ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8VYY4 | MSVITTPIETLHLKSTLRLLPRAVYRSQRIQVFPPNIFSNTSLSSPLRIDPISQVGGSRNLWRRYASDNFSEMGLDPGADPFKVIEKPSIVDRMKKANSILPHVVLASTILALIYPPSFTWFTSRYFVPALGFLMFAVGINSNEKDFLEAFKRPKAILLGYVGQYLVKPVLGFIFGLAAVSLFQLPTPIGAGIMLVSCVSGAQLSNYATFLTDPALAPLSIVMTSLSTATAVLVTPMLSLLLIGKKLPVDVKGMISSILQVVIAPIAAGLLLNKLFPKVSNAIRPFLPILSVLDTACCVGAPLALNINSVMSPFGATILLLVTMFHLSAFLAGYFLTGSVFRNAPDAKAMQRTLSYETGMQSSLLALALATKFFQDPLVGIPPAISTVVMSLMGFTLVLIWSKEKSNTF | Function: May function as sodium-coupled metabolite transporter across the chloroplast envelope.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44207
Sequence Length: 409
Subcellular Location: Membrane
|
P30844 | MHFLRRPISLRQRLILTIGAILLVFELISVFWLWHESTEQIQLFEQALRDNRNNDRHIMREIREAVASLIVPGVFMVSLTLFICYQAVRRITRPLAELQKELEARTADNLTPIAIHSATLEIEAVVSALNDLVSRLTSTLDNERLFTADVAHELRTPLAGVRLHLELLAKTHHIDVAPLVARLDQMMESVSQLLQLARAGQSFSSGNYQHVKLLEDVILPSYDELSTMLDQRQQTLLLPESAADITVQGDATLLRMLLRNLVENAHRYSPQGSNIMIKLQEDDGAVMAVEDEGPGIDESKCGELSKAFVRMDSRYGGIGLGLSIVSRITQLHHGQFFLQNRQETSGTRAWVRLKKDQYVANQI | Function: Member of the two-component regulatory system BasS/BasR Autophosphorylates and activates BasR by phosphorylation.
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 41029
Sequence Length: 363
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
|
P36557 | MRFQRRAMTLRQRLMLTIGLILLVFQLISTFWLWHESTEQIQLFEQALRDNRNNDRHIMHEIREAVASLIVPGVFMVSLTLLICYQAVRRITRPLAELQKELEARTADNLAPIAIHSSTLEIESVVSAINQLVTRLTTTLDNERLFTADVAHELRTPLSGVRLHLELLSKTHNVDVAPLIARLDQMMDSVSQLLQLARVGQSFSSGNYQEVKLLEDVILPSYDELNTMLETRQQTLLLPESAADVVVRGDATLLRMLLRNLVENAHRYSPEGTHITIHISADPDAIMAVEDEGPGIDESKCGKLSEAFVRMDSRYGGIGLGLSIVSRITQLHQGQFFLQNRTERTGTRAWVLLKKA | Function: Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well.
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 40262
Sequence Length: 356
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
|
B0R6I4 | MSDIDRGLFERVLPARIRGSYAAKFNVLLLVVVIIVAAAGGYIHLQTQSTVGENTERRVSGIAEQQAATLHDWLTQKESTTTFLASNIGGDAVRTSDVKPQLERQLATLQQDVRAIHVVSTSQDTVVASTDDARSGTTLQAGDAPWLSTIEDGTTDVSVSDPYEVDDSPVVAMTAPTDKPGWVLVMTMSLAQHSQSFNSPIATGDVKVVNGDGVITLDNRNRALLEQYTDTAGNVPAAVATARSGQTVYNTEPERTGMDDGRYATAYTPVAGTDWVLTYHVPRGQAYALQSEVTQNLAGLVVVALVGLLLVGLTVGRRTSSALDELAGVAAAIADGDLDTTIPDTDRTDELGQLVGAFGEMQTYLTTAASQADALADQNFDADVLDEDLPGAFGASLSQMHTRLEALITDLDEAREDAEQTRKDAEEARAASERLNERLERRAAEYSDEMAAAAAGDLTRRLDEDVDSEPMQDIAEAFNDMMGDVEATLAQVRSIADAVDAASTDVSTSAAEIRSASDQVSESVQDISADADQQRDRLGTVGDEVTSLSATVEEIAASADDVAETVNQAATESERGQELGEDAVAELERIEATADSAVERVTALEEAVDAIGDVTGVITDIAEQTNMLALNANIEAARADKSGDGFAVVADEVKDLADEVKESATEIETLVDDVQADVADTVADMSELGDRVDAGSETIEAALAALDDIGDQVEAANGSVQSISDATDEQAASTEEVVTMIDEVTDLSDRTATESQQVSAAAEEQAASVSEVAGRADDLDDQVSTLNDLLDQFDARAASADTDEN | Function: Mediates chemotaxis towards five attractant amino acids (leucine, isoleucine, valine, methionine and cysteine). Probably transduces the signal from the substrate-binding protein BasB to the histidine kinase CheA.
PTM: Methylated by CheR.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84831
Sequence Length: 805
Subcellular Location: Cell membrane
|
Q94FV7 | MATEEMKKLATVMAIGTANPPNCYYQADFPDFYFRVTNSDHLINLKQKFKRLCENSRIEKRYLHVTEEILKENPNIAAYEATSLNVRHKMQVKGVAELGKEAALKAIKEWGQPKSKITHLIVCCLAGVDMPGADYQLTKLLDLDPSVKRFMFYHLGCYAGGTVLRLAKDIAENNKGARVLIVCSEMTTTCFRGPSETHLDSMIGQAILGDGAAAVIVGADPDLTVERPIFELVSTAQTIVPESHGAIEGHLLESGLSFHLYKTVPTLISNNIKTCLSDAFTPLNISDWNSLFWIAHPGGPAILDQVTAKVGLEKEKLKVTRQVLKDYGNMSSATVFFIMDEMRKKSLENGQATTGEGLEWGVLFGFGPGITVETVVLRSVPVIS | Function: Polyketide synthase producing 4-hydroxybenzalacetone. Can use p-coumaryl-CoA as substrate but does not accept hexanoyl-CoA, isobutyryl-CoA, isovaleryl-CoA, and acetyl-CoA as a substrates. Catalyzes the initial key reaction step in the biosynthesis of phenylbutanoids.
Catalytic Activity: 4-coumaroyl-CoA + H(+) + H2O + malonyl-CoA = 4-hydroxybenzalacetone + 2 CO2 + 2 CoA
Sequence Mass (Da): 42225
Sequence Length: 384
Pathway: Secondary metabolite biosynthesis; flavonoid biosynthesis.
EC: 2.3.1.212
|
Q9ZU50 | MGLGGDQSFVPVMDSGQVRLKELGYKQELKRDLSVFSNFAISFSIISVLTGITTTYNTGLRFGGTVTLVYGWFLAGSFTMCVGLSMAEICSSYPTSGGLYYWSAMLAGPRWAPLASWMTGWFNIVGQWAVTASVDFSLAQLIQVIVLLSTGGRNGGGYKGSDFVVIGIHGGILFIHALLNSLPISVLSFIGQLAALWNLLGVLVLMILIPLVSTERATTKFVFTNFNTDNGLGITSYAYIFVLGLLMSQYTITGYDASAHMTEETVDADKNGPRGIISAIGISILFGWGYILGISYAVTDIPSLLSETNNSGGYAIAEIFYLAFKNRFGSGTGGIVCLGVVAVAVFFCGMSSVTSNSRMAYAFSRDGAMPMSPLWHKVNSREVPINAVWLSALISFCMALTSLGSIVAFQAMVSIATIGLYIAYAIPIILRVTLARNTFVPGPFSLGKYGMVVGWVAVLWVVTISVLFSLPVAYPITAETLNYTPVAVAGLVAITLSYWLFSARHWFTGPISNILS | Function: May play a role in primary carbon metabolism and plant growth, by mediating the transport of GABA from the cytosol to mitochondria. When expressed in a heterologous system (yeast), imports Arg and Ala across the plasma membrane and exports Lys and Glu, but does not transport proline.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55332
Sequence Length: 516
Subcellular Location: Mitochondrion membrane
|
P82251 | MGDTGLRKRREDEKSIQSQEPKTTSLQKELGLISGISIIVGTIIGSGIFVSPKSVLSNTEAVGPCLIIWAACGVLATLGALCFAELGTMITKSGGEYPYLMEAYGPIPAYLFSWASLIVIKPTSFAIICLSFSEYVCAPFYVGCKPPQIVVKCLAAAAILFISTVNSLSVRLGSYVQNIFTAAKLVIVAIIIISGLVLLAQGNTKNFDNSFEGAQLSVGAISLAFYNGLWAYDGWNQLNYITEELRNPYRNLPLAIIIGIPLVTACYILMNVSYFTVMTATELLQSQAVAVTFGDRVLYPASWIVPLFVAFSTIGAANGTCFTAGRLIYVAGREGHMLKVLSYISVRRLTPAPAIIFYGIIATIYIIPGDINSLVNYFSFAAWLFYGLTILGLIVMRFTRKELERPIKVPVVIPVLMTLISVFLVLAPIISKPTWEYLYCVLFILSGLLFYFLFVHYKFGWAQKISKPITMHLQMLMEVVPPEEDPE | Function: Associates with SLC3A1 to form a functional transporter complex that mediates the electrogenic exchange between cationic amino acids and neutral amino acids, with a stoichiometry of 1:1 . Has system b(0,+)-like activity with high affinity for extracellular cationic amino acids and L-cystine and lower affinity for intracellular neutral amino acids . Substrate exchange is driven by high concentration of intracellular neutral amino acids and the intracellular reduction of L-cystine to L-cysteine . Required for reabsorption of L-cystine and dibasic amino acids across the brush border membrane in renal proximal tubules.
Catalytic Activity: L-arginine(in) + L-leucine(out) = L-arginine(out) + L-leucine(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53481
Sequence Length: 487
Subcellular Location: Apical cell membrane
|
B9EXZ6 | MTWNKAPAADAEAGGGGDTGHARLRELGYKQELKRDLSVLSNFAFSFSIISVLTGITTLYNTGLSFGGPATMTFGWFVAGAFTMTVGLSMAEICSSFPTSGGLYYWSARLSGKRWAPFASWITGWFNIVGQWAVTTSVDFSLAQLIQVIILLSTGGNNGGGYMASKYVVIAFHAAILLSHAAINSLPITWLSFFGQFAAAWNMLGVFVLMIAVPTVATERASAKFVFTHFNTENNAGIHSNFYIFVLGLLMSQYTLTGYDASAHMTEETKNADRNGPIGIISAIGISIIVGWGYILGITFAVKDIPYLLNPENDAGGYAIAEVFYLAFKSRYGSGIGGIICLGIVAVAIYFCGMSSVTSNSRMAYAFSRDGAMPLSSVWHKVNKHEVPINAVWLSALISLCMALPSLGSLVAFQAMVSIATIGLYVAYALPILFRVTLARKHFVPGPFNLGRCGVAVGWAAVLWVATITVLFSLPVSYPVTKDTLNYTPVAVGGLFLLVLSSWLLSARHWFKGPITNLDG | Function: May be involved in the transport of amino acids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55810
Sequence Length: 520
Subcellular Location: Membrane
|
P82252 | MEETSPRRRREDEKSVHSTEPKTTSLQKEVGLLSGICIIVGTIIGSGIFISPKSVLANTESVGPCLIIWAACGVLATLGALCFAELGTMITKSGGEYPYLMEAFGPIPAYLFSWTSLIVMKPSSFAIICLSFSEYVCAAFYLGCRPPAVVVKLLAAAAILLITTVNALSVRLGSYVQNVFTAAKLVIVAIIIISGLVLLAQGNVKNFQNSFEGSQTSVGSISLAFYNGLWAYDGWNQLNYITEELRNPYRNLPMAIVIGIPLVTVCYILMNIAYFTVMTPTELLQSQAVAVTFGDRVLYPASWVVPLFVAFSTIGAANGTCFTAGRLIYVAGREGHMLKVLSYISVKRLTPAPALVFYGIIAIIYIIPGDINSLVNYFSFAAWLFYGMTILGLVVMRFTRKDLERPIKVPIFIPIIVILVSVFLILAPIISSPAWEYLYCVLFILSGLIFYFLFVHYKFRWAQKISRPITKHLQMLMEVVPPEKDPE | Function: Associates with SLC3A1 to form a functional transporter complex that mediates the electrogenic exchange between cationic amino acids and neutral amino acids, with a stoichiometry of 1:1 (By similarity). Has system b(0,+)-like activity with high affinity for extracellular cationic amino acids and L-cystine and lower affinity for intracellular neutral amino acids (By similarity). Substrate exchange is driven by high concentration of intracellular neutral amino acids and the intracellular reduction of L-cystine to L-cysteine (By similarity). Required for reabsorption of L-cystine and dibasic amino acids across the brush border membrane in renal proximal tubules (By similarity).
Catalytic Activity: L-arginine(in) + L-leucine(out) = L-arginine(out) + L-leucine(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53658
Sequence Length: 487
Subcellular Location: Apical cell membrane
|
Q9SID1 | MKIQCDVCEKAPATLICCADEAALCAKCDVEVHAANKLASKHQRLFLDSLSTKFPPCDICLEKAAFIFCVEDRALLCRDCDEATHAPNTRSANHQRFLATGIRVALSSTSCNQEVEKNHFDPSNQQSLSKPPTQQPAAPSPLWATDEFFSYSDLDCSNKEKEQLDLGELDWLAEMGLFGDQPDQEALPVAEVPELSFSHLAHAHSYNRPMKSNVPNKKQRLEYRYDDEEEHFLVPDLG | Function: Acts as negative regulator of seedling photomorphogenesis . BBX25/STH and BBX24/STO function as transcriptional corepressors of HY5 activity, leading to the down-regulation of BBX22 expression. BBX25/STH acts additively with BBX24/STO during de-etiolation and the hypocotyl shade avoidance response .
PTM: COP1-mediated ubiquitination and subsequent proteasomal degradation of BBX25/STH occurs in the dark.
Sequence Mass (Da): 26657
Sequence Length: 238
Subcellular Location: Nucleus
|
Q8L649 | MNGDNRPVEDAHYTETGFPYAATGSYMDFYGGAAQGPLNYDHAATMHPQDNLYWTMNTNAYKFGFSGSDNASFYGSYDMNDHLSRMSIGRTNWDYHPMVNVADDPENTVARSVQIGDTDEHSEAEECIANEHDPDSPQVSWQDDIDPDTMTYEELVELGEAVGTESRGLSQELIETLPTKKYKFGSIFSRKRAGERCVICQLKYKIGERQMNLPCKHVYHSECISKWLSINKVCPVCNSEVFGEPSIH | Function: E3 ubiquitin-protein ligase that limits organ size, and possibly seed size, in a dose-dependent manner. Negatively regulates the duration of cell proliferation in leaves and petals independently of the major phytohormones (e.g. auxin, cytokinin, gibberellin, brassinosteroids, ethylene, abscisic acid, jasmonic acid), probably by targeting growth stimulators for degradation . Limits the proliferation of root meristematic cells . Polyubiquitinates DA1 . Involved in the promotion of leaf senescence, in addition to its function in restricting plant growth . Possesses E3 ubiquitin-protein ligase activity in vitro .
PTM: Auto-ubiquitinated.
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): 27983
Sequence Length: 248
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
|
Q65XS5 | MKPPRRWMYGRGGGKGKPAGLLLLGVFLCLSVVLLLLLHGSSPSLEGEGRKPEAVEAAGGGGEEEEVAVARAEVEEAPLPPGNARLAFLFIARNRLPLDLVWDAFFRGDKEGRFSIFVHSRPGFVLTRATTRSGFFYNRQVNNSVQVDWGEASMIEAERVLLAHALKDPLNERFVFVSDSCVPLYNFNYTYDYIMSSSTSFVDSFADTKAGRYNPRMDPIIPVENWRKGSQWAVLTRKHAEVVVEDEEVLPEFQKHCRRRPLPEFWRDWDRPIPAEAWKAHNCIPDEHYVQTLLAQHGLEEELTRRSVTHSAWDLSSSKDRERRGWHPVTYKISDATPALVKSIKDIDNIYYETENRKEWCTSNGKPAPCFLFARKFTRAAGLKLLDLSLIAANGASTM | Function: Glycosyltransferase required for the regulation of cellulose biosynthesis in the cell wall . Required for the biosynthesis of hexoses (glucose, mannose and galactose) in both cellulosic and non-cellulosic (pectins and hemicelluloses) components of cell walls . Required for the formation of arabinogalactan proteins which contribute to the strengthening of cell walls . Possesses low glycosyltransferase activity .
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 45170
Sequence Length: 399
Subcellular Location: Membrane
EC: 2.4.-.-
|
Q9H165 | MSRRKQGKPQHLSKREFSPEPLEAILTDDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKRKQCNGSLCLEKAVDKPPSPSPIEMKKASNPVEVGIQVTPEDDDCLSTSSRGICPKQEHIADKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGICKDEPSSYTCTTCKQPFTSAWFLLQHAQNTHGLRIYLESEHGSPLTPRVGIPSGLGAECPSQPPLHGIHIADNNPFNLLRIPGSVSREASGLAEGRFPPTPPLFSPPPRHHLDPHRIERLGAEEMALATHHPSAFDRVLRLNPMAMEPPAMDFSRRLRELAGNTSSPPLSPGRPSPMQRLLQPFQPGSKPPFLATPPLPPLQSAPPPSQPPVKSKSCEFCGKTFKFQSNLVVHRRSHTGEKPYKCNLCDHACTQASKLKRHMKTHMHKSSPMTVKSDDGLSTASSPEPGTSDLVGSASSALKSVVAKFKSENDPNLIPENGDEEEEEDDEEEEEEEEEEEEELTESERVDYGFGLSLEAARHHENSSRGAVVGVGDESRALPDVMQGMVLSSMQHFSEAFHQVLGEKHKRGHLAEAEGHRDTCDEDSVAGESDRIDDGTVNGRGCSPGESASGGLSKKLLLGSPSSLSPFSKRIKLEKEFDLPPAAMPNTENVYSQWLAGYAASRQLKDPFLSFGDSRQSPFASSSEHSSENGSLRFSTPPGELDGGISGRSGTGSGGSTPHISGPGPGRPSSKEGRRSDTCEYCGKVFKNCSNLTVHRRSHTGERPYKCELCNYACAQSSKLTRHMKTHGQVGKDVYKCEICKMPFSVYSTLEKHMKKWHSDRVLNNDIKTE | Function: Transcription factor . Associated with the BAF SWI/SNF chromatin remodeling complex . Binds to the 5'-TGACCA-3' sequence motif in regulatory regions of target genes, including a distal promoter of the HBG1 hemoglobin subunit gamma-1 gene . Involved in regulation of the developmental switch from gamma- to beta-globin, probably via direct repression of HBG1; hence indirectly repressing fetal hemoglobin (HbF) level . Involved in brain development . May play a role in hematopoiesis (By similarity). Essential factor in lymphopoiesis required for B-cell formation in fetal liver (By similarity). May function as a modulator of the transcriptional repression activity of NR2F2 (By similarity).
PTM: Sumoylated with SUMO1.
Sequence Mass (Da): 91197
Sequence Length: 835
Domain: The N-terminus is involved in protein dimerization and in transactivation of transcription.
Subcellular Location: Cytoplasm
|
Q9QYE3 | MSRRKQGKPQHLSKREFSPEPLEAILTDDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKRKQCNGSLCLEKGVDKPPSPSPIEMKKASNPVEVGIQVTPEDDDCLSTSSRGICPKQEHIADKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGICKDEPSSYTCTTCKQPFTSAWFLLQHAQNTHGLRIYLESEHGSPLTPRVGIPSGLGAECPSQPPLHGIHIADNNPFNLLRIPGSVSREASGLAEGRFPPTPPLFSPPPRHHLDPHRIERLGAEEMALATHHPSAFDRVLRLNPMAMEPPAMDFSRRLRELAGNTSSPPLSPGRPSPMQRLLQPFQPGSKPPFLATPPLPPLQSAPPPSQPPVKSKSCEFCGKTFKFQSNLVVHRRSHTGEKPYKCNLCDHACTQASKLKRHMKTHMHKSSPMTVKSDDGLSTASSPEPGTSDLVGSASSALKSVVAKFKSENDPNLIPENGDEEEEEDDEEEEEEEEEEEEELTESERVDYGFGLSLEAARHHENSSRGAVVGVGDEGRALPDVMQGMVLSSMQHFSEAFHQVLGEKHKRSHLAEAEGHRDTCDEDSVAGESDRIDDGTVNGRGCSPGESASGGLSKKLLLGSPSSLSPFSKRIKLEKEFDLPPAAMPNTENVYSQWLAGYAASRQLKDPFLTFGDSRQSPFASSSEHSSENGSLRFSTPPGELDGGISGRSGTGSGGSTPHISGPGPGRPSSKEGRRSDTCPSHTPVRRSTPRAQDVWQFSDGSSRTLKF | Function: Transcription factor (By similarity). Associated with the BAF SWI/SNF chromatin remodeling complex . Binds to the 5'-TGACCA-3' sequence motif in regulatory regions of target genes (By similarity). May play a role in hematopoiesis . Essential factor in lymphopoiesis, required for B-cell formation in fetal liver . May function as a modulator of the transcriptional repression activity of NR2F2 .
PTM: Sumoylated with SUMO1.
Sequence Mass (Da): 83855
Sequence Length: 773
Domain: The N-terminus is involved in protein dimerization and in transactivation of transcription.
Subcellular Location: Cytoplasm
|
Q99PV8 | MSRRKQGNPQHLSQRELITPEADHVEATILEEDEGLEIEEPSSLGLMVGGPDPDLLTCGQCQMNFPLGDILVFIEHKKKQCGGLGPCYDKVLDKSSPPPSSRSELRRVSEPVEIGIQVTPDEDDHLLSPTKGICPKQENIAGPCRPAQLPSMAPIAASSSHPPTSVITSPLRALGVLPPCFPLPCCGARPISGDGTQGEGQMEAPFGCQCELSGKDEPSSYICTTCKQPFNSAWFLLQHAQNTHGFRIYLEPGPASTSLTPRLTIPPPLGPETVAQSPLMNFLGDSNPFNLLRMTGPILRDHPGFGEGRLPGTPPLFSPPPRHHLDPHRLSAEEMGLVAQHPSAFDRVMRLNPMAIDSPAMDFSRRLRELAGNSSTPPPVSPGRGNPMHRLLNPFQPSPKSPFLSTPPLPPMPAGTPPPQPPAKSKSCEFCGKTFKFQSNLIVHRRSHTGEKPYKCQLCDHACSQASKLKRHMKTHMHKAGSLAGRSDDGLSAASSPEPGTSELPGDLKAADGDFRHHESDPSLGPEPEDDEDEEEEEEELLLENESRPESSFSMDSELGRGRENGGGVPPGVAGAGAAAAALADEKALALGKVMEDAGLGALPQYGEKRGAFLKRAGDTGDAGAVGCGDAGAPGAVNGRGGAFAPGAEPFPALFPRKPAPLPSPGLGGPALHAAKRIKVEKDLELPPAALIPSENVYSQWLVGYAASRHFMKDPFLGFTDARQSPFATSSEHSSENGSLRFSTPPGDLLDGGLSGRSGTASGGSTPHLGGPGPGRPSSKEGRRSDTCEYCGKVFKNCSNLTVHRRSHTGERPYKCELCNYACAQSSKLTRHMKTHGQIGKEVYRCDICQMPFSVYSTLEKHMKKWHGEHLLTNDVKIEQAERS | Function: Key regulator of both differentiation and survival of T-lymphocytes during thymocyte development in mammals . Essential in controlling the responsiveness of hematopoietic stem cells to chemotactic signals by modulating the expression of receptors CCR7 and CCR9, which direct the movement of progenitor cells from the bone marrow to the thymus (By similarity). Is a regulator of IL2 promoter and enhances IL2 expression in activated CD4(+) T-lymphocytes . Tumor-suppressor protein involved in T-cell lymphomas. May function on the P53-signaling pathway. Repress transcription through direct, TFCOUP2-independent binding to a GC-rich response element.
PTM: Sumoylated with SUMO1.
Sequence Mass (Da): 94566
Sequence Length: 884
Subcellular Location: Nucleus
|
P27140 | MSTAPLSGFFLTSLSPSQSSLQKLSLRTSSTVACLPPASSSSSSSSSSSSRSVPTLIRNEPVFAAPAPIIAPYWSEEMGTEAYDEAIEALKKLLIEKEELKTVAAAKVEQITAALQTGTSSDKKAFDPVETIKQGFIKFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKVKYGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFPLDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGAFELWGLEFGLSETSSVKDVATILHWKL | Function: Reversible hydration of carbon dioxide. Required for photosynthesis in cotyledons. Binds salicylic acid. Together with BCA4, involved in the CO(2) signaling pathway which controls gas-exchange between plants and the atmosphere by modulating stomatal development and movements. Promotes water use efficiency.
PTM: S-nitrosylation at Cys-280 is up-regulated during nitrosative burst and suppresses both binding of salicylic acid and carbonic anhydrase activity. S-nitrosylated in response to an avirulent but not to a virulent bacterial strain.
Location Topology: Peripheral membrane protein
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 37450
Sequence Length: 347
Subcellular Location: Plastid
EC: 4.2.1.1
|
Q22460 | MNKILRGVIQFRNTIRKDLVKQFEEIKNNPSPTAVMFTCMDSRMLPTRFTQSQVGDMFVVRNAGNMIPDAPNYGAFSEVSVNTEPAALELAVKRGGIRHIVVCGHSDCKAINTLYGLHQCPKNFDVTSPMDHWVRRNGFASVKRLNERLHRGPSSMKFESEVAPSQSFDAIIDPMDTLAMEDKLSQINVLQQLINICSHEFLKEYLESGRLHIHGMWFDIYKGEDYLFSKDKKRFVVIDEKTVTDLLAELNARYPVPEDQDGPVAFAKSN | Cofactor: Binds 1 zinc ion per subunit.
Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 30686
Sequence Length: 270
EC: 4.2.1.1
|
O14370 | MSLMFLRRAGNIKGRNIRFALQRGSVGYSQQSSEACKNFLNTTQLRTMVQTAALHGPKPMDSSHIKVTNVKELKPLPEWKSLKFGENFTDHMLIMKWNREKGWSTPEIVPFGKLCFHPASSVFHYGFECFEGMKAFRDEKGVPRLFRPIKNAERMLSTGTRISLPSFDPAELAEIIRKFVAHENRWVPDQRGYSLYIRPTFIGTDEALGVHHCDNAMLYVIASPVGPYYSSGFKAVKLCCSEESVRAWPGGTGHYKLGGNYAPSVLPQKEAAKKGYAQILWLYGDEDYITEVGTMNCFTVWINKNGEKEIITAPLDGMILPGVTRDSILEICRERLAPKGWKITEGKYSMKEVAQASKEGRLLEVFGAGTAALVSPVKAINYKGTEYEIPMPEGQEAGPITSEISKWILDIQYGKEPNNPWSVPALP | Function: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
Catalytic Activity: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate
Sequence Mass (Da): 47855
Sequence Length: 427
Subcellular Location: Mitochondrion
EC: 2.6.1.42
|
Q9F714 | MSLVLAVYGKGGIGKSTTSANISAALALKGAKVLQIGCDPKHDSTFPITGKLQKTVIEALEEVDFHHEELSPEDIVETGFAGIDGLEAGGPPAGSGCGGYVVGESVTLLQEMGVYDKYDVILFDVLGDVVCGGFSAPLNYADYAVIIATNDFDSIFAANRLCMAIQQKSVRYKVQLAGIVANRVDYTKGGGTNMLDQFAEQVGTRLLAKVPYHELIRKSRFAGKTLFAMDPNEPELAECLAPYNEIADQILSEKPIASVPKPIGDREIFDIVGGWQ | Cofactor: Binds 1 [4Fe-4S] cluster per dimer.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.
Catalytic Activity: 2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 29494
Sequence Length: 276
Pathway: Porphyrin-containing compound metabolism; bacteriochlorophyll biosynthesis (light-independent).
EC: 1.3.7.7
|
Q7ZV60 | MTLSDFIGALKDNPYFGAGFGLVGVGTALAVARKGAQVGMIFFRRHYMITLEVPSKDKSYHWLLSWITKHAKHTQHLSVETSYMQHESGKVHTQFDFHPSPGNHIIWYGRKWIRVERVREKQMMDLHTGTPWESVTFTALGRDRQTFFNILQEARELALKQEEGRTVMYTAMGAEWRPFGFPRRRRPLSSVVLESGVAERIVDDVKEFIGNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELGYSICLMSLSDRSLSDDRLNHLLSVAPQQSIILLEDVDAAFVSRELLPTENPLAYQGMGRLTFSGLLNALDGVASSEARIVFMTTNFIERLDPALVRPGRVDLKQYVGHCSHWQLTQMFRRFYPQESAAEADHFSEQALAAHTDLSAAQVQGHFMLYKTDPAGAIKNIAEIKD | Function: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 47492
Sequence Length: 420
Subcellular Location: Mitochondrion inner membrane
|
Q48230 | MNKNKNIGIILAGGVGSRMGLGYPKQFSKIAGKTALEHTLAIFQEHKEIDEIIIVSERTSYRRIEDIVSKLDFSKVNRIIFGGKERSDSTLSAITALQDEPENTKLIIHDAVRPLLATEIISECIAKLDKYNAVDVAIPAVDTIVHVNNDTQEIIKIPKRAEYYQGQTPQAFKLGTLKKAYDIYTQGGIEGTCDCSIVLKTLPEERVGIVSGSETNIKLTRPVDLFIADKLFQSRSHFSLRNITSIDRLYDMKDQVLVVIGGSYGIGAHIIDIAKKFGIKTYSLSRSNGVDVGDVKSIEKAFAEIYAKEHKIDHIVNTAAVLNHKTLVSMSYEEILTSINVNYTGMINAVITAYPYLKQTHGSFLGFTSSSYTRGRPFYAIYSSAKAAVVNLTQAISEEWLPDNIKINCVNPERTKTPMRTKAFGIEPEGTLLDAKTVAFASLVVLASRETGNIIDVVLKDEEYITNILADLYK | Function: Catalyzes the NADPH-dependent reduction of D-ribulose 5-phosphate to D-ribitol 5-phosphate and the further reaction of D-ribitol 5-phosphate with CTP to form CDP-ribitol.
Catalytic Activity: CTP + D-ribitol 5-phosphate + H(+) = CDP-L-ribitol + diphosphate
Sequence Mass (Da): 52467
Sequence Length: 474
Pathway: Capsule biogenesis; capsule polysaccharide biosynthesis.
|
Q9Y276 | MPLSDFILALKDNPYFGAGFGLVGVGTALALARKGVQLGLVAFRRHYMITLEVPARDRSYAWLLSWLTRHSTRTQHLSVETSYLQHESGRISTKFEFVPSPGNHFIWYRGKWIRVERSREMQMIDLQTGTPWESVTFTALGTDRKVFFNILEEARELALQQEEGKTVMYTAVGSEWRPFGYPRRRRPLNSVVLQQGLADRIVRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSLSDDRLNHLLSVAPQQSLVLLEDVDAAFLSRDLAVENPVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEYVGYCSHWQLTQMFQRFYPGQAPSLAENFAEHVLRATNQISPAQVQGYFMLYKNDPVGAIHNAESLRR | Function: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 47534
Sequence Length: 419
Subcellular Location: Mitochondrion inner membrane
|
Q9P6Q3 | MDNIGAADAATSSGISGLLSGNSFLGAGIGLMGFGAGLAILRRGLISGASLVKRRMLVSVEIPSKEKSYNAFLHWMSTVPKRYSNQLAVESNRQLKMPQNAREKPDKQVANRIFSLVPGPGKHYIKYKKCWIQVERERSNRLQDLTTGTPWETITLTTLSRDRGIFSELLLEAQKFMQSAQKNKTTIYTAWATEWKPFGHPRSKRMLSSVVLESNVKKMITDDVHDFLRNSQWYDTRGIPYRRGYLLYGPPGSGKTSFLYALAGELDYDICVLNLAEKGLTDDRLNHLLSNVPPKAVVLLEDVDSAFQGRERSGEVGFHANVTFSGLLNALDGVTSSDERIIFMTTNHPEKLDPALVRPGRVDVKAYLGNATPEQVREMFTRFYGHSPEMADDLSDIVCPKNTSMASLQGLFVMNKSSPADAVDMAKELPDNPPSTPFSFNVHRKSLSV | Function: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 49856
Sequence Length: 449
Subcellular Location: Mitochondrion inner membrane
|
P32839 | MSDKPIDIQYDKQATPNLSGVITPPTNETGNDSVREKLSKLVGDAMSNNPYFAAGGGLMILGTGLAVARSGIIKASRVLYRQMIVDLEIQSKDKSYAWFLTWMAKHPQRVSRHLSVRTNYIQHDNGSVSTKFSLVPGPGNHWIRYKGAFILIKRERSAKMIDIANGSPFETVTLTTLYRDKHLFDDILNEAKDIALKTTEGKTVIYTSFGPEWRKFGQPKAKRMLPSVILDSGIKEGILDDVYDFMKNGKWYSDRGIPYRRGYLLYGPPGSGKTSFIQALAGELDYNICILNLSENNLTDDRLNHLMNNMPERSILLLEDIDAAFNKRSQTGEQGFHSSVTFSGLLNALDGVTSSEETITFMTTNHPEKLDAAIMRPGRIDYKVFVGNATPYQVEKMFMKFYPGETDICKKFVNSVKELDITVSTAQLQGLFVMNKDAPHDALKMVSSLRNANHIF | Function: Essential for the expression of the Rieske iron-sulfur protein.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 51107
Sequence Length: 456
Subcellular Location: Mitochondrion inner membrane
|
P19449 | MSEVQSPVPAESRLDRFSNKILSLRGANYIVGALGLCALIAATTVTLSINEQLIVALVCVLVFFIVGRGKSRRTQIFLEVLSALVSLRYLTWRLTETLDFDTWIQGGLGVTLLMAELYALYMLFLSYFQTIQPLHRAPLPLPDNVDDWPTVDIFIPTYDEQLSIVRLTVLGALGIDWPPDKVNVYILDDGVRPEFEQFAKDCGALYIGRVDSSHAKAGNLNHAIKRTSGDYILILDCDHIPTRAFLQIAMGWMVADRKIALMQTPHHFYSPDPFQRNLAVGYRTPPEGNLFYGVIQDGNDFWDATFFCGSCAILRREAIESIGGFAVETVTEDAHTALRMQRRGWSTAYLRIPVASGLATERLTTHIGQRMRWARGMIQIFRVDNPMLGGGLKLGQRLCYLSAMTSFFFAIPRVIFLASPLAFLFFGQNIIAASPLAVLAYAIPHMFHSIATAAKVNKGWRYSFWSEVYETTMALFLVRVTIITLMFPSKGKFNVTEKGGVLEEEEFDLGATYPNIIFAGIMTLGLLIGLFELTFHFNQLAGIAKRAYLLNCIWAMISLIILLAAIAVGRETKQVRYNHRVEAHIPVTVYEAPVAGQPNTYHNATPGMTQDVSMGGVAVHMPWPDVSTGPVKTRIHAVLDGEEIDIPATMLRCKNGKAVFTWDNNDLDTERDIVRFVFGRADAWLQWNNYEDDRPLRSLWSLLLSIKALFRKKGKMMANSRPKRKPLALPVERREPTTIQSGQTQEGKISRAAS | Function: Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose in a processive way. The thick cellulosic mats generated by this enzyme probably provide a specialized protective environment to the bacterium. Binds c-di-GMP with a dissociation constant of 30 uM.
Catalytic Activity: [(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84443
Sequence Length: 754
Domain: There are two conserved domains in the globular part of the catalytic subunit: the N-terminal domain (domain A) contains the conserved DXD motif and is possibly involved in catalysis and substrate binding. The C-terminal domain (domain B) contains the QXXRW motif and is present only in processive glycosyl transferases. It could be involved in the processivity function of the enzyme, possibly required for holding the growing glycan chain in the active site.
Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.12
|
P37653 | MSILTRWLLIPPVNARLIGRYRDYRRHGASAFSATLGCFWMILAWIFIPLEHPRWQRIRAEHKNLYPHINASRPRPLDPVRYLIQTCWLLIGASRKETPKPRRRAFSGLQNIRGRYHQWMNELPERVSHKTQHLDEKKELGHLSAGARRLILGIIVTFSLILALICVTQPFNPLAQFIFLMLLWGVALIVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVSLVCGLILLFAETYAWIVLVLGYFQVVWPLNRQPVPLPKDMSLWPSVDIFVPTYNEDLNVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQNVGVKYIARTTHEHAKAGNINNALKYAKGEFVSIFDCDHVPTRSFLQMTMGWFLKEKQLAMMQTPHHFFSPDPFERNLGRFRKTPNEGTLFYGLVQDGNDMWDATFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLTGKGLKFAQRLCYVNAMFHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVLPHMIHASLTNSKIQGKYRHSFWSEIYETVLAWYIAPPTLVALINPHKGKFNVTAKGGLVEEEYVDWVISRPYIFLVLLNLVGVAVGIWRYFYGPPTEMLTVVVSMVWVFYNLIVLGGAVAVSVESKQVRRSHRVEMTMPAAIAREDGHLFSCTVQDFSDGGLGIKINGQAQILEGQKVNLLLKRGQQEYVFPTQVARVMGNEVGLKLMPLTTQQHIDFVQCTFARADTWALWQDSYPEDKPLESLLDILKLGFRGYRHLAEFAPSSVKGIFRVLTSLVSWVVSFIPRRPERSETAQPSDQALAQQ | Function: Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose, which is produced as an extracellular component for mechanical and chemical protection at the onset of the stationary phase, when the cells exhibit multicellular behavior (rdar morphotype). Coexpression of cellulose and thin aggregative fimbriae (curli fimbrae or fibers) leads to a hydrophobic network with tightly packed cells embedded in a highly inert matrix that confers cohesion, elasticity and tissue-like properties to colonies .
Catalytic Activity: [(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 99785
Sequence Length: 872
Domain: There are two conserved domains in the globular part of the protein: the N-terminal domain (domain A) contains the conserved DXD motif and is possibly involved in catalysis and substrate binding. The C-terminal domain (domain B) contains the QXXRW motif and is present only in processive glycosyl transferases. It could be involved in the processivity function of the enzyme, possibly required for holding the growing glycan chain in the active site.
Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.12
|
P58931 | MTDTTSSTPFVEGRAEQRLNGAIARFNRWPSAPRTVLVVASCVLGAMLLLGIISAPLDLYSQCLFAAVCFLAVLVLRKIPGRLAILALVVLSLVASLRYMFWRLTSTLGFETWVDMFFGYGLVAAEFYALIVLIFGYVQTAWPLRRTPVWLKTEPEEWPTVDVFIPTYNEALSIVKLTIFAAQAMDWPKDKLRVHVLDDGRRDDFREFCRKVGVNYIRRDNNFHAKAGNLNEALKVTDGEYIALFDADHVPTRSFLQVSLGWFLKDPKLAMLQTPHFFFSPDPFEKNLDTFRAVPNEGELFYGLVQDGNDLWNATFFCGSCAVIRREPLLEIGGVAVETVTEDAHTALKLNRLGYNTAYLAIPQAAGLATESLSRHINQRIRWARGMAQIFRTDNPLLGKGLKWGQRICYANAMLHFFYGLPRLVFLTAPLAYLIFGAEIFHASALMIVAYVLPHLVHSSLTNSRIQGRFRHSFWNEVYETVLAWYILPPVLVALVNPKAGGFNVTDKGGIIDKQFFDWKLARPYLVLLAVNLIGLGFGIHQLIWGDASTAVTVAINLTWTLYNLIITSAAVAVASEARQVRSEPRVSAKLPVSIICADGRVLDGTTQDFSQNGFGLMLSDGHSITQGERVQLVLSRNGQDSLFDARVVFSKGAQIGAQFEALSLRQQSELVRLTFSRADTWAASWGAGQPDTPLAALREVGSIGIGGLFTLGRATLHELRLALSRTPTKPLDTLMDKP | Function: Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose, which is produced as an extracellular component responsible for the structural integrity and rigidity of self-supporting mats characteristic of the 'wrinkly spreader' phenotype.
Catalytic Activity: [(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82169
Sequence Length: 739
Domain: There are two conserved domains in the globular part of the protein: the N-terminal domain (domain A) contains the conserved DXD motif and is possibly involved in catalysis and substrate binding. The C-terminal domain (domain B) contains the QXXRW motif and is present only in processive glycosyl transferases. It could be involved in the processivity function of the enzyme, possibly required for holding the growing glycan chain in the active site.
Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.12
|
Q93IN2 | MSALSRWLLIPPVSARLSERYQGYRRHGASPFSAALGCLWTILAWIVFPLEHPRWQRIRDGHKALYPHINAARPRPLDPARYLIQTLWLVMISSTKERHEPRWRSFARLKDVRGRYHQWMDTLPERVRQKTTHLEKEKELGHLSNGARRFILGVIVTFSLILALICITQPFNPLSQFIFLLLLWGVALLVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVSLVCGLILLFAETYAWIVLVLGYFQVVWPLNRQPVPLPKEMSQWPTVDIFVPTYNEDLNVVKNTIYASLGIDWPKDKLNIWILDDGGRESFRHFARHVGVHYIARTTHEHAKAGNINNALKHAKGEFVAIFDCDHVPTRSFLQMTMGWFLKEKQLAMMQTPHHFFSPDPFERNLGRFRKTPNEGTLFYGLVQDGNDMWDATFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLFGKGLKLAQRLCYLNAMFHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVIPHMVHASLTNSKIQGKYRHSFWSEIYETVLAWYIAPPTLVALINPHKGKFNVTAKGGLVEEKYVDWVISRPYIFLVLLNLLGVAAGVWRYYYGPENETLTVIVSLVWVFYNLVILGGAVAVSVESKQVRRAHRVEIAMPGAIAREDGHLFSCTVHDFSDGGLGIKINGQAQVLEGQKVNLLLKRGQQEYVFPTQVVRVTGNEVGLQLMPLTTKQHIDFVQCTFARADTWALWQDSFPEDKPLESLLDILKLGFRGYRHLAEFAPPSVKVIFRSLTALIAWIVSFIPRRPERQAAIQPSDRVMAQAQQ | Function: Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose, which is produced as an extracellular component for mechanical and chemical protection at the onset of the stationary phase, when the cells exhibit multicellular behavior (rdar morphotype). Coexpression of cellulose and thin aggregative fimbriae leads to a hydrophobic network with tightly packed cells embedded in a highly inert matrix.
Catalytic Activity: [(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 100044
Sequence Length: 874
Domain: There are two conserved domains in the globular part of the protein: the N-terminal domain (domain A) contains the conserved DXD motif and is possibly involved in catalysis and substrate binding. The C-terminal domain (domain B) contains the QXXRW motif and is present only in processive glycosyl transferases. It could be involved in the processivity function of the enzyme, possibly required for holding the growing glycan chain in the active site.
Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.12
|
P58932 | MPLVVPHAAMPEGRLMTAASRRSASPLPTLATWALWLLGALLLVFVVAVPMDVTQQLVFSGVLFAVALAVRNRGGRVVILMMMGMSLAVSCRYIWWRMTQTMGVGSAVDFILGLGLLGAELYAFVILVLGYFQVLWPLNRKPVPLPADQRLWPSVDVFIPTYNEPLSVVRTTVLAASVIDWPAGKITIHLLDDGRRDEFRAFCAEVGINYVTRTNNAHAKAGNINAALKKCSGDYVAIFDCDHIPTRSFLQVAMGWFLHDTKLALVQMPHYFFSPDPFERNLDTHGKVPNEGELFYGLLQDGNDQWNATFFCGSCAVIKRTALEEVGGVAVETVTEDAHTALKLQRRGYRTAYLAVPQAAGLATESLSGHVAQRIRWARGMAQIARIDNPLLGRGLKLSQRLCYLNAMLHFFYGVPRIIYLTAPLAYLFFGAHVIQASALMILAYALPHILQANLTNLRVQSRFRHLLWNEVYETTLAWYIFRPTLVALLNPKLGKFNVTPKGGLVARSYFDAQIAKPYLFLLLLNVVGMVAGVLRLIYVGGSGEQQTIWFNLAWTLYNMVLLGATIATASETRQVRSAHRVPLDVPVTLYLPDGDVLPSRSVNFSTGGMAIMLAQPQPIEPGLPVQIGLSHRGVEQTLPAVVRQDRDGQVSIQFTQMSMEQERWLVASTFARADIWLSQWGQHDRDAFWRSMGQVLEASARGFGRLGGHIVDSARQGFRPRRAVDLES | Function: Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose, which is produced as an extracellular component for mechanical and chemical protection (By similarity).
Catalytic Activity: [(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80915
Sequence Length: 729
Domain: There are two conserved domains in the globular part of the protein: the N-terminal domain (domain A) contains the conserved DXD motif and is possibly involved in catalysis and substrate binding. The C-terminal domain (domain B) contains the QXXRW motif and is present only in processive glycosyl transferases. It could be involved in the processivity function of the enzyme, possibly required for holding the growing glycan chain in the active site.
Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.12
|
P37716 | MKMVSLIALLVFATGAQAAPVASKAPAPQPAGSDLPPLPAAASQAATPAAASADQPATTAPAADAASASAADAVVDNAENAIAASDVATVHTYSLKELGAQSALKMQGAATLQGLQFGIPADQLVTSARLIVSGAMSPSLQPDTSAVTITLNEQFIGTLRPDPTHPTFGPLSFDINPIFFITGNRLNFSFASSSKGCTDPSNGLLWASVSEHSELQITTIPLPPRRQLSRLPQPFFDKNVKQKIVIPFVLAQTFDPEVLKATGILASWFGQQTDFRGVTFPVFSTIPQTGNAVVVGVADELPSALGRQAVNGPTLMEVANPSDPNGTVLLVTGRDRDEVITASKGIGFGSSALPTANRMDVAPIDVGARVAYDAPSFIPTNRPVRLGELVPDSALQAQGYAPGALSVPFRVSPDLYTWRDRPYKLNVRFRAPPGPIVDVSRSSLNVGINDTYLEAYPLREPDSTLDQILRRVGLGRGDDSVQKHTMPIPPYRVFGQNQLLFYFEMAAMAEPGCKPGPSTFHMSVDPDSTIDLSNSYHITRMPNLAFMASAGYPFTTYADLSRSAVVLPDHPNGMVVSAYLDLMGFMGATTWYPVSGVDVVSSDHVNDVADRNLIVLSTLANSGDVSQLLSKSSYQISDGRLHMGLRSTLSGVWNLFQDPMSGISNTAPTDVESTLTGGVAAMIEAESPLASGRTVLALLSGDGQGLNNLVQILAQRKNQAKIQGDLVLAHGDDLTSYRSSPLYTVGTVPLWLEPDWYMHNHPSRVIVVGLLGCILIVAVMVRALAKHALRRRRELQEERQRT | Function: Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 85382
Sequence Length: 802
Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular Location: Cell inner membrane
|
Q8N1M1 | MTVTYSSKVANATFFGFHRLLLKWRGSIYKLLYREFIVFAVLYTAISLVYRLLLTGVQKRYFEKLSIYCDRYAEQIPVTFVLGFYVTLVVNRWWNQFVNLPWPDRLMFLISSSVHGSDEHGRLLRRTLMRYVNLTSLLIFRSVSTAVYKRFPTMDHVVEAGFMTTDERKLFNHLKSPHLKYWVPFIWFGNLATKARNEGRIRDSVDLQSLMTEMNRYRSWCSLLFGYDWVGIPLVYTQVVTLAVYTFFFACLIGRQFLDPTKGYAGHDLDLYIPIFTLLQFFFYAGWLKVAEQLINPFGEDDDDFETNWCIDRNLQVSLLAVDEMHMSLPKMKKDIYWDDSAARPPYTLAAADYCIPSFLGSTVQMGLSGSDFPDEEWLWDYEKHGHRHSMIRRVKRFLSAHEHPSSPRRRSYRRQTSDSSMFLPRDDLSPARDLLDVPSRNPPRASPTWKKSCFPEGSPTLHFSMGELSTIRETSQTSTLQSLTPQSSVRTSPIKMPLVPEVLITAAEAPVPTSGGYHHDSATSILSSEFTGVQPSKTEQQQGPMGSILSPSEKETPPGGPSPQTVSASAEENIFNCEEDPGDTFLKRWSLPGFLGSSHTSLGNLSPDPMSSQPALLIDTETSSEISGINIVAGSRVSSDMLYLMENLDTKETDIIELNKETEESPK | Function: Forms calcium-sensitive chloride channels. Permeable to bicarbonate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76107
Sequence Length: 668
Subcellular Location: Cell membrane
|
Q8NFU0 | MTVSYTLKVAEARFGGFSGLLLRWRGSIYKLLYKEFLLFGALYAVLSITYRLLLTQEQRYVYAQVARYCNRSADLIPLSFVLGFYVTLVVNRWWSQYTSIPLPDQLMCVISASVHGVDQRGRLLRRTLIRYANLASVLVLRSVSTRVLKRFPTMEHVVDAGFMSQEERKKFESLKSDFNKYWVPCVWFTNLAAQARRDGRIRDDIALCLLLEELNKYRAKCSMLFHYDWISIPLVYTQVVTIAVYSFFALSLVGRQFVEPEAGAAKPQKLLKPGQEPAPALGDPDMYVPLTTLLQFFFYAGWLKVAEQIINPFGEDDDDFETNQLIDRNLQVSLLSVDEMYQNLPPAEKDQYWDEDQPQPPYTVATAAESLRPSFLGSTFNLRMSDDPEQSLQVEASPGSGRPAPAAQTPLLGRFLGVGAPSPAISLRNFGRVRGTPRPPHLLRFRAEEGGDPEAAARIEEESAESGDEALEP | Function: Forms calcium-sensitive chloride channels. Permeable to bicarbonate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53497
Sequence Length: 473
Subcellular Location: Cell membrane
|
P34319 | MTNNNDPKCVVIEEPDDVPVKPPKIFDFTDWPFEIPDIFKRKELSYNYNYDLATSKSLMIVRMIFKWRGSLWQAVYKELIVWICAYSLVSVIYRFALTRSQKDIFERFGEYCDARMGYLPLNFVLGFFCNIIIRRWLKLYTSLGNIDNIALFVSAYVRGTDDRARQIRRNIIRYCVISQCLVFRDIHVGVRRRFPTLEAVAQAGIMLPHELEKFNSIKSRYQKYWVSFNWALELLNVAKTEKSIDGDNARNAIAQEISKFRSALTTVSMYDWVPIPLMYPQLVNMAVHTYFFLCIFTRQFFISADAHNKTEVDLYIPFMTIIEFIFYMGWLKVAMELLNPFGEDADDFDCNLLIDRNLAIGLTSVDDAYDQLPEVKPDVFTGGSVKPLDSDDTRSLKYHFGSAAQMEEISYLKKEENKMIAAGKKPNKLKLWVKSVRRKRFETSATQPSFPIP | Function: Forms chloride channels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52830
Sequence Length: 453
Subcellular Location: Cell membrane
|
Q9M2J9 | MNPRREPRGGRSSLFDGIEEGGIRAASSYSHEINEHENERALEGLQDRVILLKRLSGDINEEVDTHNRMLDRMGNDMDSSRGFLSGTMDRFKTVFETKSSRRMLTLVASFVGLFLVIYYLTR | Function: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE associated with ER-derived vesicles (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 13973
Sequence Length: 122
Subcellular Location: Golgi apparatus membrane
|
Q94CG2 | MNFRRENRASRTSLFDGLDGLEEGRLRASSSYAHDERDNDEALENLQDRVSFLKRVTGDIHEEVENHNRLLDKVGNKMDSARGIMSGTINRFKLVFEKKSNRKSCKLIAYFVLLFLIMYYLIRLLNYIKG | Function: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE associated with ER-derived vesicles (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 15207
Sequence Length: 130
Subcellular Location: Golgi apparatus membrane
|
Q3MHP8 | MADWARAQSPGAVEEILDRENKRMADSLASKVTRLKSLALDIDRDAEDQNRYLDGMDSDFTSMTGLLTGSVKRFSTMARSGRDNRKLLCGVAVGLIVAFFILSYLLSRART | Function: Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 12320
Sequence Length: 111
Subcellular Location: Golgi apparatus membrane
|
O35153 | MADWTRAQSSGAVEDILDRENKRMADSLASKVTRLKSLALDIDRDTEDQNRYLDGMDSDFTSVTGLLTGSVKRFSTMARSGRDNRKLLCGMAVVLIVAFFILSYLLSRTRT | Function: Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 12428
Sequence Length: 111
Subcellular Location: Golgi apparatus membrane
|
Q5RBX2 | MADWARAQSPGAVEEILDRENKRMADNLASKVTRLKSLALDIDKDAEDQNRYLDGMDSDFTSMTGLLTGSVKRFSTMARSGRDNRKLLCGMAVGLIVAFFILSYFLSRART | Function: Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 12385
Sequence Length: 111
Subcellular Location: Golgi apparatus membrane
|
O35152 | MADWTRAQSSGAVEEIVDRENKRMADSLASKVTRLKSLALDIDRDTEDQNRYLDGMDSDFTSVTGLLTGSVKRFSTVARSGRDTRKLLCGMAVVLIVAFFILSYLFSRTRT | Function: Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 12417
Sequence Length: 111
Subcellular Location: Golgi apparatus membrane
|
Q95Y80 | MSEGSGDQSQQRPWASPRQQPIKGIVQPRVLPPFGKPTRHTNKLDYIMTTVLKEAGKHKHVWPFQKPVDAVALCIPLYHERVARPMDLKTIENRLKSTYYTCAQECIDDIETVFQNCYTFNGKEDDVTIMAQNVHEVIKKSLEQAPREEHDMDVYWGKNKKKPAKSDGGSKSSSSKKNDARGPSEAPSEAGSEVSSVTTASAAAPTVSESASVAAKPERKVAGKKTGKRKAESEDDEKPEPLRAKREVAVVKKEVHQPLLPSMKPCLKLLNDFSTKKYQEFAWPFNEPVDAEQLGLHDYHKIIKEPMDLKSMKAKMESGAYKEPSDFEHDVRLMLRNCFLYNPVGDPVHSFGLRFQEVFDRRWAELGDSSSRASSVAPQSAPIAPTPKVAKSSAPKEPKESRKEHKKETTFEASGAKSEDLMQINNALSMIREREEKLKAELAAAQAIKDKLTSVKNRREDNPNEPFPEKLINETRALCTTQVGQNASSSSASSAALRNGRSKKAASARLYGYEFDSDDEDNKMALTYEEKRNLSNLINNLPNNQLNTIISIIQRRERSALMQQQLDDSEVELDFESLGDMCLREMGAFIKTIPTLNGNGDDEKPKTSSNPTSSGATGSKGSSSLESKNGKKKKNFNMSESSDDETSNSRKRRKRESSESQSSSSSDDDSDDEDRPSIPRKSGQPPSTSREWNQSSAPPPRMGGMGGQPPMSRVPASSSTSVSAIGKNNAAASSNSYQAPKPAPVPAPTSSRPPAAPRPPSKPKKTGGASILDTLLPDTFGASPPQFFQSQPTTSATIRSPTESQPGNGEDEQTRIQRMRMEAKRARQKEDEGSVSLSNQMEMMAAFEFDNTY | Function: Required for the establishment and maintenance of stable cell fate in several lineages including V5.pa, T, Z1/Z4 and QR lineages probably by repressing the expression of cell fate determinants . Required to maintain non-distal tip cell (DTC) fate of somatic gonadal cells through the htz-1-mediated repression of transcription factor ceh-22. Regulates the subnuclear localization of histone variant htz-1 in somatic gonadal cells . Plays a role in the attenuation of the let-60/ras pathway, probably by preventing expression of activators of the pathway . Involved in adult locomotion. Acts together with the sumoylation pathway to prevent muscle myosin depletion in aging adults probably by preventing myoblast growth factor receptor egl-15 overexpression . May play a role in vulva development .
Sequence Mass (Da): 94086
Sequence Length: 853
Domain: The BROMO domain 2 is essential for the interaction with smo-1 and E2 enzyme ubc-9.
Subcellular Location: Nucleus
|
O15155 | MRRAGLGEGVPPGNYGNYGYANSGYSACEEENERLTESLRSKVTAIKSLSIEIGHEVKTQNKLLAEMDSQFDSTTGFLGKTMGKLKILSRGSQTKLLCYMMLFSLFVFFIIYWIIKLR | Function: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 13289
Sequence Length: 118
Subcellular Location: Endoplasmic reticulum membrane
|
Q62896 | MRRAGLGDGAPPGGYGNYGYANSGYNACEEENDRLTESLRSKVTAIKSLSIEIGHEVKNQNKLLAEMDSQFDSTTGFLGKTMGRLKILSRGSQTKLLCYMMLFSLFVFFVIYWIIKLR | Function: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 13230
Sequence Length: 118
Subcellular Location: Endoplasmic reticulum membrane
|
P0ABD4 | MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIGEDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 18495
Sequence Length: 158
EC: 1.16.3.1
|
P63698 | MQGDPDVLRLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRAESFDEMRHAEEITDRILLLDGLPNYQRIGSLRIGQTLREQFEADLAIEYDVLNRLKPGIVMCREKQDTTSAVLLEKIVADEEEHIDYLETQLELMDKLGEELYSAQCVSRPPT | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 18341
Sequence Length: 159
EC: 1.16.3.1
|
P43315 | MQGDPDVLRLLNEQLTSELTAINQYFLHSKMQENWGFTELAERTRVESFDEMRHAEAITDRILLLDGLPNYQRIGSLRVGQTLREQFEADLAIEYEVMSRLKPGIIMCREKQDSTSAVLLEKIVADEEEHIDYLETQLALMGQLGEELYSAQCVSRPPS | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex (By similarity). Probably plays a crucial role in the intracellular existence of this organism by functioning as a temporary depository for iron in iron deprivation.
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18263
Sequence Length: 159
Subcellular Location: Cytoplasm
EC: 1.16.3.1
|
Q9HWF9 | MQGHPEVIDYLNTLLTGELAARDQYFIHSRMYEDWGFSKLYERLNHEMEEETQHADALLRRILLLEGTPRMRPDDIHPGTTVPEMLEADLKLERHVRAALAKGIALCEQHKDFVSRDILKAQLADTEEDHAYWLEQQLGLIARMGLENYLQSQI | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 17940
Sequence Length: 154
EC: 1.16.3.1
|
P77930 | MQGHPDVINYLVTLLKGELAARDQYFIHSRMYEDWGLTKLYERINHEMEEETQHADALMRRILMLEGTPDMRADDLEVGSTVPEMIEADLKLEYKVRGALCKGIELCELHKDYISRDILRAQLADTEEDHTYWLEKQQGLIKAIGLENYLQSQM | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 18001
Sequence Length: 154
EC: 1.16.3.1
|
Q59738 | MKGDAKVIEFLNAALRSELTAISQYWVHFRLQEDWGLAKMAKKSREESIEEMGHADKIIARILFLEGHPNLQKLDPLRIGEGPRETLECDLAGEHDALKLYREARDYCAEVGDIVSKNIFESLITDEEGHVDFLETQISLYDRLGPQGFALLNAAPMDAAE | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 18173
Sequence Length: 161
EC: 1.16.3.1
|
O68926 | MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLTRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLGIGEDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIAKLGMQNYLQSQIKVTD | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 18355
Sequence Length: 158
EC: 1.16.3.1
|
P24602 | MKGKPAVLAQLHKLLRGELAARDQYFIHSRMYQDWGLEKLYSRIDHEMQDETAHASLLIERILFLEETPDLSQQDPIRVGKTVPEMLQYDLDYEYEVIANLKEAMAVCEQEQDYQSRDLLLKILADTEEDHAYWLEKQLGLIEKIGLQNYLQSQMS | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 18331
Sequence Length: 156
EC: 1.16.3.1
|
Q06002 | MYRRSYVFQTRKEQYERAEEAPRAAEPDRLAEARAAAPNLAALQGLGERVAAHVQRARALEQRHAVLRRQLDAFQRLDELAGPEDALARHVEGNRQRARDLAAERTRLERQGAEAQRALDEFRSKYENECECQLLLKEMLERLNKEADEALLRNLRLQIEAQFLQDDISAAKDRYKKNLLEIQTYVTILQQIIQTTPQAAAITSGMREEKLLTEREAAALQCQLEDGREMICLLQAQRTELQAQTAALEQAIRDAHECYDDEIQLYNEQIDTLRKEIEEAERSLERSSYDCRQLVVVQQTLRNELDRYHRIIENEGNRLSSAFIETPITLYTASHGASLSPRHGGKDLTRAVQDITAAKPRLKGLPKNLPRKKEMVAKDRADEILEETLLRGPEDMKPGRVVIKEEGESKLEPGDEEASPPTQEGAPEDVPDGGKISKAFEKLGKMIKEKVKGPKEPEPPADLYTKGRYVMVSGDGSFVDPGFCVFSVPAKGGVVVSKGDDSVPPDSGVEPSPQQPEPPLEEGQGPPQEKEDGLKEEGGPPEGKGEPPEGKGDSVKEEGGPPEGKGDGVKEEGGPPEGKGDGVKEEGGPPEGKGDGVKKEGEPPEGKGEGLKEEEGPLQKKEDGRPPTPHPADKGDEKNAKELKGLQGKQDDQKEEGARGPCPMVAPGPEGPSTPRSQGPQVILGGSEGHGARSGSRLARSPPRKLAYEKVEVMESIEKFSTESIQTYEETAVIVETMIEKTKANKKKLGEKGSSSA | Function: Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity).
PTM: Proteolytically cleaved during lens cell fiber differentiation with increased fragmentation as fiber cell age increases.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 83181
Sequence Length: 757
Subcellular Location: Cell membrane
|
Q06637 | MYRSSFLREVRKEKYERSDAYDELRGSPEFDSLAQAQGLENLQELNERFASYINRARVLEQRNTILRKQLETFQRMDELVGLDEAFAGQIEFNRQRMRELASDRAKLEREEKDAQRMLDEYHNKYRNEREYQQKLKETLERLNKEADEALLCNLELQIESQFLQDDINATKDRYKKNLMEIQTYVNILQQIIQTTPRVSPITTGISEEKLVAERRIPVLQSQLEEYKSILCQLQAQKYKLQTETTMLEQAIKNTQESYDDEIQLYNEQIENLRKGIEEAERTLEKYTTDCRQLVIYQQSLENELERYKRIIENEDSRLNSAIAGTPVTLFTQIYRPVQPQASRGRDITQAMQEIASVKPRQKALTKKLSRKKEIMSKDITDGLSPEKLYERTVEVFDQDQLEFRHEGSVTCEPGQEELELVEKEAVPEDVPDGAQISKAFDKLCNLVKEKIRVYKRPEAKVDSHPKGRYVLVTGEEGYEEPCFSSIPAGGGITVSTSNGKVTIGGDVEPIPELPEPSEPSEKEKRDICERRDEFETQDKLKEEEKEDLFEWGKIRGKIEQVTKYPDVSEPEAVPSPGLISPAEPGVLQETDHDREDKQGLLFREAGLPGSVSYEKVEVVESIEKFSDDRIQTYEETAMIVETMIEKTSKKKPGDKGS | Function: Required for the correct formation of lens intermediate filaments.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 76105
Sequence Length: 657
Subcellular Location: Cell membrane
|
Q12934 | MYRRSYVFQTRKEQYEHADEASRAAEPERPADEGWAGATSLAALQGLGERVAAHVQRARALEQRHAGLRRQLDAFQRLGELAGPEDALARQVESNRQRVRDLEAERARLERQGTEAQRALDEFRSKYENECECQLLLKEMLERLNKEADEALLHNLRLQLEAQFLQDDISAAKDRHKKNLLEVQTYISILQQIIHTTPPASIVTSGMREEKLLTEREVAALRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAHECYDDEIQLYNEQIETLRKEIEETERVLEKSSYDCRQLAVAQQTLKNELDRYHRIIEIEGNRLTSAFIETPIPLFTQSHGVSLSTGSGGKDLTRALQDITAAKPRQKALPKNVPRRKEIITKDKTNGALEDAPLKGLEDTKLVQVVLKEESESKFESESKEVSPLTQEGAPEDVPDGGQISKGFGKLYRKVKEKVRSPKEPETPTELYTKERHVLVTGDANYVDPRFYVSSITAKGGVAVSVAEDSVLYDGQVEPSPESPKPPLENGQVGLQEKEDGQPIDQQPIDKEIEPDGAELEGPEEKREGEERDEESRRPCAMVTPGAEEPSIPEPPKPAADQDGAEVLGTRSRSLPEKGPPKALAYKTVEVVESIEKISTESIQTYEETAVIVETMIGKTKSDKKKSGEKSS | Function: Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA . Involved in altering the calcium regulation of MIP water permeability .
PTM: Proteolytically cleaved during lens cell fiber differentiation with increased fragmentation as fiber cell age increases.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74544
Sequence Length: 665
Subcellular Location: Cell membrane
|
P77989 | MGRDVLNFNVDWLYIPEDLNDAYKFDFDESNFEVVSLPHANKTFPHHYFKEEDYRFVSWYRKHFKVDERYKGKKVYIHFEGVITVAKVYVNGEFVGEHKGGYTPFEFDITEYIKYGNFENLIAVQVDSREHKDIPPEGHLVDYMLFGGIYRNVWLKILNDTHIKDVYFVVDKLQDSVAEISITTTIAGKEISNGKILTEVINKEGVVCSSVVTDIKEMQKEIVQQIKMDNPLTWHPDHPYLYNVSVKLIAENEILDNYTFKTGIRTVEFRDDGKFYINGEPLKLRGLNRHQTFPYVGGAMPDRVQRKDADILKYELGLNYVRTSHYPQAVSFLDRCDEIGLLVFEEIPGWQHIGDENWKNIAKENLKEMILRDRNHPCIFMWGVRINESLDDHDFYKEMNEIAHKLDRSRPTGGVRYLRDSEKLEDVFTYNDFIYNLEGKIQLPNHKKYMVTEYMGHMYPTKSYDNLNRLITHARLHALIQDKQYGIPNMAGASGWCAFDYNTTSAFGSGDNICYHGVCDIFRLPKFAAHFYRSQADPHLYGPYVFIASYLIPSFEEENGDKLLVFSNCEEVELYINDKFVKRQMPNRVDFPSLPHPPFEFSMKECGINYMEVRVNNASITAIGLIDGKEVARHTLRPYGKPHKLILSCDDNEIMADGADCTRVVVSVVDENGSILPYANIPVSFEIEGEGKLIGENPLTLEAGRGAVYVKSTRKPGEIILKAKSHYVAEESNVSIKTKSIGY | Function: Beta-galactosidase.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 85765
Sequence Length: 743
EC: 3.2.1.23
|
P26257 | MRKIIPINNNWYFKADYEEGYEKVDDLRSFENVNLPHTNIELPYNYFDEKMYQIKSCYKYPLHISEKYRDKVIYIHFEGVMAYAQVYLNGLYIGEHKGGYTPFDIRIDEVYDWKKELNMLTVVVDSTERSDIPPKGGQIDYLTYGGIYREVSLGIYDDVFIKNIKVETHGIYDNEKSLNLIVHLENLNHQSGNVKFKVKINDKNGKEVFYKEFNTYLDAVKDVYSFNIENLKDIKLWDVDNPNLYEIKVGMKINNFSDEYDNKFGFREAVFKPDGFYLNGRKLKLRGLNRHQSYPYVGYAMPRRVQEKDAEILKNELHLNIVRTSHYPQSKHFLNKCDELGLLVFEEIPGWQYIGNSEWKKVAEQNLREMITRDWNHPSIILWGVRINESQDDDAFYKNMNKIAHEIDPTRQTGGVRYITNSSFLEDVYTFNDFIHDGINKPLRKQQEVTGLEHNVPYLVTEYNGHMYPTKRFDNEERQMEHCLRHLRIQNASYLDDSISGAIGWCAFDYNTHKDFGSGDRICYHGVMDMFRLPKFASYVYKSQVSPDIEPILEPVTFWARGERSIGGVIPLIIFTNCDYIELQYGNKTKIDNIYPNRDAYKGIPYPPIIIDYDIVKPEMIGAWGMVWEDLTLKGFYKGNKVIERKFSREPIPTYLYVVPDDTILSATQKDATRIVVKILDQYGNLLPFINEVIKIEIEGPAKLQGPNEVALIGGA | Function: Displays beta-galactosidase activity with the artificial chromogenic substrate o-nitrophenyl-beta-D-galactopyranoside (ONPG).
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 83781
Sequence Length: 716
EC: 3.2.1.23
|
P48982 | MLRTTLAPLVLALALALPAAAATPESWPTFGTQGTQFVRDGKPYQLLSGAIHFQRIPRAYWKDRLQKARALGLNTVETYVFWNLVEPQQGQFDFSGNNDVAAFVKEAAAQGLNVILRPGPYACAEWEAGGYPAWLFGKGNIRVRSRDPRFLAASQAYLDALAKQVQPLLNHNGGPIIAVQVENEYGSYADDHAYMADNRAMYVKAGFDKALLFTSDGADMLANGTLPDTLAVVNFAPGEAKSAFDKLIKFRPDQPRMVGEYWAGWFDHWGKPHAATDARQQAEEFEWILRQGHSANLYMFIGGTSFGFMNGANFQNNPSDHYAPQTTSYDYDAILDEAGHPTPKFALMRDAIARVTGVQPPALPAPITTTTLPATPLRESASLWDNLPTPIAIDTPQPMEQFGQDYGYILYRTTITGPRKGPLYLGDVRDVARVYVDQRPVGSVERRLQQVSLEVEIPAGQHTLDVLVENSGRINYGTRMADGRAGLVDPVLLDSQQLTGWQAFPLPMRTPDSIRGWTGKAVQGPAFHRGTLRIGTPTDTYLDMRAFGKGFAWANGVNLGRHWNIGPQTALYLRPSSARVTTRWWSSTWTMLHPSVRG | Function: Preferentially hydrolyzes beta(1->3) galactosyl linkages over beta(1->4) linkages.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 66086
Sequence Length: 598
EC: 3.2.1.23
|
A2RAL4 | MRFTSIEAVALTAVSLASADELAYSPPYYPSPWANGQGDWAEAYQRAVDIVSQMTLAEKVNLTTGTGWELELCVGQTGGVPRLGIPGMCAQDSPLGVRDSDYNSAFPAGVNVAATWDKNLAYLRGQAMGQEFSDKGADIQLGPAAGPLGRSPDGGRNWEGFSPDPALSGVLFAETIKGIQDAGVVATAKHYIAYEQEHFRQAPEAQGYGFNITESGSANLDDKTMHELYLWPFADAIRAGAGAVMCSYNQINNSYGCQNSYTLNKLLKAELGFQGFVMSDWAAHHAGVSGALAGLDMSMPGDVDYDSGTSYWGTNLTISVLNGTVPQWRVDDMAVRIMAAYYKVGRDRLWTPPNFSSWTRDEYGFKYYYVSEGPYEKVNQFVNVQRNHSELIRRIGADSTVLLKNDGALPLTGKERLVALIGEDAGSNPYGANGCSDRGCDNGTLAMGWGSGTANFPYLVTPEQAISNEVLKNKNGVFTATDNWAIDQIEALAKTASVSLVFVNADSGEGYINVDGNLGDRRNLTLWRNGDNVIKAAASNCNNTIVIIHSVGPVLVNEWYDNPNVTAILWGGLPGQESGNSLADVLYGRVNPGAKSPFTWGKTREAYQDYLYTEPNNGNGAPQEDFVEGVFIDYRGFDKRNETPIYEFGYGLSYTTFNYSNLQVEVLSAPAYEPASGETEAAPTFGEVGNASDYLYPDGLQRITKFIYPWLNSTDLEASSGDASYGQDASDYLPEGATDGSAQPILPAGGGAGGNPRLYDELIRVSVTIKNTGKVAGDEVPQLYVSLGGPNEPKIVLRQFERITLQPSKETQWSTTLTRRDLANWNVETQDWEITSYPKMVFAGSSSRKLPLRASLPTVH | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 93229
Sequence Length: 860
Pathway: Glycan metabolism; cellulose degradation.
Subcellular Location: Secreted
EC: 3.2.1.21
|
P42973 | MGNMPKDFLWGGALAAHQFEGGWNQGGKGPSVVDVMTAGAHGVPRKITDTIEENEFYPNHEAIDFYHRYKEDIALFAEMGLKCLRTSIGWSRIFPKGDEAEPNEAGLQFYDDVFDELLKHGIEPVITLSHFEMPLHLAREYGGFRNRKVVDFFVNFAEACFTRYKDKVKYWMTFNEINNQMDVNNPLFLWTNSGVVVGENENAKEVMYQTAHHELVASALAVAKGKDINPEFQIGAMVSHVPIYPFSSNPEDVMLAEEEMRQRYFFPDVQVRGYYPSYALKEFEREGYNITFEDGDDEILRNGTVDYLGFSYYMSTTVKSDVKNDNTGDIVNGGLPNGVENPYITSSDWGWAIDPTGLRYTLNRFYDRYQIPLFIVENGFGAVDTLEEDGKVHDPERIQYLKSHIEALKKAVTYDGVDLIGYTPWGIIDIVSFTTGEMKKRYGMIYVDRDNEGNGSMKRYKKDSFEWYKNVIQTNGEEL | Function: Catalyzes the hydrolysis of aryl-phospho-beta-D-glucosides such as 4-methylumbelliferyl-phospho-beta-D-glucopyranoside (MUG-P), phosphoarbutin and phosphosalicin. Plays a major role in the utilization of arbutin or salicin as the sole carbon source. BglA and BglH are the major proteins contributing to hydrolysis of MUG-P by extracts of late-exponential-phase or stationary-phase B.subtilis cells.
Catalytic Activity: 6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate
Sequence Mass (Da): 54841
Sequence Length: 479
EC: 3.2.1.86
|
Q46829 | MIVKKLTLPKDFLWGGAVAAHQVEGGWNKGGKGPSICDVLTGGAHGVPREITKEVLPGKYYPNHEAVDFYGHYKEDIKLFAEMGFKCFRTSIAWTRIFPKGDEAQPNEEGLKFYDDMFDELLKYNIEPVITLSHFEMPLHLVQQYGSWTNRKVVDFFVRFAEVVFERYKHKVKYWMTFNEINNQRNWRAPLFGYCCSGVVYTEHENPEETMYQVLHHQFVASALAVKAARRINPEMKVGCMLAMVPLYPYSCNPDDVMFAQESMRERYVFTDVQLRGYYPSYVLNEWERRGFNIKMEDGDLDVLREGTCDYLGFSYYMTNAVKAEGGTGDAISGFEGSVPNPYVKASDWGWQIDPVGLRYALCELYERYQRPLFIVENGFGAYDKVEEDGSINDDYRIDYLRAHIEEMKKAVTYDGVDLMGYTPWGCIDCVSFTTGQYSKRYGFIYVNKHDDGTGDMSRSRKKSFNWYKEVIASNGEKL | Function: Catalyzes the hydrolysis of phosphorylated beta-glucosides into glucose-6-phosphate (G-6-P) and aglycone. It has a high affinity for phosphorylated aromatic beta-glucosides (p-nitrophenyl-beta-glucoside, phenyl beta-glucoside, arbutin), with the exception of phosphorylated salicin, and a low affinity for phosphorylated beta-methyl-glucoside. Apparently, it has only a very limited role in the utilization of external beta-glucosides.
Catalytic Activity: 6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate
Sequence Mass (Da): 55361
Sequence Length: 479
EC: 3.2.1.86
|
Q5B5S8 | MKLGWLEAAALTAASVASAQVKQDDLPVSPPYYPSPWSNGEGEWAEAYNRAVQIVSQMTLDEKVNLTTGTGMSEKCVGQTGSVPRLGINSICLQDGPLGIRFTDYNSAFPAGVNVAATWDRQLAYIRGHAMGQEFSDKGIDVQLGPAAGPLGRFPDGGRNWEGFSPDPVLSGVLFAETIKGIQDAGVIATAKHYLLNEQEHFRQVPEANGYGYNITETLSENVDDKTLHELYLWPFADAVRAGVGAIMCSYQHLNNTQACQNSHLLNKLLKAELGFQGFVMSDWSATHSGVGSALAGMDMTMPGDIAFNDGLSYYGPNLTISVLNGTVPQWRVDDMAVRVMAAFYKVGRDRLATPPNFSSWTRAEKGYEHASIDGGAYGTVNEFVDVQQDHASLIRRVGADSIVLLKNEGSLPLTGKERNVAILGEDAGSNPYGANGCDDRGCAQGTLAMGWGSGTANFPYLVTPEQAIQQEVLKGRGNVFAVTDNWALDKVNKTASESTVSLVFVNAGAGEGFISVDGNEGDRKNLTLWKNGENLIKAAASNCNNTIVVIHSVGAVLVDQFYEHPNVTAILWAGLPGQESGNSLVDVLYGRVNPNGKSPFTWGKTREAYGAPLLTEANNGNGAPQTDHTEGVFIDYRHFDRTNQTPIYEFGHGLSYTTFKYSNLTVQKLNAPAYSPASGQTKAAPTFGTIGEAEDYVFPDSITRVREFIYPWINSTDLKESSGDPNYGWDDEDYIPEGAKDGSPQDVLPSGGGAGGNPRLYDDLFRITAIIKNTGPVAGTEVPQLYVSLGGPNEPKVVLRGFDKLVIQPGEERVFTTTLTRRDLSNWDMEKDDWVITSYPKKVFVGSSSRKLPLRASLPAVQ | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 93242
Sequence Length: 863
Pathway: Glycan metabolism; cellulose degradation.
Subcellular Location: Secreted
EC: 3.2.1.21
|
P22073 | MTIFQFPQDFMWGTATAAYQIEGAYQEDGRGLSIWDTFAHTPGKVFNGDNGNVACDSYHRYEEDIRLMKELGIRTYRFSVSWPRIFPNGDGEVNQEGLDYYHRVVDLLNDNGIEPFCTLYHWDLPQALQDAGGWGNRRTIQAFVQFAETMFREFHGKIQHWLTFNEPWCIAFLSNMLGVHAPGLTNLQTAIDVGHHLLVAHGLSVRRFRELGTSGQIGIAPNVSWAVPYSTSEEDKAACARTISLHSDWFLQPIYQGSYPQFLVDWFAEQGATVPIQDGDMDIIGEPIDMIGINYYSMSVNRFNPEAGFLQSEEINMGLPVTDIGWPVESRGLYEVLHYLQKYGNIDIYITENGACINDEVVNGKVQDDRRISYMQQHLVQVHRTIHDGLHVKGYMAWSLLDNFEWAEGYNMRFGMIHVDFRTQVRTPKESYYWYRNVVSNNWLETRR | Function: BglA is intracellular and cleaves cellobiose probably through inorganic phosphate mediated hydrolysis.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 51649
Sequence Length: 448
EC: 3.2.1.21
|
B9K7M5 | MKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGDVACDHYNRWKEDIEIIEKIGAKAYRFSISWPRILPEGTGKVNQKGLDFYNRIIDTLLEKNITPFITIYHWDLPFSLQLKGGWANRDIADWFAEYSRVLFENFGDRVKHWITLNEPWVVAIVGHLYGVHAPGMKDIYVAFHTVHNLLRAHAKSVKVFRETVKDGKIGIVFNNGYFEPASEREEDIRAARFMHQFNNYPLFLNPIYRGEYPDLVLEFAREYLPRNYEDDMEEIKQEIDFVGLNYYSGHMVKYDPNSPARVSFVERNLPKTAMGWEIVPEGIYWILKGVKEEYNPQEVYITENGAAFDDVVSEGGKVHDQNRIDYLRAHIEQVWRAIQDGVPLKGYFVWSLLDNFEWAEGYSKRFGIVYVDYNTQKRIIKDSGYWYSNVIKNNGLTD | Function: Broad substrate specificity glycosidase. Releases glucose from soluble glucooligomers, with a preference for longer oligomers; acts more readily on cellotetraose than on cellobiose. Displays similar activities towards the disaccharides lactose and cellobiose. Is also able to hydrolyze various aryl-beta-glycosides in vitro.
Catalytic Activity: Hydrolysis of (1->4)-linkages in (1->4)-beta-D-glucans, to remove successive glucose units.
Sequence Mass (Da): 51535
Sequence Length: 444
Pathway: Glycan metabolism; cellulose degradation.
EC: 3.2.1.74
|
P14002 | MAVDIKKIIKQMTLEEKAGLCSGLDFWHTKPVERLGIPSIMMTDGPHGLRKQREDAEIADINNSVPATCFPSAAGLACSWDRELVERVGAALGEECQAENVSILLGPGANIKRSPLCGRNFEYFSEDPYLSSELAASHIKGVQSQGVGACLKHFAANNQEHRRMTVDTIVDERTLREIYFASFENAVKKARPWVVMCAYNKLNGEYCSENRYLLTEVLKNEWMHDGFVVSDWGAVNDRVSGLDAGLDLEMPTSHGITDKKIVEAVKSGKLSENILNRAVERILKVIFMALENKKENAQYDKDAHHRLARQAAAESMVLLKNEDDVLPLKKSGTIALIGAFVKKPRYQGSGSSHITPTRLDDIYEEIKKAGGDKVNLVYSEGYRLENDGIDEELINEAKKAASSSDVAVVFAGLPDEYESEGFDRTHMSIPENQNRLIEAVAEVQSNIVVVLLNGSPVEMPWIDKVKSVLEAYLGGQALGGALADVLFGEVNPSGKLAETFPVKLSHNPSYLNFPGEDDRVEYKEGLFVGYRYYDTKGIEPLFPFGHGLSYTKFEYSDISVDKKDVSDNSIINVSVKVKNVGKMAGKEIVQLYVKDVKSSVRRPEKELKGFEKVFLNPGEEKTVTFTLDKRAFAYYNTQIKDWHVESGEFLILIGRSSRDIVLKESVRVNSTVKIRKRFTVNSAVEDVMSDSSAAAVLGPVLKEITDALQIDMDNAHDMMAANIKNMPLRSLVGYSQGRLSEEMLEELVDKINNVE | Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 83900
Sequence Length: 755
Pathway: Glycan metabolism; cellulose degradation.
EC: 3.2.1.21
|
P11988 | MKAFPETFLWGGATAANQVEGAWQEDGKGISTSDLQPHGVMGKMEPRILGKENIKDVAIDFYHRYPEDIALFAEMGFTCLRISIAWARIFPQGDEVEPNEAGLAFYDRLFDEMAQAGIKPLVTLSHYEMPYGLVKNYGGWANRAVIDHFEHYARTVFTRYQHKVALWLTFNEINMSLHAPFTGVGLAEESGEAEVYQAIHHQLVASARAVKACHSLLPEAKIGNMLLGGLVYPLTCQPQDMLQAMEENRRWMFFGDVQARGQYPGYMQRFFRDHNITIEMTESDAEDLKHTVDFISFSYYMTGCVSHDESINKNAQGNILNMIPNPHLKSSEWGWQIDPVGLRVLLNTLWDRYQKPLFIVENGLGAKDSVEADGSIQDDYRIAYLNDHLVQVNEAIADGVDIMGYTSWGPIDLVSASHSQMSKRYGFIYVDRDDNGEGSLTRTRKKSFGWYAEVIKTRGLSLKKITIKAP | Function: Catalyzes the hydrolysis of phosphorylated beta-glucosides into glucose-6-phosphate (G-6-P) and aglycone. It has a high affinity for phosphorylated aromatic beta-glucosides (p-nitrophenyl-beta-glucoside, phenyl beta-glucoside, arbutin and phosphorylated salicin), and a low affinity for phosphorylated beta-methyl-glucoside.
Catalytic Activity: 6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate
Sequence Mass (Da): 53161
Sequence Length: 470
EC: 3.2.1.86
|
Q5BFG8 | MSFQKVDPAQIESVLSKLTLEEKISLLAGKNFWETQDYPEKGVPPVKTSDGPNGARGATFKGGVTAACFPASSLLAATWDLDAAKHIGEALADETRSKGARVLLAPTVCIHRHPLGGRNFESFSEDPFLAGKLAAQYIKGLQGNGVAATIKHYAANEQETCRFTVNEHITERALREIYLKPFEIAIKESNPLAVMTAYNIVNGTHADSNNFLLRDVLRGEWGWKGLVMSDWGGTNSTADALNAGLDLEMPGPTRWRKVDEVLAVVKSGAVLEETIDERARNVLELLAKLNCFENPTIPEEKAINRPEHQKLIRSVGSQGLVLLKNEGDVLPLRKEILTNKKVALLGFAREALIHGGGSASVNAHYRVTPEEGLRAALGDTVEFEYAKGAHTFRQLPLMSDNVVNLEGQPGWTLDFFADEEPNGEPGSSISSEQPSYIPLFVKESWGSVRASAHFTPTQSGKHYFGMSGLGRSKLLIDGEVIYEQKLNCPDSMGFLLGGVEEPEIQYSFEAGKTYAVEVVSVKPTSKGGLALLDGFIGFRLGFMTEEEHNRDLLSEAVDVAKRSDIAIVFTGHTPDWETEGQDQISFHLPSNGSQDRLVAAVGAANPNTVVVNCTGVAVAMPWLDKVKAVVQAWFPGQEAGNAIADVLTGAVNPSGRLPVSFPRAIEDAPAHGNFPGDYTDGKDNRRHLEVTYKEGVFVGYRHYDLSEANRAKVLFPFGYGLSYTTFTHANHKASATSRNTVEVAVDVTNVGTCAGADVVQVYAGAKLAVPENPVKELVGFAKVHLKPGETKTANITFEVRQLTHFTERSGKWELESGDYEISIGQSVRDITGKVEIGLEAQNYKP | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 91790
Sequence Length: 845
Pathway: Glycan metabolism; cellulose degradation.
EC: 3.2.1.21
|
P38645 | MTESAMTSRAGRGRGADLVAAVVQGHAAASDAAGDLSFPDGFIWGAATAAYQIEGAWREDGRGLWDVFSHTPGKVASGHTGDIACDHYHRYADDVRLMAGLGDRVYRFSVAWPRIVPDGSGPVNPAGLDFYDRLVDELLGHGITPYPTLYHWDLPQTLEDRGGWAARDTAYRFAEYALAVHRRLGDRVRCWITLNEPWVAAFLATHRGAPGAADVPRFRAVHHLLLGHGLGLRLRSAGAGQLGLTLSLSPVIEARPGVRGGGRRVDALANRQFLDPALRGRYPEEVLKIMAGHARLGHPGRDLETIHQPVDLLGVNYYSHVRLAAEGEPANRLPGSEGIRFERPTAVTAWPGDRPDGLRTLLLRLSRDYPGVGLIITENGAAFDDRADGDRVHDPERIRYLTATLRAVHDAIMAGADLRGYFVWSVLDNFEWAYGYHKRGIVYVDYTTMRRIPRESALWYRDVVRRNGLRNGE | Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 52228
Sequence Length: 473
Subcellular Location: Cytoplasm
EC: 3.2.1.21
|
Q5AWD4 | MLTSWGKTGFVLALALGGRAAENVITSDTFFYGESPPVYPSPEGTGAGDWASAYTKARAFVAQLSDDEKIQLTAGVSSNTACSGFIQPIDRLGFPGICMSDAGNGLRGTDYVNGWSSGISVGASWNRDLAHSRGAYMGQEYRKKGVNMILGPVVGPLGRVALGGRNWEGYAADPYLSGVLVSESVKGLQSQKVATSVKHFIANEQETNRNPTTDSERNVVQSVSSNIDDKTMHELYLWPFQDAVLAGATNLMCSYNRVNNSYACQNSKLLNGVLKTELGFQGYVVTDWGAQHAGIASANAGLDVVMPRSSTWNSNLTTAIANGTMEASRLDDMITRLMATWYYLDQDTEFPSPGVGMPSSPSAAHQAVIATSPEAKPILLQSAIESHVLVKNTDGALPLKSPKLISVFGYDAYAPLTYDLGNNFDFSSTRVRSDLYKNGTLYVGGGSGLNSPAYIDAPIDAIKRRAYEDGSSVLWDFTSENPSVDYTSDVCLVFINAYATEGYDRQALSDTHSDSVVENIAGNCSNTIVVVHNAGIRTAEAWVDHANVTAIIYAHLPGQDIGRALVRLLYGESNFSGRLPYTVAKNSSDYGSLLEPSQPEGKYQYFPQSDFSEGVYIDYRAFDKDGIVPQYAFGYGLSYTTFEYSDLKISKNSDGVPSIYPAKASILPGGNPHLFDELVTVTAKIRNTGNVDGQEVAQLYVGIPDGPVRQLRGFDKVLIESGSSATVTFSLTRRDLSTWDANAQEWSLQRGTYKIFVGRDSRDLPLEETLVF | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 83526
Sequence Length: 772
Pathway: Glycan metabolism; cellulose degradation.
Subcellular Location: Secreted
EC: 3.2.1.21
|
Q5B681 | MHSNILPVLTSVATLLGLVQGQSQQPYRDWAKAYEAAETLVLPWTLEQQANISVRDGTAPGFVPFEPSDGVRSVQGSGKDYDNPAMRTSSNLDDRTLHELYLWPWIDGVANGLGSVMCVMNRVNGIIGCENDHIMNGILKNETGFRGFIVPDVTAPVDKAAGLLGGLGWNSGYSVSEIMAAVKNGSIPESVMTEHALRIVATQLNLLQPPEEYAFPVETADLNVRDPSSKDFIRRAGSESIVLLKNKNNTLPLRSPMSLGIFGKDAANLATGPTPQSDFSNFAGDTYDGHLITGGGSYSPAPYVVSPLDALTARAADGQGFGYKYILSDNWTVTPSESTGEGFFQTSGVSVSQYARESEHCLVFINAFGKEGSDRRTLADETGDKLVNDVADYCGSTIVIINNAGVRLVDAWIEHENVTVFTDLIPCSNQVHTNMFCFPGCPERRRSRQESGHAIVDVLFGDVNPSAKLVYTIAKSKDDYNGQICECCECDYTEGLYIDYRHFDQAGIEPRFEFGFGLCFKSDGRANIAAYTTFTHSDLTINPSTDITTLQPYATGPITEGGPSDLFEQILTISASISNTGGVAGAEVAQLYLSFPDAAKAPVRQLRGFEKVYLEPGETKFVSFPIQRRDLSIWDEQTSKWKIVGGKYGVVLGRSSRDFTVEETLELLTI | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 72928
Sequence Length: 670
Pathway: Glycan metabolism; cellulose degradation.
Subcellular Location: Secreted
EC: 3.2.1.21
|
Q5BG51 | MTVLAPWALWEKTKDVMVLEQQYQSMCTWIAAIPENMKRHRHLCDPVVLQFAVAVRESNPWAVMTAYHKINGVHCSEDPRLIRDIPRSEWKYDGLVLCDWWGIYSTSELINAGMDLEMPGPTDWRCKILAWATRSRKVSIETIDSSVRRVLKLVNRVLAAQSEPVKDSDTEKNRALLRETTAVPVVLLKKNEANVLPLVKDSKTRYALIGDHWKNPAVAGDDSSEVTPYYVSTPYSAFVEAVGEDSFICAMGCYSHKFAPLLYSTITQPGSDAHGMLLEFFNKDPNGSSDAELLYTTTTEKTDLKFADSLPPDTVPEYTSSGSAPSRGSRWGCAGWIREAVEIARQVDIPVILTGLSADYEYEGIDRKSLGLPGRVDELIERVTEANPKTIIITEAGTATTMPWADKTPTVIHSWFGRQETGHGIVDILFGDVNPSGRLPLTFPRNLEVPPVYESDPKHIMTISVSLKNTGQCPGAEIVQVYVKDVSSSVQRPRKELKSFKKVHLAPGENMKIEVTS | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 57627
Sequence Length: 517
Pathway: Glycan metabolism; cellulose degradation.
Subcellular Location: Secreted
EC: 3.2.1.21
|
Q5LIC7 | MKQQKCNYFPSLWWRGREKGLSTFLFLLLFSISLHAQRQDILLNNNWNFRFSHQVQGDTRRVDLPHTWNAQDALAGKIDYKRGIGNYEKALYIRPEWKGKRLFLRFDGVNSIADVFINRKHIGEHRGGYGAFIFEITDLVKYGEKNSVLVRANNGEQLDIMPLVGDFNFYGGIYRDVHLLITDETCISPLDYASPGVYLVQEVVSPQEAKVCAKVNLSNRAADGTAELQVLVTDGTKVICKESRNVSLKQGADILEQLPLLIQKPRLWNGCEDPFMYQVSISLHKDGKQIDSVTQPLGLRYYHTDPDKGFFLNGKHLPLHGVCRHQDRAEVGNALRPQHHEEDVALMREMGVNAIRLAHYPQATYMYDLMDKHGIVTWAEIPFVGPGGYADKGFVDQASFRENGKQQLIELIRQHYNHPSICFWGLFNELKEVGDNPVEYVKELNALAKQEDPTRPTTSASNQDGNLNFITENIAWNRYDGWYGSTPKTLATFLDRTHKKHPELRIGISEYGAGASIYHQQDSLKQPSASGWWHPENWQTYYHMENWKIIAERPFVWGTFVWNMFDFGAAHRTEGDRPGINDKGLVTFDRKVRKDAFYFYKANWNKQEPMIYLAEKRCRLRYQPEQTFMAFTTAPEAELFVNGVSCGKQKADTYSTVVWKNVKLTSGENIIRVTTPGKKPLTDEVTVEYKEDRPL | Function: Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.
Catalytic Activity: a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate
Sequence Mass (Da): 79909
Sequence Length: 695
Domain: The N-K motif seems to be a discriminant that could be employed as a fingerprint to identify beta-glucuronidases from the large GH2 family of proteins.
EC: 3.2.1.31
|
Q8XP19 | MLYPIITESRQLIDLSGIWKFKLNEGNGLTEELSKAPLEDTIEMAVPSSYNDLVESQEVRDHVGWVWYERNFTIPKTLLNERIVLRFGSATHEAKVYLNGELLVEHKGGFTPFEAEINDLLVSGDNRLTVAVNNIIDETTLPVGLVKEVEVDGKKVIKNSVNFDFFNYAGIHRPVKIYTTPKSYIEDITIVTDFKENNGYVNYEVQAVGKCNIKVTIIDEENNIVAEGEGKEGKLTINNVHLWEPMNAYLYKLKVELLDDEEIIDTYFEEFGVRTVEVKDGKFLINNKPFYFKGFGKHEDSYVNGRGINEAINIKDFNLMKWIGANSFRTSHYPYSEEIMRLADREGIVVIDETPAVGLHLNFMATGFGGDAPKRDTWKEIGTKEAHERILRELVSRDKNHPCVVMWSVANEPDSDSEGAKEYFEPLIKLTKELDPQKRPVTVVTYLMSTPDRCKVGDIVDVLCLNRYYGWYVAGGDLEEAKRMLEDELKGWEERCPKTPIMFTEYGADTVAGLHDTVPVMFTEEYQVEYYKANHEVMDKCKNFVGEQVWNFADFATSQGIIRVQGNKKGIFTRERKPKMIAHSLRERWTNIPEFGYKK | Function: Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon . As part of the GI microbiome, this enzyme is able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract .
Catalytic Activity: a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate
Sequence Mass (Da): 68729
Sequence Length: 599
Domain: The N-K motif seems to be a discriminant that could be employed as a fingerprint to identify beta-glucuronidases from the large GH2 family of proteins.
EC: 3.2.1.31
|
P05804 | MLRPVETPTREIKKLDGLWAFSLDRENCGIDQRWWESALQESRAIAVPGSFNDQFADADIRNYAGNVWYQREVFIPKGWAGQRIVLRFDAVTHYGKVWVNNQEVMEHQGGYTPFEADVTPYVIAGKSVRITVCVNNELNWQTIPPGMVITDENGKKKQSYFHDFFNYAGIHRSVMLYTTPNTWVDDITVVTHVAQDCNHASVDWQVVANGDVSVELRDADQQVVATGQGTSGTLQVVNPHLWQPGEGYLYELCVTAKSQTECDIYPLRVGIRSVAVKGEQFLINHKPFYFTGFGRHEDADLRGKGFDNVLMVHDHALMDWIGANSYRTSHYPYAEEMLDWADEHGIVVIDETAAVGFNLSLGIGFEAGNKPKELYSEEAVNGETQQAHLQAIKELIARDKNHPSVVMWSIANEPDTRPQGAREYFAPLAEATRKLDPTRPITCVNVMFCDAHTDTISDLFDVLCLNRYYGWYVQSGDLETAEKVLEKELLAWQEKLHQPIIITEYGVDTLAGLHSMYTDMWSEEYQCAWLDMYHRVFDRVSAVVGEQVWNFADFATSQGILRVGGNKKGIFTRDRKPKSAAFLLQKRWTGMNFGEKPQQGGKQ | Function: Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG) and with 4-methylumbelliferyl-glucuronide . Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme is able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract .
Catalytic Activity: a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate
Sequence Mass (Da): 68447
Sequence Length: 603
Domain: The N-K motif seems to be a discriminant that could be employed as a fingerprint to identify beta-glucuronidases from the large GH2 family of proteins.
EC: 3.2.1.31
|
P08236 | MARGSAVAWAALGPLLWGCALGLQGGMLYPQESPSRECKELDGLWSFRADFSDNRRRGFEEQWYRRPLWESGPTVDMPVPSSFNDISQDWRLRHFVGWVWYEREVILPERWTQDLRTRVVLRIGSAHSYAIVWVNGVDTLEHEGGYLPFEADISNLVQVGPLPSRLRITIAINNTLTPTTLPPGTIQYLTDTSKYPKGYFVQNTYFDFFNYAGLQRSVLLYTTPTTYIDDITVTTSVEQDSGLVNYQISVKGSNLFKLEVRLLDAENKVVANGTGTQGQLKVPGVSLWWPYLMHERPAYLYSLEVQLTAQTSLGPVSDFYTLPVGIRTVAVTKSQFLINGKPFYFHGVNKHEDADIRGKGFDWPLLVKDFNLLRWLGANAFRTSHYPYAEEVMQMCDRYGIVVIDECPGVGLALPQFFNNVSLHHHMQVMEEVVRRDKNHPAVVMWSVANEPASHLESAGYYLKMVIAHTKSLDPSRPVTFVSNSNYAADKGAPYVDVICLNSYYSWYHDYGHLELIQLQLATQFENWYKKYQKPIIQSEYGAETIAGFHQDPPLMFTEEYQKSLLEQYHLGLDQKRRKYVVGELIWNFADFMTEQSPTRVLGNKKGIFTRQRQPKSAAFLLRERYWKIANETRYPHSVAKSQCLENSLFT | Function: Plays an important role in the degradation of dermatan and keratan sulfates.
PTM: N-linked glycosylated with 3 to 4 oligosaccharide chains.
Catalytic Activity: a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate
Sequence Mass (Da): 74732
Sequence Length: 651
Subcellular Location: Lysosome
EC: 3.2.1.31
|
P12265 | MSLKWSACWVALGQLLCSCALALKGGMLFPKESPSRELKALDGLWHFRADLSNNRLQGFEQQWYRQPLRESGPVLDMPVPSSFNDITQEAALRDFIGWVWYEREAILPRRWTQDTDMRVVLRINSAHYYAVVWVNGIHVVEHEGGHLPFEADISKLVQSGPLTTCRITIAINNTLTPHTLPPGTIVYKTDTSMYPKGYFVQDTSFDFFNYAGLHRSVVLYTTPTTYIDDITVITNVEQDIGLVTYWISVQGSEHFQLEVQLLDEGGKVVAHGTGNQGQLQVPSANLWWPYLMHEHPAYMYSLEVKVTTTESVTDYYTLPIGIRTVAVTKSKFLINGKPFYFQGVNKHEDSDIRGKGFDWPLLVKDFNLLRWLGANSFRTSHYPYSEEVLQLCDRYGIVVIDECPGVGIVLPQSFGNESLRHHLEVMEELVRRDKNHPAVVMWSVANEPSSALKPAAYYFKTLITHTKALDLTRPVTFVSNAKYDADLGAPYVDVICVNSYFSWYHDYGHLEVIQPQLNSQFENWYKTHQKPIIQSEYGADAIPGIHEDPPRMFSEEYQKAVLENYHSVLDQKRKEYVVGELIWNFADFMTNQSPLRVIGNKKGIFTRQRQPKTSAFILRERYWRIANETGGHGSGPRTQCFGSRPFTF | Function: Plays an important role in the degradation of dermatan and keratan sulfates.
Catalytic Activity: a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate
Sequence Mass (Da): 74195
Sequence Length: 648
Subcellular Location: Lysosome
EC: 3.2.1.31
|
P06760 | MSPRRSVCWFVLGQLLCSCAVALQGGMLFPKETPSRELKVLDGLWSFRADYSNNRLQGFEKQWYRQPLRESGPTLDMPVPSSFNDITQEAELRNFIGWVWYEREAVLPQRWTQDTDRRVVLRINSAHYYAVVWVNGIHVVEHEGGHLPFEADITKLVQSGPLTTFRVTIAINNTLTPYTLPPGTIVYKTDPSMYPKGYFVQDISFDFFNYAGLHRSVVLYTTPTTYIDDITVTTDVDRDVGLVNYWISVQGSDHFQLEVRLLDEDGKIVARGTGNEGQLKVPRAHLWWPYLMHEHPAYLYSLEVTMTTPESVSDFYTLPVGIRTVAVTKSKFLINGKPFYFQGVNKHEDSDIRGRGFDWPLLIKDFNLLRWLGANSFRTSHYPYSEEVLQLCDRYGIVVIDECPGVGIVLPQSFGNVSLRHHLEVMDELVRRDKNHPAVVMWSVANEPVSSLKPAGYYFKTLIAHTKALDPTRPVTFVSNTRYDADMGAPYVDVICVNSYLSWYHDYGHLEVIQLQLTSQFENWYKMYQKPIIQSEYGADAVSGLHEDPPRMFSEEYQTALLENYHLILDEKRKEYVIGELIWNFADFMTNQSPLRVTGNKKGIFTRQRNPKMAAFILRERYWRIANETRGYGSVPRTQCMGSRPFTF | Function: Plays an important role in the degradation of dermatan and keratan sulfates.
PTM: Undergoes a post-transcriptional proteolytic cleavage near its C-terminal end, which reduces its size by approximately 3 kDa. The site of this cleavage has as yet not been determined.
Catalytic Activity: a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate
Sequence Mass (Da): 74793
Sequence Length: 648
Subcellular Location: Lysosome
EC: 3.2.1.31
|
Q8E0N2 | MLYPLLTKTRNTYDLGGIWNFKLGEHNPNELLPSDEVMVIPTSFNDLMVSKEKRDYIGDFWYEKVIEVPKVSEDEEMVLRFGSVTHQAKIYVDGVLVGEHKGGFTPFEVLVPECKYNNEKIKVSICANNVLDYTTLPVGNYSEIIQEDGSIKKKVRENFDFFNYAGVHRPLKLMIRPKNHIFDITITSRLSDDLQSADLHFLVETNQKVDEVRISVFDEDNKLVGETKDSRLFLSDVHLWEVLNAYLYTARVEIFVDNQLQDVYEENFGLREIEVTNGQFLLNRKPIYFKGFGKHEDTFINGRGLNEAANLMDLNLLKDMGANSFRTSHYPYSEEMMRLADRMGVLVIDEVPAVGLFQNFNASLDLSPKDNGTWNLMQTKAAHEQAIQELVKRDKNHPSVVMWVVANEPASHEAGAHDYFEPLVKLYKDLDPQKRPVTLVNILMATPDRDQVMDLVDVVCLNRYYGWYVDHGDLTNAEVGIRKELLEWQDKFPDKPIIITEYGADTLPGLHSTWNIPYTEEFQCDFYEMSHRVFDGIPNLVGEQVWNFADFETNLMILRVQGNHKGLFSRNRQPKQVVKEFKKRWMTIPHYHNKKNSVK | Function: Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.
Catalytic Activity: a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate
Sequence Mass (Da): 69398
Sequence Length: 599
Domain: The N-K motif seems to be a discriminant that could be employed as a fingerprint to identify beta-glucuronidases from the large GH2 family of proteins.
EC: 3.2.1.31
|
P16084 | MEKWARIKYTPNLPLGENGERVTASQKHIELSCEAACEGMVLLKNDRNVLPIRKGTRVALFGKGVFDYVKGGGGSGDVTVPYIRNLYEGLSQYTSDISIYDKSVRFYQEYVADQYRLGIAPGMIKEPALPEDILADAAAYADTAIIAISRFSGEGWDRKVAGVDREIKCEAKDLVEQGNKIFDHGDFYLTNAEKKMVKMVKENFSSVIVVMNVGGVVDTTWFKKDDQISSVLMAWQGGIEGGLAAARILLGKVNPSGKLSDTFAARLEDYPSTEGFHEDDDYVDYTEDIYVGYRYFETIPGAKEKVNYPFGYGLSYTTFLLEDYKAEPFVASAADEVGKSDSDLADAIVASVTVTNIGKIPGKEVVQLYYSAPQGKLGKPAKVLGGYAKTRLLQPGESQRVTIALYMEDMASYDDLGKVKKAAWLLEKGEYHFFLGTSVRDTRLLDYTYELSKNIIVEQVSNKLVPTSLPKRMLADGTYEELPQTEPVDTYATIFPRPKNWKETIEHDVLKTPVVRPQDRFQLFLPPKEGDPKKFIEVAECKVTLEDFIAQLSNEQLASLLGGQPNVGMANTFGYGNLPEVGVPNAQTCDGPAGVRIAPEVGVVTTAFPCSTLLACTWNEDICYEVGVAGGEEAKECNFGAWLTPAVNIHRSPLCGRNFEYYSEDPFLAGKQAAAMVRGIQSNNIIATPKHFALNNKESNRKGSDSRASERAIREIYLKAFEIIVKEQSPGASCLQYNIVNGQRSSESHDLLTGILRDEWGFEGVVVSDWWGFGEHYKEVLAGNDIKMGCGYTEQLLEAIDKKALKRKDLEKRQSESSRCFSNSTKLKAA | Function: B.fibrisolvens beta-glucosidase hydrolyzes cellobiose to a limited extent, cellotriose to cellobiose and glucose, and cellotetraose and cellopentaose to predominantly glucose.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 91852
Sequence Length: 830
EC: 3.2.1.21
|
P07337 | MSKFDVEQLLSELNQDEKISLLSAVDFWHTKKIERLGIPAVRVSDGPNGIRGTKFFDGVPSGCFPNGTGLASTFDRDLLETAGKLMAKESIAKNAAVILGPTTNMQRGPLGGRGFESFSEDPYLAGMATSSVVKGMQGEGIAATVKHFVCNDLEDQRFSSNSIVSERALREIYLEPFRLAVKHANPVCIMTAYNKVNGDHCSQSKKLLIDILRDEWKWDGMLMSDWFGTYTTAAAIKNGLDIEFPGPTRWRTRALVSHSLNSREQITTEDVDDRVRQVLKMIKFVVDNLEKTGIVENGPESTSNNTKETSDLLREIAADSIVLLKNKNNYLTSKERRQYHVIGPNAKAKTSSGGGSASMNSYYVVSPYEGIVNKLGKEVDYTVGAYSHKSIGGLAESSLIDAAKPADAENAGLIAKFYSNPVEERSEDEEPFHVTKVNRSNVHLFDFKHEKVDPKNPYFFVTLTGQYVPQEDGDYIFSLQVYGSGLFYLNDELIIDQKHNQERGSFCFGAGTKERTKKLTLKKGQVYNVRVEYGSGPTSGLVGEFGAGGFQAGVIKAIDDDEEIRNAAELAAKHDKAVLIIGLNGEWETEGYDRENMDLPKRTNELVRAVLKANPNTVIVNQSGTPVEFPWLEEANALVQAWYGGNELGNAIADVLYGDVVPNGKLSLSWPFKLQDNPAFLNFKTEFGRVVYGEDIFVGYRYYEKLQRKVAFPFGYGLSYTTFELDISDFKVTDDKIDISVDVKNTGDKFAGSEVVQVYFSALNSKVSRPVKELKGFEKVHLEPGEKKTVNIELELKDAISYFNEELGKWHVEAGEYLVSVGTSSDDILSVKEFKVEKDLYWKGL | Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 93917
Sequence Length: 845
Pathway: Glycan metabolism; cellulose degradation.
EC: 3.2.1.21
|
Q9LD45 | MDAFSSFFDSQPGSRSWSYDSLKNFRQISPAVQNHLKRVYLTLCCALVASAFGAYLHVLWNIGGILTTIGCIGTMIWLLSCPPYEHQKRLSLLFVSAVLEGASVGPLIKVAIDVDPSILITAFVGTAIAFVCFSAAAMLARRREYLYLGGLLSSGLSMLMWLQFASSIFGGSASIFKFELYFGLLIFVGYMVVDTQEIIEKAHLGDMDYVKHSLTLFTDFVAVFVRILIIMLKNSADKEEKKKKRRN | Function: Suppressor of apoptosis. Modulator of endoplasmic reticulum stress-mediated programmed cell death. Involved in methyl jasmonate-induced leaf senescence through regulating cytoplasmic calcium level.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27483
Sequence Length: 247
Subcellular Location: Endoplasmic reticulum membrane
|
Q9VSH3 | MADTANYINDRFQTFMNGLGDRYEPYVREHLSKVYMVLGSTAAATAMGAMLQMRDFLDLGVLAAVATLVLVLGLHFYKDDGKNYYTRLGMLYAFGFCSGQTLGPLLGYICSINPAIILSALTGTFVTFISLSLSALLAEQGKYLYLGGMLVSVINTMALLSLFNMVFKSYFVQVTQLYVGVFVMAAFIVYDTQNIVEKCRNGNRDVVQHALDLFFDVLSMFRRLLIILTQKEERKQNERRQNKTK | Function: Suppressor of apoptosis (By similarity). Modulates unfolded protein response signaling . Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduces cell survival during starvation .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27574
Sequence Length: 245
Subcellular Location: Endoplasmic reticulum membrane
|
P55061 | MNIFDRKINFDALLKFSHITPSTQQHLKKVYASFALCMFVAAAGAYVHMVTHFIQAGLLSALGSLILMIWLMATPHSHETEQKRLGLLAGFAFLTGVGLGPALEFCIAVNPSILPTAFMGTAMIFTCFTLSALYARRRSYLFLGGILMSALSLLLLSSLGNVFFGSIWLFQANLYVGLVVMCGFVLFDTQLIIEKAEHGDQDYIWHCIDLFLDFITVFRKLMMILAMNEKDKKKEKK | Function: Suppressor of apoptosis . Modulates unfolded protein response signaling . Modulates ER calcium homeostasis by acting as a calcium-leak channel . Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduces cell survival during starvation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26538
Sequence Length: 237
Domain: The intra-membrane loop at the C-terminus acts as a calcium pore, mediating calcium leak from the ER into the cytosol.
Subcellular Location: Endoplasmic reticulum membrane
|
Q9D2C7 | MNIFDRKINFDALLKFSHITPSTQQHLKKVYASFALCMFVAAAGAYVHVVTHFIQAGLLSALGSLALMIWLMATPHSHETEQKRLGLLAGFAFLTGVGLGPALELCIAVNPSILPTAFMGTAMIFTCFSLSALYARRRSYLFLGGILMSAMSLMLLSSLGNLFFGSIWLFQANLYLGLLVMCGFVLFDTQLIIEKAEHGDKDYIWHCVDLFLDFVTLFRKLMLILAFNEKDKKKEKK | Function: Suppressor of apoptosis (By similarity). Modulates unfolded protein response signaling (By similarity). Modulates ER calcium homeostasis by acting as a calcium-leak channel (By similarity). Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduces cell survival during starvation .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26478
Sequence Length: 237
Domain: The intra-membrane loop at the C-terminus acts as a calcium pore, mediating calcium leak from the ER into the cytosol.
Subcellular Location: Endoplasmic reticulum membrane
|
Q9MBD8 | MDAFYSTSSAYGAAASGWGYDSLKNFRQISPAVQSHLKLVYLTLCVALAASAVGAYLHVALNIGGMLTMLGCVGSIAWLFSVPVFEERKRFGILLAAALLEGASVGPLIKLAVDFDSSILVTAFVGTAIAFGCFTCAAIVAKRREYLYLGGLLSSGLSILLWLQFAASIFGHSTGSFMFEVYFGLLIFLGYMVYDTQEIIERAHHGDMDYIKHALTLFTDFVAVLVRILVIMLKNASDKSEEKKRKKRS | Function: Suppressor of apoptosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27114
Sequence Length: 249
Subcellular Location: Membrane
|
P55062 | MNIFDRKINFDALLKFSHITPSTQQHLKKVYASFALCMFVAAAGAYVHVVTRFIQAGLLSALGALALMICLMATPHSHETEQKRLGLLAGFAFLTGVGLGPALELCIAINPSILPTAFMGTAMIFTCFSLSALYARRRSYLFLGGILMSAMSLMFVSSLGNLFFGSIWLFQANLYMGLLVMCGFVLFDTQLIIEKAEHGDKDYIWHCIDLFLDFVTLFRKLMLILAFNEKDKKKEKK | Function: Suppressor of apoptosis. Modulates unfolded protein response signaling. Modulates ER calcium homeostasis by acting as a calcium-leak channel. Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduces cell survival during starvation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26464
Sequence Length: 237
Domain: The intra-membrane loop at the C-terminus acts as a calcium pore, mediating calcium leak from the ER into the cytosol.
Subcellular Location: Endoplasmic reticulum membrane
|
Q0H8X2 | MRLLKTHPILGLANSYLIDSPQPSNISYMWNFGSLLGVCLIIQILTGVFLAMHYTPSVDLAFISVEHIMRDVNYGWLIRYLHANTASFFFIFVYLHIGRGLYYGSYKSPRTLLWSIGVIILVLMMAIAFLGFNGQKYMCFYNIDITIIQYLSIPTLITPSTRLKPILDKHNIKPVLLFENLTNSETKKIAYQALKPFSGIYMIVNLITEKYYVGSAVTGNLYMRFHKHLFSFTGNKRVANAVNKYGLSEFAFLVLEIVPQKDKIDSTLLLNREDYYLETLKPEYNIAPLASNSLGWKHSEESLAKMRENYSEERRQQVANINKGKTLSEETRELIRKSALLRKSMSSETRMKCAVNVQPVTIINLDGTNIMNFVSIKEASIAISCNEKTIRRALNGNGIVKKNYIVKVIK | Function: Mitochondrial DNA endonuclease involved in intron homing.
PTM: The mature protein may arise from proteolytic cleavage of an in-frame translation of COB exon 1 plus intron 1, containing the bI1 open reading frame.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46822
Sequence Length: 410
Subcellular Location: Mitochondrion
|
Q9UHR4 | MSRGPEEVNRLTESTYRNVMEQFNPGLRNLINLGKNYEKAVNAMILAGKAYYDGVAKIGEIATGSPVSTELGHVLIEISSTHKKLNESLDENFKKFHKEIIHELEKKIELDVKYMNATLKRYQTEHKNKLESLEKSQAELKKIRRKSQGSRNALKYEHKEIEYVETVTSRQSEIQKFIADGCKEALLEEKRRFCFLVDKHCGFANHIHYYHLQSAELLNSKLPRWQETCVDAIKVPEKIMNMIEEIKTPASTPVSGTPQASPMIERSNVVRKDYDTLSKCSPKMPPAPSGRAYTSPLIDMFNNPATAAPNSQRVNNSTGTSEDPSLQRSVSVATGLNMMKKQKVKTIFPHTAGSNKTLLSFAQGDVITLLIPEEKDGWLYGEHDVSKARGWFPSSYTKLLEENETEAVTVPTPSPTPVRSISTVNLSENSSVVIPPPDYLECLSMGAAADRRADSARTTSTFKAPASKPETAAPNDANGTAKPPFLSGENPFATVKLRPTVTNDRSAPIIR | Function: May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection.
PTM: Phosphorylated on tyrosine in response to insulin.
Sequence Mass (Da): 56883
Sequence Length: 511
Domain: The IMD domain is predicted to have a helical structure. It may induce actin bundling and filopodia formation (By similarity).
Subcellular Location: Cytoplasm
|
B0CC69 | MSEETFPQASALTLLSDPNIDLLSLVAAAGEVRMTYFGRQVMLHRINDIQNGLCPEDCGYCAQSKISDAPIKKYPLKSEEDIIQEAYEAKAKGVYRYCMVSSGRGPTAERTEHLAHIIRRIKNEVGIQTCLSAGLMDHEQAAVLKEAGLDRLNHNLNTSESHTPDIVTTHTFQDRINTLKAARSAGLDLCSGMIAGMGETDQDIVDIAYQLHEYQVPSIPINFLIPISGNPIYDCNQLTPQRCLRILCLFRFVNPKAEIRIGGGREGHLRSLQALALYPANSLFVEGYLATRGHSVDQVYQLIHDAGFEVAGETSLTGDLSATSQFQLDDNPNILNPQTTISFSNS | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 38083
Sequence Length: 346
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
EC: 2.8.1.6
|
Q6FAP9 | MTLRNDWTRDEIQALYDQPFLDLVFQAQQVHREHFSANTIQVSTLLSIKTGKCPEDCKYCSQSAHYDSKLEAEKRIAVDKVISEAKAAKDSGSSRFCMGAAWRNPHERDMPYVLEMVREVKALGLETCMTLGMLNQSQAERLSDAGLDYYNHNLDTSREYYNNIISTRTFDDRLNTLDHVRSAGMKVCSGGIVGLGEQKQDRIGLLHELATLPIHPESVPINMLVPIEGTPLADVEKLDVTEWIRTIAVARIIMPYSYIRLSAGRESLSDSDQALAFMAGANSLFSGDKLLTTPNAGEGKDQVLFAKLGLVAEKPKVSVRAMAVDAMSA | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36505
Sequence Length: 329
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
EC: 2.8.1.6
|
B7MGN3 | MAHRPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFDPRQVQVSTLLSIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGVKAMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKVREAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDAFDFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDKDLQLFRKLGLNPQQTAVLAGDNEQQQRLEQALMTPDTDEYYNAAAL | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 38662
Sequence Length: 346
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
EC: 2.8.1.6
|
Q2GHB1 | MNTCTTIRNNWQLDEILELFNTPFNDLILRSHLTHRQFFNNNEIQLAALLNIKTGGCPENCRYCSQSAHYKTDLQKEALLDVENIKKAIQTAKNSGADRFCFAAAWRQLRDKDIEYICNIINLIKSEKLESCASLGMITLDQAKKLKNAGLDFYNHNIDTSRDFYSNVTTTRNYDDRLASLNNIYEAGINICSGGILGLGESIEDRAKMLLTLANLKEHPRSVPINRLVPIKGTPFENNIKVDNIDFIKTIAVTRILMPKSYVRLAAGRKDMSEEMQALCLFAGANSIFYGEKLLTTPNSNCDDDKNLLSKLGIKTKEPVLLNSQN | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36793
Sequence Length: 326
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
EC: 2.8.1.6
|
Q47C02 | MTSAIKPKAGTRPSKARIRQSFERAAPTYDDAAAIQRRICIRLAEGLPDIAPTHLLDAGCGTGYAQANLQTRFPDAHRVALDLSPGMLQRVATPCCRVAGDLEHLPLADSSLDLYWSSLAVQWCDLAVALREAHRTLRPGGVIALASLGPATFHELRHAFADVDDHRHTLAFHSPGEIRQLASLAGLAAIDIKKSTEIAHYPDFKTLLRAVKAIGANQLGDGRRTSLMSRSSFQLAESACEQLRTPAGLPLTYDVIYLYARK | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28500
Sequence Length: 262
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
P12999 | MATVNKQAIAAAFGRAAAHYEQHADLQRQSADALLAMLPQRKYTHVLDAGCGPGWMSRHWRERHAQVTALDLSPPMLVQARQKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPKGVVAFTTLVQGSLPELHQAWQAVDERPHANRFLPPDEIEQSLNGVHYQHHIQPITLWFDDALSAMRSLKGIGATHLHEGRDPRILTRSQLQRLQLAWPQQQGRYPLTYHLFLGVIARE | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28276
Sequence Length: 251
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
D8MPW4 | MQTVNKQAIAQAFGRAAQSYNQHAGLQRLCGEELASYATRRQGQKVLDAGCGPGWFSQHWRAAGNHVTALDLSAEMLVQAQALHTADCYQPGDIEALPFSDASFDLCWSNLAVQWCSDLSLALTELYRVTSPGGQVLFSTLSADSLHELSAAWQPLDLPAPVNRFLPFDAIAHAGQHLPLTLMQQTLTVGFPDVLSALRSLKGIGATHLHQGRHGGLLSRRHLQQLEQHWPRDRRGYLLSYHLVYGVMHRE | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27725
Sequence Length: 251
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
D9SJ16 | MNEFVIDKKAMRQAFSRAAEGYDASAVLQREVCMRMLERLEYIKLQPARLLDAGSGTGWGGRQLAEKYPAAQVISLDIAIGMLQTSKSRSSWWQKLFGGCRQLPVCADVEALPLAANSLDMVWSNLAVQWCNDLPATFVELHRVLKTEGLLMFSTLGPDTLKELRQAFKGVDERSHLNRFADMHDIGDMLVQAGFAEPVMDMEYLTLTYEDVRGVLQDLKAIGAHNTTAGRGQGLMGKAAWARLLENYEKLRRDGKLPATYEVVYGHAWKPAPRVNRDGAAIIKTSFKIK | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32394
Sequence Length: 290
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
Q749W5 | MIDRRKVRNAFHRGAADYDAYAAVQKRVMERILSLLFAEGVEPARILDVGAGTGALALRLADRYPSAAITCVDLAHGMARQARDNLGRTMERLVAVADAEHLPLRDGVFDLVVSTSTFQWLTTLDRAFAEARRVLADDGLFAFALFGDGTFKELKASYRAALHSVPRGGRDRTHRFFTRDEVRAALARAGFRSVEVFDEDEVEYHPDVPAFLRSVKRIGAGNASPVAGRGLSGRRVMETMMRTYAERFGGADGIPATYTVVYGVGKR | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29414
Sequence Length: 267
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
Q7VL11 | MAKLAKQLIAKRFVSHLTEYDQYAIAQQQINHQLVDLLQANTDKTFQRALEIGCGTGNLTEKLLAKIPIEHLTLNDFNAIYYPTVLQKIKQKKPLVVVDFMQGDAEQLVFTRNFDLVSAASVVQWFDSPQQFLRNSAYALKPGGVVLFNSFSPLNLQEIRQLTGIGLNYPTRLQWQEWLAQDFEQCQLIEQPIKLTFDSPLAVLIHLKKTGVTAVSNKPWNRHQIKQFCMEYQAHFACEQGVYLTYTPILMLGIKKNG | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29501
Sequence Length: 258
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
P45249 | MGSLTSVDKSRIRQAFQKALNDYDRHALIQQKMTINLMAHLQDYLPNGSLDSVLELGCGSGMLSSLLQKQISADYWLFNDLCDVQTQLAEKLPQSFDFYCGDAEHFLFLQQFDLIASASAVQWFHQPDAFIAHCKTGLKTNGLLAVATFGEDNLKEVRQITNIGLNYPTLSQWQTWLAKDFELLWCEDFKVILDFDTPLDVLKHLKYTGVTATNQKNWTRKNLNGFIGDYLSAFGMPSGKVRLTYHPLFFIARYSHIENQ | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29676
Sequence Length: 260
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
Q2SBD7 | MNHAVTIKSFVSTSPLSDLERGAVDKSKVAESFSAAAATYDLLAGMQKEVGESLVSLSREGCPQDIIDVGCGTGWLTHRLKNSFPEARLCAYDLSPGMIEYALAHHDNVAEIWAVADMESLPVANASQDLVFSNMAMQWLDDPRAWFAEASRVLRPGGRLICSTLLTQTLFELEQAWHGVDGGRHVNRFLSAEQVAEAAVSCGLRGECRESLYVRFHDSALDVMKELKGIGAHNIQSERPQGLTGKRRLRRVIENYEKCRQEQGVPATYHVGVCVYSRI | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30783
Sequence Length: 279
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
Q9K623 | MFIDKQTVERHFSKSAHLYDGVNHVQRKMAHRLVQLLDEKRRDAKDEPRAILDIGCGTGWLTRECLKSFPQATIDAVDLSKQMLEVAEKNVSSHPNVQFIQGDIEKMVREKPSAKTYDVIVANAVFQWLDKPTETVAQLRSWLKPNGLLLFSTFGPDTFYELHDSFQLAAKQLGIIDERRGLDYLSKTEWKRTLDGLFAELTIHEEKAIESYATVEQFLHTVKKMGATYSQSSRPLSKRYYQLMKEIYEQRYRTEDSIPATYDCLYVLCQA | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 31379
Sequence Length: 271
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
A1WVM4 | MNPGDAQSIDRRCVRRSFDASAERYDEVAVLQREVADRLLERLEPVRVHPRRVLDLGAGTGYATRGLLRRYRKAEVHAVDLAPAMLQRVRRRAPWLRRPRCVCADLHALPYPDDSFELVFSNLALQWAEDLPTALRELQRVTAPEGAVMFATFGPETLHELRGAWAEVGDQARVHRFADKHDVGDRMLEAGFVDPVLDGESFTLTYAQPREVMRDLKALGASNADPGRPRGLLSPHRLARVEAAYRLAWRQPDGRVPATYEVVYGHAWGMGGTPQRADDTGEVRLDVHGIRRRRR | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33395
Sequence Length: 295
Pathway: Cofactor biosynthesis; biotin biosynthesis.
EC: 2.1.1.197
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.