTAHRNYPDRKVTKADAVVAEMGSLEGSNHRNINKMLVNQVLPTCQLQMGMTELAPGSVWNTMPAHVHSRRMEAYFYFEIPEEHAICHFMGEVDETRHVWMKGDQAVLSPEWSIHSAAATHNYTFIWGMGGENLDYGDQDFSLITDLK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the isomerization of 5-dehydro-4-deoxy-D-glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate.
Catalytic Activity: 5-dehydro-4-deoxy-D-glucuronate = 3-deoxy-D-glycero-2,5-hexodiulosonate
Sequence Mass (Da): 31666
Sequence Length: 280
Pathway: Glycan metabolism... |
Q9X756 | MDSHTLIQALIYLGAAALIVPIASVLGLGSVLGYLIAGCIIGPWALRLVNDAEAILHFAEIGVVLMLVAMGLELDPQRLWKLRASVFDGGALQMVACGVLIGLFCMLLGLRWQVAELIGMTLALSSTAIAMQAMNERNLTVSQMGRSAFAVLLFQDIAAIPLVAMIPLLAASGGATSLMAFALSALKVAAALALVVVLGRYLTRPLLRFVARSGLREVFSAVACSWSSALGLLLEEVGLSMAMGAFLAGVLLASSEYRHALENDIEPVKGLLLGLFFIGVGMSIDFAPWSPNPLRIVILLVGFPAIKMLMLWLIAQPLGV... | Function: Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67353
Sequence Length: 621
Subcellular Location: Cell inner membrane
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Q8ZRW2 | MDSHTLLQALIYLGSAALIVPIAVRLGLGSVLGYLIAGCIIGPWGLRLVTDAESILHFAEIGVVLMLFVIGLELDPQRLWKLRASVFGGGALQMGVCGGLIGLFCMFLGLRWQVAELIGMTLALSSTAIAMQAMNERNLTVSQVGRSAFAVLLFQDIAAIPLVAMIPLLAASGASTTLGAFALSALKVAGALALVVLLGRYVTRPALRFVARSGLREVFSAVALFLVFGFGLLLEEVGLSMAMGAFLAGVLLASSEYRHALESDIEPFKGLLLGLFFIGVGMSIDFGTLVENPLRILLLLAGFLAIKIVMLWLVARPLGV... | Function: Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67054
Sequence Length: 620
Subcellular Location: Cell inner membrane
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E7R7R2 | MSRYFLLACTLALQCVAASQEDYIVKDLPGLSNIPAVVRPVMHAGHLEIDEEHNTELFFWRFQNPKNNGTHQTLHRNELIVWLNGGPGCSSMDGAMMETGPLRVSDKLEVELNPGSWTQVADILFVDQPAGTGFSYTDSYDTELKQAAQHFWQFLKTYYQLFPEDRTKKLYLAGESYAGQYIPYFAKEIIENNSLNISLEGLLIGNGWIDPDIQSLSYVPFSLEAGFLDRQSPSMAQVLKQHEKCQQAIDDPSNHDFEKVECVKIFHSILAASRDETKPAKEQCVNMYDYRKHDYFPACGSNWPEGLPTVTKFLNLDAVQ... | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine res... |
B6H7A4 | MLLSALSLLLSPLVSASSAADYYVRSLPGAPEGPFLKMHAGHIEVDPDTNGNLFFWHFQNRHIANRQRTVIWLNGGPGCSSMDGAFMEVGPYRLQDDHTLKYNEGRWDEFANLLFVDNPVGTGFSYANTNSYLHELDEMAAHFVIFLEKFFELFPEYANDDLYIAGESYAGQHIPYIAKAIQDRNKGITENGGTKWPLKGLLIGNGWISPADQYPSYFKFIEREGLAKPGTSLHHNINALNEVCLSKLETPGAKNKLDVGACELVLQQFLDLTTEDHQCYNMYDVRLKDEAKSCGMNWPPDLKNIEPYLQRPDVVKALNI... | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine res... |
Q0USX0 | MLLTHTSSRWRTAAVCALAATASWLPSVQAAEKTQADYFVSSLPGAPEGPLLKMHAGHIEVDAEHNSNLFFWHYENRHIADRQRTVLWLNGGPGCSSMDGAMMEIGPYRVKHGGHLEYNNGSWDEFANMLFIDQPVGTGFSYVNTDSYLTDLDQMAEHMMIFLEKWFKLFPEYENDDLYIAGESYAGQHIPYIARAILNRNKNQNTDPKPWNLKGLLIGNGWISPADQYLAYLPFAYQNGMIQADSDSAKRVEQQQSICIQKLQDGGHDKVDTSECEQIMVAILEETKDRKADRMNQCLNMYDIRLRDDSSCGMNWPPDL... | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine res... |
D0MVS1 | MVTRHVLAAALAGSMTSAQRLHPTSQRASDDLIQNLPGLDPAAKVTQHAGRIALHDNDKNKMFYWHFQAAQDPEKAPLVIWLNGGPGCTSMQGLFLGNSPFTLKDDSTIGKNEHSWHEFANLLFVDQPIGTGMSYTKGNDYRLDEETIAQDFYEFLTKFLQRHNKYLSDGDDGVSNSRAVYMFGESHAGRWIPEFSDHIMKQNNDPKNQIKINLDGVGIGNGWVHPRIQYEYSDYAHGLGLLTFGQVRSLKASYAECLAALDAGTYYSRSCLDNMDSITGSVKPGNGGNSLNFYDVRQYLRNVGSYPSGQSNIAKYMNKM... | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine res... |
E3L8A5 | MSSFQSATTRQGLHRRNMNSETPQSEFIQRLRRSPPSESSSSTPSSSTTTSSTTTTSNTSGKKKKTAPSASDFYVPSLPGQPKDSQLILYAGHLSFSPPDTTIEPEKDSYGFFFLNKARHIANRPVLLVWLNGGPGCSSFDGSLMEVGPLRMVLKGDGTLKEVDAAWNEYANMLFIDQPTGTGYSYGPKPNYVHELDVSSANLVNLLARFFKIFPEYQQMDLYICGESFAGQYIPYLAQAILDTNIISAPLKGIMIGNGWIDPINQYLAYPEFAFKVGLVNPSSKAADLVNEELKKCTEWIDSNSTTPIHIEACEGILSA... | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine res... |
B6K7U7 | MSLSFLLRVAGLFFLQFNSAQAKSQVHEQWHVSSIPNVPAGYTGSLHSGYLNLTDKLEGDLFFTLYGSENEVHQNRTIIWLNGGPGCSSEDGSMLELGPLRLTNDSLVYYNAASWVRLGNVLFVDQPMGTGFSFADTRDAILNDNEKMSNDFAYFLQEFVKAFPEYATDTWYIAGESFAGQYIPAIAKKVIDSDIVNLSGIAIGNGWIEPASHYLTYLDYLVERGLLERGSALFEALTAVQAKCLMSLEQSASGMLEDENSCDKYLFDILFSVSDKSGEFCFNMYDVTLTSPYPSCGMEWPLELPALTDFLSSPDVMKAL... | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine res... |
O60123 | MISKLLKIVLLTAGVIGNTLADSRIHEQYLVKAFPNEPVDYEGRMHAGHLNQTDQLDGDLFFWMFESVKPEYEHRSILWLNGGPGCSSEDGSLMEVGPFRLDDNNTFQLNPGRWDELGNLLFVDQPLGTGYSYSLAKDFQSNNEKMANDFSIFFEKFLEEFPERANDEWFIAGESFAGQYIPHIAAKLKEKNLVNLGGLAIGNGWINPLSHYETYLNYLVEKGMVDFESELGQYLHHSWAECLLAFDKIGSGSGDLSKCESFLGDILYMVSKEPGKACMNMYDISLESTYPTCGMDWPYDLSYLTEFLSTREAMTSLNVN... | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine res... |
A7EYY7 | MRSLTTKTSSALLTVWGLLSVSLMPSVGQADKTAGDYFVHSLPGAPAGPLLKMHAGHIEVTPEHHGNIFFWHFQNRHIANKQRTVIWLNGGPGCSSEDGALMEIGPYRVKDGSNGPKLEYNPGSWDEFANVMFVDNPVGTGFSFVDSDSYIHDLPEMADQFVQFLEKWFALFPEYEHDDLYLAGESYAGQHIPYITKAILERNKKPDAKHKWPVKGMLIGNGWISPVEQYMSYLPFAYEKGLVKKDSEKAKKLESQQAICTKMLNENGGRDKVDNSQCEQILQEILSTTQSKGSDGNMQCYNMYDVRLKDSYPSCGMNWP... | Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic Activity: Preferential release of a C-terminal arginine or lysine res... |
Q9PNB8 | MKLQGFVLLISGPSGAGKSTLLKKLFDEFEDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYGTSLKHTQNALDNGKIVVFDIDVQGFKIARKKMADKIVSVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKELSEYDYLIINDELKQSYEALRAILIAHKFRTKGQNLGQIQNIWNEGE | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 24025
Sequence Length: 207
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q3AC14 | MHKGMLVVVSGPSGAGKGTICQEIRKRNPNLFYSISATTREKRVGEIDGVHYYFIDRQQFEKMIANDEFLEWADVYGNYYGTPKKPVFEALARGQDVILEIDIKGARQVKKTYPEGVFVFILPPSISILEERLRKRGTDKEEIIVKRMQMAWEEIANCDWYDYLILNDDLETAVNDLEAVLTAEKLKPKRVNYRVLLEGGVLER | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23494
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q9A7N9 | MNKSHHPHRGLLLMVVAPSGVGKTSLTRRLVSDHGDLHLSISATTRDPRPGEHDGRDYHFVSRDKFQGMLAEDAFLEWAEVYGNFYGSPKAPIMDALSRGESVLFDIDFQGAMKVHKQAGADSVLVYILPPSLAEMSRRLHTRSQDSEEVIHRRLSRAKDEVAAWEQFDYVILNDDFDRAYADLAHIYHAERLKRARNPWIGDLVSDLLKEEI | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 24219
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q3J2A5 | MARRGLLLILSSPSGAGKSTLSKRLTAWDPSIRFSVSATTRAPRPGEVDGRDYYFRTRDEFIAAVEAGEMLEHAEVFGNFYGSPKAPVEKALEQGHDTLFDIDWQGGQQIRNSSLGRDVVSIFVLPPSIGELDRRLRSRAQDSEEVIATRMARSKDEISHWAEYDYVLVNRDLDLAEEQLKMILSAERLRRDRQPDLMDFVRGLNGEFETR | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23948
Sequence Length: 211
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q11HG8 | MESASPSATIRRRGVMLVLSSPSGAGKSTIARSLLENDHEFELSVSVTTRPRRPSEIEGVHYHFKTQRDFEMMRDGGDLLEWAEVHGNCYGTPRGPVERAIAGGRDMLFDIDWQGAAQLREKMPDDIVSVFILPPTMKELLARLTRRAEDTPEIIERRLRNAHHEIEQWRDYDYVVINDDLDRAFASVRAIVSAERLRHERRPGLEDFVAGLLAERPE | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 24890
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q3AQL3 | MAVEPSGKLIVFSAPSGAGKTTIATMVLQRIANLSFSVSATTRKQREGEQDGVNYYFLDKATFEKKIEQGGFIEHEFFFGNYYGTLLDATESVLASGKNLLLDVDVKGALNVRKLFGERSLLIFIQPPSMEVLIERLQGRGSEDDAALQERLERARFEMSFADQFDTIIVNNNLTAAVDDVEAAIVNFIG | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 20968
Sequence Length: 190
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q822M8 | MKDKVRVPFSPDHPSCAPKLFTISAPAGAGKTTLVRMLAQEFPDSFQKTLSLTTRAPRPEEVSGIDYWFVSQEEFKQRLDSNNFLEWVLLFGEYYGTSRLEIDEIWKSGKHAVAVIDVEGALSLKSKIPTVTIFISAPSQEELERRLKYRGSEQDSQRQERLQHSLIEQAASNQFEYVIINDDLQKSYEILKSIFIAEEHRNVL | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23398
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q9Z961 | MNKILVDSPFSPDHQKCCPKLFTISAPAGVGKTTLVRMLEQEFSSAFAETISVTTRKPREGEVPGKDYHFVSHEEFQRLLDRQALLEWVFLFGECYGTSMLEIERIWSLGKHAVAVIDIQGALFIRSRMPSVSIFIAPPSQEELERRLASRGSEEGSQRKERLEHSLIELAAANQFDYVIINDDLNQAYRVLKSIFIAEEHRNIL | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23368
Sequence Length: 205
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q8KFS5 | MSAEQVLDQGRLIVFSAPSGTGKSTVAKLVMERLGSLEFSVSATTRQMRAGERDGVDYHFLSREEFEKKIAENGFIEHEFFFGNFYGTLLDKTIDAIKAGHNLLFDLDVKGALNLKRIFGDQALLVFLKPPSMEELARRLQARDSESAEALKSRLERAEMELSHAGEFDFVVVNDDLGRTVDAVATRIAEFLPQP | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 21773
Sequence Length: 195
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q9HTM2 | MSGTLYIVSAPSGAGKTSLVKALLDAAPEVRVSVSHTTRGMRPGEVDGVNYHFTSREEFLAMLERNEFLEHAEVFGNLYGTSQRWVEKTLAEGLDLILEIDWQGAQQVRRLMPEAQSIFILPPSQEALRQRLTNRGQDSDEVIERRMREAVSEMSHYVEYDHLVINDDFAHALDDLKAIFRARQLRQDAQQQRHAELLGRLLA | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23102
Sequence Length: 203
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q4K3R4 | MTHSTGTLYIISAPSGAGKSSLVKALTDAKPEIRVSVSHTTRAMRPGEVDGVNYHFVSRETFVKMGEHGDFLERAEVFGNLYGTSQSHLQQTLDAGHDLILEIDWQGAEQVRKLMPQARSIFILPPSLQALHQRLTNRGQDSDEVIDGRMREAVSEMSHYVDYDYLIINDDFAHALGDLKAIFRANQLQQKRQQQRFGKLLAELLG | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23121
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q88C87 | MNHSSGTLYIVSAPSGAGKTSLVTALTKDDQQIRVSVSHTTRAMRPGEQHGVNYHFVVHEEFKALIAQGDFLEHAEVFGNFYGTSRSALQQTLDQGYDLILEIDWQGAQQVRKLMPQALSVFILPPSQEALRHRLDGRGQDSEEIIAGRMKEAVSEMVHYDEYDYVIINDDFDTALADLKAVFRSNRLLLKKQQQRHAALLKQMIG | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23184
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q4FQY7 | MTGSLFIITAASGTGKTSLVKQLLATTNDLTVSVSHTTRDPRPGEIDGHHYHFTDVDNFVTAISESQFLEHAEVFGNYYGTSEQSVRAQLDAGVDVILEIDWQGALQVKKIFTDAIMIFILPPSIATLRQRLSTRGQDSMEVIEQRLAGAVNEMAQYINFDYVIINDNFEVALTELKAIIVADRQTLKRQQQRYQRTITNLLSNIVDK | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23293
Sequence Length: 208
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q984S9 | MVPRDLGSRIRRRGLMLVLSSPSGAGKSTIARNLLESDSSLELSVSVTTRPRRGSEIEGVHYHFRTMREFERLRDSDALLEWAEVHGNCYATPREPAELALAQGRDMLFDIDWQGAQQLKEKMRADIVSIFILPPSMKELKARLKRRAEDQEAVIETRLKNARNEIEHWKEYDFVIVNDDLDRAFAEVRGIVVAERLRRDRRPGLFDFVSGLLDEKTV | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 25105
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q7UP92 | MNDPSCSSADETAHPGRLVIISGPSGAGKSTVVKQLMKRCDVPLQLSVSATTREPRPGEIHGQDYFFLSHEEFERRRKLNDFVECKQVFSMGQWYGTLKDQVATGLNAGKWVILEIDVQGAMAVLDDPHYRPVTIFVHPGSMEELERRLRNRGTESESSLTARLETAAAEMQCLSRYQYEIINESVDNAVTEICQILLDQRKTTPCSKN | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23450
Sequence Length: 209
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q2IX83 | MKDGAAGSLNGIERRGLMFVLSSPSGAGKTTLSRMLVDEAPGLRMSVSATTRPKRPGEVDGRDYYFVDRPKFDAMVEAGEFLEWANVFDNCYGTPRAPVEAALSAGNDVLFDIDWQGTQQLRSRASNDVVSVFILPPSVQDLEHRLHTRAQDSDEVIRGRMKKAGDEMSHFDAYDYIVVNDNIGVAFESVKAILRAEQLKRERQIGIDAFVREMRRELEK | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 24616
Sequence Length: 220
Subcellular Location: Cytoplasm
EC: 2.7.4.8
|
Q6A8B2 | MDNSVRVRVPATSANLGPGYDCIGLALDLWDEVSVGVLDRPGVMIDVTGEGADTVPHDESHLVMATLRQGLVELGYPHPDAGLHLTAINSIPQSRGLGSSAAAVVSGLALAWGLARPGFPLDRSALLTMAAAIEGHPDNAAPAILGGAQLAWLDGEAVNHIGLTVNPSIVFRVYVPDRLVPTALARQVLPEQVDRVDAVHQVLAASLLVTALTTSPEHLLAATQDWIHQPYRRALMPESAALTDRLRGRGVATVISGAGPTVLALGSRDQLEKVSDVDTAGFVAHDLVLGEGVHFF | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 31006
Sequence Length: 296
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.... |
Q9RRU5 | MSSPARPFTVRAPASSANLGPGFDSLGLSVPLYTTLRVTPQDKAEVVPLGTELADTPADESNYVYRAMTLAAKRAGRTLPPARVEIETEVPLARGLGSSAAALVAGVVAGNELLGRPLDDETVLDVTAREEGHPDNVAPALFGGIVVATLDKLGTHYVRLDPPAHLGVTVLVPDFELSTSKARAVLPREYSRADTVHALSHAALLAAALAQGRLDLLRHAMQDYVHQVWRAPLVPGLSDILEHAHEYGALGAALSGAGPTVLCFHDQRGSTATLHHYLHDVMTKNGLSGRVMDFPIDAAGTVVEHAK | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 32390
Sequence Length: 307
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.... |
Q24XU1 | MVRVRIPATSANLGPGFDCLGMALSLYNVVQIEAADSFQIALKGDYTAGIPGDETNLVWQSMCNLWEAIGFEIPTVSLELENNIPPTRGMGSSSAAIVGGLVAANEYAGGVLSKQQILQIANRIEGHPDNVAPALLGGVTLAVTAEASVIARTVHSQPQFMALAIVPDFYLSTEKSRNVLPASISRADAVYNLSRTALLVEALIHENHELLKEGMQDRLHQNQRAGLVPGLGETLQVALDSGAYGSALSGSGPTILALVSSHRAEQVSQAMVDSLAAHGLTAKAYLLSVDSEGAAVI | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 31093
Sequence Length: 297
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.... |
Q21017 | MAAPRRRMGLEKIGLYDVGRAIGKGNFATVRIARHKIAKTKVAIKSIDVSALDRENLIKLEREVKIVKVIDHPHIVKSYEIMRVDNMLYIVSEYCSSGELYETLIEKGRVAENVARKWFSETASAVAYLHSQGIVHRDLKAENILLGKNSNIKIIDFGFSNFQTGDQLLNTWCGSPPYAAPELLLGNSYDGMKADIWSMGVLLYILVAGGFPFPSDSVNKLKRSVLSGLVKIPYWVSVECADFIRKMLVLNPGKRYTIQNVLQHRWMHIRDDVQKNQAAQLLEAIPSSSIEIRQQSTKLNPTIMMFMQQHGKWSEEQIID... | Function: Regulates chemoreceptor expression by phosphorylating the hda-4 class II histone deacetylase (HDAC) and inhibiting the gene repression functions of hda-4 and the mef-2 transcription factor, enabling the correct sensing and transduction of food signals. Role in determining body size, the dauer decision and ser... |
P22209 | MHRRQFFQEYRSPQQQQGHPPRSEYQVLEEIGRGSFGSVRKVIHIPTKKLLVRKDIKYGHMNSKERQQLIAECSILSQLKHENIVEFYNWDFDEQKEVLYLYMEYCSRGDLSQMIKHYKQEHKYIPEKIVWGILAQLLTALYKCHYGVELPTLTTIYDRMKPPVKGKNIVIHRDLKPGNIFLSYDDSDYNINEQVDGHEEVNSNYYRDHRVNSGKRGSPMDYSQVVVKLGDFGLAKSLETSIQFATTYVGTPYYMSPEVLMDQPYSPLSDIWSLGCVIFEMCSLHPPFQAKNYLELQTKIKNGKCDTVPEYYSRGLNAII... | Function: This protein is probably a serine/threonine protein kinase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 51203
Sequence Length: 435
EC: 2.7.11.1
|
Q01919 | MASVPKRHTYGGNVVTDRDRHSLQRNNEILHPIHKNQRKHATFGPYIIGSTLGEGEFGKVKLGWTKASSSNEVPKQVAIKLIRRDTIKKDADKEIKIYREINALKHLTHPNIIYLEEVLQNSKYIGIVLEFVSGGEFYKYIQRKRRLKESSACRLFAQLISGVNYMHYKGLVHRDLKLENLLLDKHENLVITDFGFVNEFFEDNELMKTSCGSPCYAAPELVVSTKAYEARKADVWSCGVILYAMLAGYLPWDDDHENPTGDDIARLYKYITQTPLKFPEYITPIPRDLLRRILVPNPRRRINLQTIKRHVWLKPHEAFL... | Function: This protein is probably a serine/threonine protein kinase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 90088
Sequence Length: 800
EC: 2.7.11.1
|
P25341 | MTQQEYRSPSQRLSKGRSMSLPKIFARNLRSLQNNAPPGKNINVNCLNVNSCSLSASPSSQINMACNGNKQDLPIPFPLHVECNDSWSSSKLNKFKSMFNHNRSKSSGTTDASTSEKGTHKREPRSTIHTELLQSSIIGEPNVHSTTSSTLIPNEAICSTPNEISGSSSPDAELFTFDMPTDPSSFHTPSSPSYIAKDSRNLSNGSLNDINENEELQNFHRKISENGSASPLANLSLSNSPIDSPRKNSETRKDQIPMNITPRLRRAASEPFNTAKDGLMREDYIALKQPPSLGDIVEPRRSRRLRTKSFGNKFQDITVE... | Function: Flippase activator that phosphorylates DFN1 and DFN2 and which is involved in the generation of phospholipid asymmetry in membranes by the inward translocation of phospholipids.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 81462
Sequence Length: 72... |
P16497 | MEQDTQHVKPLQTKTDIHAVLASNGRIIYISANSKLHLGYLQGEMIGSFLKTFLHEEDQFLVESYFYNEHHLMPCTFRFIKKDHTIVWVEAAVEIVTTRAERTEREIILKMKVLEEETGHQSLNCEKHEIEPASPESTTYITDDYERLVENLPSPLCISVKGKIVYVNSAMLSMLGAKSKDAIIGKSSYEFIEEEYHDIVKNRIIRMQKGMEVGMIEQTWKRLDGTPVHLEVKASPTVYKNQQAELLLLIDISSRKKFQTILQKSRERYQLLIQNSIDTIAVIHNGKWVFMNESGISLFEAATYEDLIGKNIYDQLHPCD... | Function: Phosphorylates the sporulation-regulatory proteins spo0A and spo0F. It also autophosphorylates in the presence of ATP.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 69171
Sequence Length: 606
EC: 2.7.13.3
|
Q84VQ1 | MGNANGKDEDAAAGSGGADVTSSSARSNGGDPSARSRHRRPSSDSMSSSPPGSPARSPSPFLFAPQVPVAPLQRANAPPPNNIQWNQSQRVFDNPPEQGIPTIITWNQGGNDVAVEGSWDNWRSRKKLQKSGKDHSILFVLPSGIYHYKVIVDGESKYIPDLPFVADEVGNVCNILDVHNFVPENPESIVEFEAPPSPDHSYGQTLPAAEDYAKEPLAVPPQLHLTLLGTTEETAIATKPQHVVLNHVFIEQGWTPQSIVALGLTHRFESKYITVVLYKPLTR | Function: Regulatory subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex, which may play a role in a signal transduction cascade regulating gene expression and carbohydrate metabolism in higher plants. The SnRK complex may also be involved in the regulation of fatty acid synthesis by phosphoryla... |
Q9SCY5 | MGNVNAREEANSNNASAVEDEDAEICSREAMSAASDGNHVAPPELMGQSPPHSPRATQSPLMFAPQVPVLPLQRPDEIHIPNPSWMQSPSSLYEEASNEQGIPTMITWCHGGKEIAVEGSWDNWKTRSRLQRSGKDFTIMKVLPSGVYEYRFIVDGQWRHAPELPLARDDAGNTFNILDLQDYVPEDIQSISGFEPPQSPENSYSNLLLGAEDYSKEPPVVPPHLQMTLLNLPAANPDIPSPLPRPQHVILNHLYMQKGKSGPSVVALGSTHRFLAKYVTVVLYKSLQR | Function: Regulatory subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex, which may play a role in a signal transduction cascade regulating gene expression and carbohydrate metabolism in higher plants. The SnRK complex may also be involved in the regulation of fatty acid synthesis by phosphoryla... |
Q08430 | MEILKDYLLHICFILFPILLYQVFWLGKPAILVPKINSGLVTLFACGASVLCIIFPIHEMDYIQYGLQMIPVIICLFYISTASGLTVAASVLCFELLFYEPSAMFVFTLLPFLIIIPILFQKKWPFMSKAKKLLLSLLISCVEIFLFFASSWILSALNILNFQKSGIFVYEAAVSGLFRSSVLLLSIYIIESIAENIALRSQLIHSEKMTIVSELAASVAHEVRNPLTVVRGFVQLLFNDETLQNKSSADYKKLVLSELDRAQGIITNYLDMAKQQLYEKEVFDLSALIKETSSLMVSYANYKSVTVEAETEPDLLIYGD... | Function: Phosphorylates the sporulation-regulatory proteins spo0A and spo0F. Spo0F is required for the KinB activity.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47812
Sequence Length: 428
Subcellular Location: ... |
O34206 | MSMPLPMKLRTRLFLSISALITVSLFGLLLGLFSVMQLGRAQEQRMSHHYATIEVSQQLRQLLGDQLVILLRETPDGQALERSQNDFRRVLEQGRANTVDSAEQAALDGVRDAYLQLQAHTPALLEAPMVDNDGFSEAFNGLRLRLQDLQQLALAGISDAETSARHRAYLVAGLLGLVGVAILLIGFVTAHSIARRFGAPIETLARAADRIGEGDFDVTLPMTNVAEVGQLTRRFGLMAEALRQYRKTSVEEVLSGERRLQAVLDSIDDGLVIFDNQGRIEHANPVAIRQLFVSNDPHGKRIDEILSDVDVQEAVEKALL... | Function: Member of the two-component regulatory system AlgB/KinB involved in regulation of alginate biosynthesis genes. KinB functions as a membrane-associated protein kinase that phosphorylates AlgB, probably in response to environmental signals.
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein... |
P39764 | MRKYQARIISIILAMIFIMFWDYLFYFIGKNPINWPVDIVYTAVTLVSVWMLAYYIDEKQQLVKKMKDNEWKYKQLSEEKNRIMDNLQEIVFQTNAKGEITYLNQAWASITGFSISECMGTMYNDYFIKEKHVADHINTQIQNKASSGMFTAKYVTKNGTIFWGEVHYKLYYDRDDQFTGSLGTMSDITERKEAEDELIEINERLARESQKLSITSELAAGIAHEVRNPLTSVSGFLQIMKTQYPDRKDYFDIIFSEIKRIDLVLSELLLLAKPQAITFKTHQLNEILKQVTTLLDTNAILSNIVIEKNFKETDGCMING... | Function: Phosphorylates the sporulation-regulatory protein Spo0A a transcription factor that also controls biofilm formation (Probable). Requires FloT and FloA for localization to DRMs and for activity .
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass ... |
O31671 | MLERCKLKILKGACGRVKLYIILVVIPAIVISFFVYEKEKDTIAAEHKQEASVLLNLHRNKINYLIGETMARMTSLSIAIDRPVDIKKMQSILEKTFDSEPRFSGLYFLNAKGDVTASTTELKTKVNLADRSFFIKAKETKKTVISDSYSSRITGQPIFTICVPVLDSKRNVTDYLVAAIQIDYLKNLINLLSPDVYIEVVNQDGKMIFASGQASHAEDQKPVSGYLDDISWNMKVYPNPVTIEELSKSLVLPLSCIIVLLNILFILVLYYLLKRQTQLERSENEAQKLELIGTLAASTAHEIRNPLTGISGFIQLLQKK... | Function: Phosphorylates the sporulation-regulatory protein spo0F and, to a minor extent, is responsible for heterogeneous expression of spo0A during logarithmical growth. Also phosphorylates spo0A under biofilm growth conditions.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Loca... |
O31661 | METLGVQTNSELREELNRLKEENARLKKELNQHQVIVNNTLDAIFICDNEMRIVQANEATERMLQVDSEDLKKRSVLDFLFSIPKDELNLSVKKFFKKGFLWKEVPIRLDCGATKYIEFLAKRGIGEDFFFVVMRDISSKKILEREFSMNEQLFKDLFDRAVDGIVLFDKDGGFIDANLSFCKSFEINHNELSHLSLYEFIDSGSRKDFDNIWKALNRKGKAKGELPVKLRSGVQKLFEFTITSNIISGFYMSIMRDITEKRSMELQLFKSEERFREIFENAMDAIIIWSNDGRIVKANQSACKIFELPMNLLLKRKLCD... | Function: Phosphorylates the sporulation-regulatory protein spo0A under biofilm growth conditions. Also able to weakly phosphorylate spo0F.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 85513
Sequence Length: 738
EC: 2.7.13.3
|
Q8LBB2 | MATVPEIKIMRSESLGHRSDVSSPEAKLGMRVEDLWDEQKPQLSPNEKLNACFESIPVSAFPLSSDSQDIEIRSDTSLAEAVQTLSKFKVLSAPVVDVDAPEDASWIDRYIGIVEFPGIVVWLLHQLEPPSPRSPAVAASNGFSHDFTTDVLDNGDSAVTSGNFFEVLTSSELYKNTKVRDISGTFRWAPFLALQKENSFLTMLLLLSKYKMKSIPVVDLGVAKIENIITQSGVIHMLAECAGLLWFEDWGIKTLSEVGLPIMSKDHIIKIYEDEPVLQAFKLMRRKRIGGIPVIERNSEKPVGNISLRDVQFLLTAPEI... | Function: Regulatory subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex, which may play a role in a signal transduction cascade regulating gene expression and carbohydrate metabolism in higher plants. The SnRK complex may also be involved in the regulation of fatty acid synthesis by phosphoryla... |
P34540 | MEPRTDGAECGVQVFCRIRPLNKTEEKNADRFLPKFPSEDSISLGGKVYVFDKVFKPNTTQEQVYKGAAYHIVQDVLSGYNGTVFAYGQTSSGKTHTMEGVIGDNGLSGIIPRIVADIFNHIYSMDENLQFHIKVSYYEIYNEKIRDLLDPEKVNLSIHEDKNRVPYVKGATERFVGGPDEVLQAIEDGKSNRMVAVTNMNEHSSRSHSVFLITVKQEHQTTKKQLTGKLYLVDLAGSEKVSKTGAQGTVLEEAKNINKSLTALGIVISALAEGTKSHVPYRDSKLTRILQESLGGNSRTTVIICASPSHFNEAETKSTL... | Function: Microtubule-dependent motor protein required for organelle transport . Plays a role in endosome transport . Required for the transport of mitochondria along the axon of motor neurons . Involved in the nuclear migration of hyp7 hypodermal precursor cells . Required for the formation of dendritic branches of PV... |
A7NI79 | MTRLSSGGRIEVICGCMFSGKTEELIRRLNHVRLARQRLIAFTPRRDTRYRLGSLVSHNGLSVEARVIDSIRDTPAHLNTDIHVVAVDELHLLDDPPDAAREVCQDLADRGLRVIVAGLDQDFRAQPFPAMAQLMAVAEQVDKLYAICVRCGAYATRSQRLIDGKPAPADAPTIVVGGQELYEARCRACYEPAR | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 21494
Sequence Length: 194
Subcellular Location: Cytoplasm
EC: 2.7.1.21
|
Q5LUY8 | MAKLYFNYSTMNAGKSTVLLQASHNYRERGMQTYLMTAAIDGRAGTGRIASRIGIGAEADIFTPRDDVFAMIRDRLGAGPVACVFVDEAQFLSPEQVWQLARVVDDLDVPVLAYGLRVDFQGKLFPGSATLLALADEMREVRTICKCGRKATMVIRQDASGRAITEGAQVQIGGNETYVSLCRKHWREATGDPGAKGH | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 21618
Sequence Length: 198
Subcellular Location: Cytoplasm
EC: 2.7.1.21
|
Q2RZH4 | MDRDRTTGWMEVICGSMFSGKTEELIRRLRRARIARQHTRVFKPALDERYSEDEVVSHNENSVTTTPVEAPPQIQELVQEADVVGIDEAQFFDDDLVPTCQALAEDGHRVIVVGLDTDYRAEPFDPMPQLMAVAEHVTKLHAVCVVCGAPANHSQRIVPGEDRVLVGATEAYEPRCRACFEPEPVTVTRPRPHTEALRAVATDDADASTNEADPEAADAASADGTAA | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 24876
Sequence Length: 227
Subcellular Location: Cytoplasm
EC: 2.7.1.21
|
Q07866 | MYDNMSTMVYIKEDKLEKLTQDEIISKTKQVIQGLEALKNEHNSILQSLLETLKCLKKDDESNLVEEKSNMIRKSLEMLELGLSEAQVMMALSNHLNAVESEKQKLRAQVRRLCQENQWLRDELANTQQKLQKSEQSVAQLEEEKKHLEFMNQLKKYDDDISPSEDKDTDSTKEPLDDLFPNDEDDPGQGIQQQHSSAAAAAQQGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAANLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLC... | Function: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport . The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity).
PTM: Phosphorylation at Ser-460 by ERK inhibits interaction with CLSTN1 an... |
Q9H0B6 | MAMMVFPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLVAPEAGEAEPGSQERCILLRRSLEAIELGLGEAQVILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQIRKLDEDASPNEEKGDVPKDTLDDLFPNEDEQSPAPSPGGGDVSGQHGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKEAAHLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKFH... | Function: Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (Probable). Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence dire... |
O88448 | MATMVLPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLASHEAGEAEPGSQERCLLLRRSLEAIELGLGEAQVILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQIRKLDEMLPQEEKGDVPKDSLDDLFPNEDEQSPAPSPGGGDVAAQHGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAAHLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKFHP... | Function: Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity. Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosome... |
Q6P597 | MSVQVAAPGSAGLGPERLSPEELVRQTRQVVQGLEALRAEHHGLAGHLAEALAGQGPAAGLEMLEEKQQVVSHSLEAIELGLGEAQVLLALSAHVGALEAEKQRLRSQARRLAQENVWLREELEETQRRLRASEESVAQLEEEKRHLEFLGQLRQYDPPAESQQSESPPRRDSLASLFPSEEEERKGPEAAGAAAAQQGGYEIPARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATDLLHDALQIREQTLGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEI... | Function: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Plays a role during spermiogenesis in the development of the sperm tail midpiece and in the normal function of spermatozoa (By similarity). May play a role in the formation of the mitochondrial sheath form... |
Q9UH77 | MEGESVKLSSQTLIQAGDDEKNQRTITVNPAHMGKAFKVMNELRSKQLLCDVMIVAEDVEIEAHRVVLAACSPYFCAMFTGDMSESKAKKIEIKDVDGQTLSKLIDYIYTAEIEVTEENVQVLLPAASLLQLMDVRQNCCDFLQSQLHPTNCLGIRAFADVHTCTDLLQQANAYAEQHFPEVMLGEEFLSLSLDQVCSLISSDKLTVSSEEKVFEAVISWINYEKETRLEHMAKLMEHVRLPLLPRDYLVQTVEEEALIKNNNTCKDFLIEAMKYHLLPLDQRLLIKNPRTKPRTPVSLPKVMIVVGGQAPKAIRSVECY... | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of ion transport in the distal nephron . The BCR(KLHL3) complex acts by mediating ubiquitination and degradation of WNK1 and WNK4, two activators of Na-Cl cotransporter SLC12A3/NCC in distal convoluted tub... |
E0CZ16 | MEGESVKPSPQPTAQAEDEEKNRRTVTVNAAHMGKAFKVMNELRSKRLLCDVMIVAEDVEVEAHRVVLAACSPYFCAMFTGDMSESKAKKIEIKDVDGQTLSKLIDYIYTAEIEVTEENVQVLLPAASLLQLMDVRQNCCDFLQSQLHPTNCLGIRAFADVHTCTDLLQQANAYAEQHFPEVMLGEEFLSLSLDQVCSLISSDKLTVSSEEKVFEAVISWINYEKETRLDHMAKLMEHVRLPLLPRDYLVQTVEEEALIKNNNTCKDFLIEAMKYHLLPLDQRLLIKNPRTKPRTPVSLPKVMIVVGGQAPKAIRSVECY... | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of ion transport in the distal nephron . The BCR(KLHL3) complex acts by mediating ubiquitination and degradation of WNK1 and WNK4, two activators of Na-Cl cotransporter SLC12A3/NCC in distal convoluted tub... |
Q5REP9 | MEGESVKLSSQTLIQAGDDEKNQRTITVNPAHMGKAFKVMNELRSKQLLCDVMIVAEDVEIEAHRVVLAACSPYFCAMFTGDMSESKAKKIEIKDVDGQTLSKLIDYVYTAEIEVTEENVQVLLPAASLLQLMDVRQNCCDFLQSQLHPTNCLGIRAFADVHTCTDLLQQANAYAEQHFPEVMLGEEFLSLSLDQVCSLISSDKLTVSSEEKVFEAVISWINYEKGTRLEHMAKLMEHVRLPLLPRDYLVQTVEEEALIKNNNTCKDFLIEAMKYHLLPLDQRLLIKNPRTKPRTPVSLPKVMIVVGGQAPKAIRSVECY... | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of ion transport in the distal nephron. The BCR(KLHL3) complex acts by mediating ubiquitination and degradation of WNK1 and WNK4, two activators of Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubu... |
Q5ZI33 | MAAPGSEKSSKKKTEKKLAAREEAKLLAGFMGVMNSMRKQRTLCDVILMVQERRIPAHRVVLASASHFFNLMFTTNMLESKSFEVELKDAEPDIIEQLVEFAYTARISVNSNNVQSLLDAANQYQIEPVKKMCVDFLKEQVDASNCLGISVLAECLDCPELKATADDFIHQHFTEVYKTDEFLQLDVKRVTHLLNQDTLTVRAEDQVYDAAVRWLKYDEPNRQPYMVDILAKVRFPLISKNFLSKTVQAEPLIQDNPECLKMVISGMRYHLLSPEDREELVEGTRPRRKKHDYRIALFGGSQPQSCRYFNPKDYSWTDIR... | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. The BCR(KLHL7) complex acts by mediating ubiquitination and subsequent degradation of substrate proteins. Probably mediates 'Lys-48'-linked ubiquitination (By similarity).
Sequence Mass (Da): 66196
Sequence Length: 586
Pathway: P... |
Q8IXQ5 | MAASGVEKSSKKKTEKKLAAREEAKLLAGFMGVMNNMRKQKTLCDVILMVQERKIPAHRVVLAAASHFFNLMFTTNMLESKSFEVELKDAEPDIIEQLVEFAYTARISVNSNNVQSLLDAANQYQIEPVKKMCVDFLKEQVDASNCLGISVLAECLDCPELKATADDFIHQHFTEVYKTDEFLQLDVKRVTHLLNQDTLTVRAEDQVYDAAVRWLKYDEPNRQPFMVDILAKVRFPLISKNFLSKTVQAEPLIQDNPECLKMVISGMRYHLLSPEDREELVDGTRPRRKKHDYRIALFGGSQPQSCRYFNPKDYSWTDIR... | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. The BCR(KLHL7) complex acts by mediating ubiquitination and subsequent degradation of substrate proteins. Probably mediates 'Lys-48'-linked ubiquitination.
Sequence Mass (Da): 65992
Sequence Length: 586
Pathway: Protein modificat... |
G5ED84 | MPVYAKAIFGSFPSVQQVRVENGERCLIEAMDELNKNEKGLYRPVRLENGDQISTTDDVLNGKLARVSYTPFEEFELVSNSKGSCMEYENQEQSSKIMEQMRILRQTEELCDVELLVAGSVIRAHRYILAAASPYFKAMFTNGMVEMKKLTIELQDIPEESVRIIVDYIYTDKIAITMNNVHQLIFTATVLQMDVIVVACQQFLATMITSHNCMSLYHFSDIYNCTNLISSIEDFASSQFRCIRKSPEFNSISFHHLKSLLNRSDLNVSEEQDVFETIVQWVSSNPRDRQHHFVQLFKTLRLHLVGWNFLCEAVNSNSYV... | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates degradation of glutamate receptors in neurons. The BCR(kel-8) ubiquitin ligase complex mediates ubiquitination and subsequent degradation of rpy-1. Indirectly regulates the protein turnover of glr-1, possibly via ub... |
O43240 | MRAPHLHLSAASGARALAKLLPLLMAQLWAAEAALLPQNDTRLDPEAYGSPCARGSQPWQVSLFNGLSFHCAGVLVDQSWVLTAAHCGNKPLWARVGDDHLLLLQGEQLRRTTRSVVHPKYHQGSGPILPRRTDEHDLMLLKLARPVVLGPRVRALQLPYRCAQPGDQCQVAGWGTTAARRVKYNKGLTCSSITILSPKECEVFYPGVVTNNMICAGLDRGQDPCQSDSGGPLVCDETLQGILSWGVYPCGSAQHPAVYTQICKYMSWINKVIRSN | Function: Has a tumor-suppressor role for NES1 in breast and prostate cancer.
Sequence Mass (Da): 30170
Sequence Length: 276
Subcellular Location: Secreted
EC: 3.4.21.-
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Q07970 | MASRNQNRPPRSPNAKKEGLGGISFDKRRKVETQGGTGRRQAFSAVNKQDVTMNSDVGSIEECGKVDFTKDEILALLSERAKAGKFDTKAKIEQMTDIIKRLKVCVKWFQQADETHVQEKENLKVSLESSEQKYNHKELEARTKEEELQATISKLEENVVSLHEKLAKEESSTQDAIECHRREKEARVAAEKVQASLGEELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNSKLQTDLETVRAALTRAEKEKSSILENLSTLRGHSKSLQDQLSSSRVLQDDAIKQKDSLLSEVTNLRNELQQVRDDRDRQVVQS... | Function: Kinesin that supports microtubule movement in an ATP-dependent manner and has a minus-end directed polarity. Plays a crucial role in spindle morphogenesis in male meiosis. In mitosis, is required for normal microtubule accumulation at the spindle poles during prophase and may play a role in spindle assembly d... |
F4JGP4 | MPLRNQNRAPLPSPNVKKEALSSIPFDKRRKETQGTGRRQVLSTVNRQDANSDVGSTEECGKVEFTKDEVLALLNERAKAGKFDTKGKIEQMTDIIKKLKVCVRWYQQVDETHVQDKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKLSKEKLSKLDAIENHRREKDCRVVAEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKL... | Function: Kinesin that supports microtubule movement in an ATP-dependent manner and that functions as a minus-end directed motor as well as a plus-end tracking protein. During mitosis, is involved in early spindle assembly. Participates in the capture of antiparallel interpolar microtubules and helps in generating forc... |
P34885 | MLFTGTVRVRVLEARQLRPTEWSRRFRQDEAATAAIDSYVNVDWDEYHIGKTQVRPKTNEPRWNEEFTASGVHQGKAIGFSVFHSCVMPPDDFVANTRIAFDQLKIGSANDIWVDLEPHGQLHVVVEMHGTNVEDVHSHNKTRVFKERTNAFNDRQRRGAMRRKIHEVTGHKFMALFLRQPTFCAHCKEFIWGIGKQGYQCQICTVVVHKRCHEDVVWKCPGNKADAVEELGKEIQETGAGRFNINMPHRFSVHSYKRPTFCDHCGSMLYGLINQGLQCSTCKLNVHKRCQRNVANNCGINAKQMAAELAQLGLTGDKMS... | Function: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. Involved in neuropeptide secretion in motor axons. Likely to act via the extracellular signal-regulated kinase/mitogen-activated protein... |
Q16974 | MEKRVARRGALRQKNVHEVKNHKFLARFFKQPTFCSHCKDFIWGFGKQGFQCQVCSLVVHKRCHEFVCFICPGADKGPDSDATNLHKFKLHSYGSPTFCDHCGSLLYGLLHQGLKCDSCDMNVHKRCEKNVPLLCGTDHTERRGRILIKGAVKGSKVLVEILEAKNLCPMDPNGLADPYVKVKLIPYDAHKLKLKTKTIKASLNPVWNESFTVDIGPEDNSKRLSLEVWDWDRTSRNDFMGSLSFGISELIKSPVEGWFKLLNQEEGEFYGVPVTDDITESIQEIKSKMHRSSISSEKRYPEPDKVQNMSKQDIVRASDF... | Cofactor: Binds 3 Ca(2+) ions per C2 domain.
Function: This is calcium-dependent, phospholipid-dependent, serine- and threonine-specific enzyme. Activation of PKC by serotonin results in presynaptic facilitation of depressed sensory-to-motor neuron synapses, which is thought to underlie behavioral dishabituation.
Catal... |
P34722 | MAQAENACRLKLLRADVPVDLLPAGCSATDLQPAVNVKEKIEVNGESRLVQKKKTLYPEWEKCWDTAVAEGRILQIVLMFNQTPVVEATMRLEDIISKCKSDAITHIWINTKPNGRILAQTRHLKNAPDDDHPVEDIMTSRSNSGPGIQRRRGAIKHARVHEIRGHQFVATFFRQPHFCSLCSDFMWGLNKQGYQCQLCSAAVHKKCHEKVIMQCPGSAKNTKETMALKERFKVDIPHRFKTYNFKSPTFCDHCGSMLYGLFKQGLRCEVCNVACHHKCERLMSNLCGVNQKQLSEMYHEIKRGTHATASCPPNIANLHL... | Function: Diacylglycerol (DAG)-dependent serine/threonine-protein kinase that phosphorylates a range of cellular proteins (Probable). Phosphorylates mlk-1, a component of the JNK pathway. Involved in axon regeneration after injury probably by activating the JNK pathway . Plays a role in resistance to fungal infection a... |
Q6ZFT5 | MEVVVARQPKAKKQINLFYCSECEELALKVAASSDTIHLQSINWRSFDDGFPNLFINNAHDIRGQHVAFLASFSSPSVIFEQISVIFALPKLFIASFTLVLPFFPTGSFERVEEEGDVATAFTLARILSMIPKSRGGPTSVVIYDIHALQERFYFGDDVLPCFETGIPLLLQRLRQLPDADNITIAFPDDGAWKRFHKLLLNFPMVVCAKVREGDKRIVRIKEGNPEGRHVVIVDDLVQSGGTLRECQKVLAAHGAAKVSAYVTHAVFPKQSYERFTHTNSAGSADKFAYFWITDSCPQTVKAINQQPPFEVLSLAGSIA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)
Sequence Mass (Da): 36149
Sequence Length: 325
EC: 2.7.6.1
|
Q9XGA1 | MEKPNTKQVLLFYCVEAEELARKVAAQSPLITLQSINWRSFDDGFPNLFINNAQDIRGQHVAFLAAFSSPAVIFEQLSVIYALPRLFVASFTLVLPFFPTGSFERMEEEGDVATAFTMARILSNIPVSRGGPTSVVIYDIHALQERFYFSDNVLPLFETGIPLLKQRLDQLPDADKIVVAFPDDGAWKRFHKQLDHFPMVVCAKVREGDKRIVRLKEGNPAGCHVVIVDDLVQSGGTLIECQKVLAAHGATKVSAYVTHAVFPKNSFERFTHKDDGSDKAFTYFWITDSCPRTVKSIANKAPFEVLSLAGSIADALQI | Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)
Sequence Mass (Da): 35385
Sequence Length: 318
Subcellular Location: Cytoplasm
EC: 2.7.6.1
|
Q9YAW0 | MEGPEQWVIVGGWGSASAEFSEGLSRNMGLKLVKPVFKLFPDEEEYVRIEGDISGFTGAIVVQSFERPASRSLVYSLLIADALKEAGVGRIVLMAPYMGYTRQDRVFLPGEPVSVRAVMRALASSGYNALASIEVHKEYVLDYFDGSTLNIFPFTYMLKETGISCGDNTIIVAPDKGSLPRVERLARETGCRSYGYLVKERDRITGEVRLAKSTVDPRGKNAIVVDDIISTGGTIALASQWLLENGANSVFVLAAHYLGIGNAEEKMMKAGVSRVVTGNTLPRKPSKIVTYVDLTGLAAGQLTKLVSNL | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-r... |
P14193 | MSNQYGDKNLKIFSLNSNPELAKEIADIVGVQLGKCSVTRFSDGEVQINIEESIRGCDCYIIQSTSDPVNEHIMELLIMVDALKRASAKTINIVIPYYGYARQDRKARSREPITAKLFANLLETAGATRVIALDLHAPQIQGFFDIPIDHLMGVPILGEYFEGKNLEDIVIVSPDHGGVTRARKLADRLKAPIAIIDKRRPRPNVAEVMNIVGNIEGKTAILIDDIIDTAGTITLAANALVENGAKEVYACCTHPVLSGPAVERINNSTIKELVVTNSIKLPEEKKIERFKQLSVGPLLAEAIIRVHEQQSVSYLFS | Cofactor: Binds 2 Mg(2+) ions per subunit. Each Mg(2+) binds only one residue (His-136 and Asp-175, respectively) of this protein, however the magnesium ions also bind substrates and water molecules to complete their coordination spheres . Can also use Mn(2+) and Cd(2+) ions, but the activity is less than that obtained... |
Q8G5P2 | MVSAILEGKPDKNLILVTGRIHPKLAEDVAEQLGIDVLETTAYDFANGEMYVRYTESVRGADVFVLQSHYKPINKAIMEQLIMIDALKRASARSITAVCPLLGYSRQDKKHRGREPISCRLVFDLLKTAGADRIMSVDLHAAQSQGFFDGPVDHLVAMPVLVDYIRDRFQGHLDNVAVVSPDAGRIRVAEQWAQRLGGGPLAFVHKTRDITRPNQAVANRVVGDVAGKDCVLVDDLIDTAGTIAGACHVLQDAGAKSVTVVATHGVLSGPAVERLKNCGAREVVLTDTVPIPEEKRWDGLTVLSIAPLLASAIRAVFEDG... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-r... |
Q89DJ1 | MSAKNGSIKLVAGNSNPALAQAIAQGLHLPLTKAVVRRFADMEIFVEIQENVRGSDAFIIQSTSFPANDHLMELLIITDALRRSSARRITAVLPYFGYARQDRKSGSRTPISAKLVANLITQAGVDRVMTLDLHAGQIQGFFDIPTDNLYAAPLMVRDIKDKFDLSKTMVISPDVGGVARARGLAKRINTPLAIVDKRRERPGESEVMNVIGDVAGYTCILVDDIVDSGGTLVNAADALIAKGAKDVYAYITHGVLSGGAAARITNSKLKELVITDSILPTDAVSKAPNIRTLPIASLISDAIARTAAEESVSSLFD | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-r... |
P11980 | MPKPDSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSAPITARNTGIICTIGPASRSVEMLKEMIKSGMNVARLNFSHGTHEYHAETIKNVRAATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVKEKGADYLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKAADVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRA... | Function: Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic proc... |
P30613 | MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKIISKIENHEGV... | Function: Pyruvate kinase that catalyzes the conversion of phosphoenolpyruvate to pyruvate with the synthesis of ATP, and which plays a key role in glycolysis.
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 61830
Sequence Length: 574
Pathway: Carbohydrate degradation; glycolys... |
A0A1X9ISP7 | MSLLLSNSALVGPKFRSSRISHASASLDIGLQRATSPQNASVATCFEETKGRIAKLFHKNELSVSTYDTAWVAMVPSPTSSEEPCFPACLNWLLENQCHDGSWARPHHHHMLKKDVLSSTLACILALKKWGVGEEQISRGLHFVELNFASATEKGQITPMGFDIIFPAMLDNARGLSLNLQLEPTTLNDLIYKRDLELKRCNQSNSAEKEVYWAHIAEGMGKLQDWESVMKYQRKNGSLFNSPSTTAAAFIALRNSDCLNYLYSAMNKFGSAVPAVYPLDIYSQLCLVDNLERLGISRFFSTEIQSVLDDTYRCWLDGDE... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities . Catalyzes the conversion of ent-copalyl diphosphate (ent-... |
Q0JA81 | MVPALRRGGGGPRFPQCVAWIQRNQRGDGSWRHAAAAHQQLGSSPEIVTERDLSSTLACVLALARWDAGSEHVRRGLQFIGRNMSVAMDDQTAAPASGSVVSFAAMLRMAMEMGLEVPAVSQADVRDRDAGVICHGGRTEYTAYVSEGLGNIQNWNEVMKFQRKNGSLFNSPYTTAAALVHNYDAKALQYLDMLLDKFGSAVPAAYPANIQSQLYMVDVLEKMGISRHFVGEIKSILDMTYSCWKQRDEEIVLDMQTCGMAFRMLRMNGYDVSSDELSHFSEPSSFHNSLQGYLNDTRSLLELHKASKVSIAEKEVILDN... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Sequence Mass (Da): 102596
Sequence Length: 937
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.-
|
A0A1X9ISH5 | MSTLKLIPFSTSIDKQFSGRTSILGGKCCLQIDGPKTTKKQSKILVEKIRERISNGKVVEISASAYDTAWVAMVPSREMSGRPSFPECLDWIVENQNPDGSWGLNPFLVKDSLSCTLACLLALRKWGLPNHLLHKGIEFIESNISRAATDDENQVAPIGFNIIFPAMISYAKELDLTLTLPPSSLNALLRARDSEMIRREGKWEYVGEGLGDSCNWNQIIQKHQSRNGSLFNSPATTAAAAIHCRDHKCFDYLISVVNKCNGWAPTVYPMDIYARLCMIDTLQRLGIDCHFRVELDAIFDEIYRNWQEREEEIFSDVTCQ... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities . Catalyzes the conversion of (+)-copalyl diphosphate ((+)-... |
Q0JA83 | MFQLELVNVVMHQRKAIEDTMRKKKKQQLHKFEMLPSPYDTAWVAMVPLPGSSSQLPCFPQCVEWILQNQQSNGSWDLNQLDSITKDALLSTLACVLALRRGLLFIGRNFSIAMDEQLAAPIGFNITFPGMLSSVIEMGLEVPIGQTDVERVLHLQETELKREYEENYRGRNTYMAYVSEGLGNAQDWNEVMNFQRKNGSLFNSLSITAAVLVHNYDAKAHRYLNLLLNKFGTAVYTKNIHRQLSMLDALENMGISRHFDGEIKSILDMTYSCWLQRDEEVMLDITTCAMAFRILRMNGYDVSSDDLCHIAEVSDFHSSH... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Sequence Mass (Da): 84125
Sequence Length: 739
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.-
|
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