ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P37458 | MSLMQFSGLLVVWLLSTLFIATLTWFEFRRVRFNFNVFFSLLFLLTFFFGFPLTSVLVFRFDVGVAPPEILLQALLSAACFYGVYYVTYKTRLRKRVVDVPRKPLFTMNRVETHLTWVILMGIALVSVAIFFMHNGFLLFRLHSYSQIFSSEVSGVALKRFFYFFIPAMLVVYFLRQDSKAWLFFLVSTVAFGLLTYMIVGGTRANIIIAFAIFLFIGIIRGWISLWMLAAAGVLGIVGMFWLALKRYGLNVSGDEAFYTFLYLTRDTFSPWENLALLLQNYHNIEFQGLAPIVRDFYVFIPTWLWPGRPSIVLNSANYF... | Function: Probably involved in the polymerization of enterobacterial common antigen (ECA) trisaccharide repeat units.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51647
Sequence Length: 452
Pathway: Bacterial outer membrane biogenesis; enterobacterial common antigen biosynthesis.
Subcellular Locat... |
Q46800 | MFDFASYHRAATLADAINLLADNPQAKLLAGGTDVLIQLHHHNDRYRHIVDIHNLAELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPRGVRFVPINGFHTGPGKVSLEHDEILVAFHFPPQPKEHAGSAHFKYAMRDAMDISTIGCAAHCRLDNGNFSELRLAFGVAAPTPIRCQHAEQTAQNAPLNLQTLEAISESVLQDVAPRSSWRASKEFRLHLIQTMTKKVISEAVAAAGGKLQ | Function: Presumed to be a dehydrogenase, but possibly an oxidase. Participates in limited purine salvage (requires aspartate) but does not support aerobic growth on purines as the sole carbon source (purine catabolism).
Catalytic Activity: H2O + NAD(+) + xanthine = H(+) + NADH + urate
Sequence Mass (Da): 31557
Sequenc... |
O32145 | MNGQVTKARMNIQLWRPAALDEAYSLLEKLAPDVCAASGSTLLQLQWDKGTLPKQHLVSLEGIDEMRGISTSDTHVSIGGLTSLNECRKNPLIKRALSCFSDAASAVAAPGIRSRATIGGNIASKIGDFIPLLLVLGAELIVYQKELIRLPLGAWLSEEDFRTAIVTRVIIPRAEGERVFYHKLGRRQAFTGAAAVAAGRFLKDGSIRLAAGHADITPRRLLDSEAKWMAPGWDPHELYKTLIHELPFSSDVFMSAAYRKKAAANVIMAELMAEGGE | Function: Oxidizes hypoxanthine and xanthine to uric acid.
Catalytic Activity: H2O + NAD(+) + xanthine = H(+) + NADH + urate
Sequence Mass (Da): 30119
Sequence Length: 277
Pathway: Purine metabolism; hypoxanthine degradation; urate from hypoxanthine: step 1/2.
EC: 1.17.1.4
|
Q46801 | MNHSETITIECTINGMPFQLHAAPGTPLSELLREQGLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRTLEGEAKGGKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAKPREKPLTITEIRRGLAGNLCRCTGYQMIVNTVLDCEKTK | Cofactor: Binds 2 [2Fe-2S] clusters.
Function: Iron-sulfur subunit of the xanthine dehydrogenase complex.
Sequence Mass (Da): 16922
Sequence Length: 159
Pathway: Purine metabolism; hypoxanthine degradation; urate from hypoxanthine: step 1/2.
|
O32144 | MIINKPSRVRPDGRGKVTGELKYMTDLSFPGMLYGKVLRSAYPHAEIVSVCTIKAEKMEGVQAVVTHKDVPGLNRFGIVIPDQPVLCEDRVRYVGDAIAAVAAETEEIAEAALELIQVEYKELEVMDSPEKALRPNAQRLHEDGNILHRAFFSNGDVEEGFQASDTVFEETYELPRQMHTYMETEGGVAVPEDDGGFTMYAGTQHGYKDRFQLARIFDIPEEKIRIVSSPMGGSFGGKDELNIQPYAALLALKSGRPVKIHQTRKESVRSGIKRHPMKITIKTGADHSGNLLAHDVKIVADTGAYATLGPAVLDFSVEHA... | Cofactor: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Function: Oxidizes hypoxanthine and xanthine to uric acid.
Catalytic Activity: H2O + NAD(+) + xanthine = H(+) + NADH + urate
Sequence Mass (Da): 80434
Sequence Length: 745
Pathway: Purine metabolism; hypoxanthine degradation; urate from hypoxanthine: ste... |
Q46814 | MIIHFTLNGAPQELTVNPGENVQKLLFNMGMHSVRNSDDGFGFAGSDAIIFNGNIVNASLLIAAQLEKADIRTAESLGKWNELSLVQQAMVDVGVVQSGYNDPAAALIITDLLDRIAAPTREEIDDALSGLFSRDAGWQQYYQVIELAVARKNNPQATIDIAPTFRDDLEVIGKHYPKTDAAKMVQAKPCYVEDRVTADACVIKMLRSPHAHALITHLDVSKAEALPGVVHVITHLNCPDIYYTPGGQSAPEPSPLDRRMFGKKMRHVGDRVAAVVAESEEIALEALKLIDVEYEVLKPVMSIDEAMAEDAPVVHDEPVV... | Cofactor: Binds 2 [2Fe-2S] centers.
Function: Probably has no xanthine dehydrogenase activity; however deletion results in increased adenine sensitivity, suggesting that this protein contributes to the conversion of adenine to guanine nucleotides during purine salvage.
Sequence Mass (Da): 103519
Sequence Length: 956
EC... |
O32143 | MDIKEAGPFPVKKEQFRMTVNGQAWEVAAVPTTHLSDLLRKEFQLTGTKVSCGIGRCGACSILIDGKLANACMTMAYQADGHSITTIEGLQKEELDMCQTAFLEEGGFQCGYCTPGMIIALKALFRETPQPSDKDIEEGLAGNLCRCTGYGGIMRSACRIRRELNGGRRESGF | Cofactor: Binds 2 [2Fe-2S] clusters.
Function: Oxidizes hypoxanthine and xanthine to uric acid.
Catalytic Activity: H2O + NAD(+) + xanthine = H(+) + NADH + urate
Sequence Mass (Da): 18838
Sequence Length: 173
Pathway: Purine metabolism; hypoxanthine degradation; urate from hypoxanthine: step 1/2.
EC: 1.17.1.4
|
Q9A9Z0 | MSSAIYPSLKGKRVVITGGGSGIGAGLTAGFARQGAEVIFLDIADEDSRALEAELAGSPIPPVYKRCDLMNLEAIKAVFAEIGDVDVLVNNAGNDDRHKLADVTGAYWDERINVNLRHMLFCTQAVAPGMKKRGGGAVINFGSISWHLGLEDLVLYETAKAGIEGMTRALARELGPDDIRVTCVVPGNVKTKRQEKWYTPEGEAQIVAAQCLKGRIVPENVAALVLFLASDDASLCTGHEYWIDAGWR | Function: Involved in the degradation of D-xylose . Catalyzes the initial reaction in the xylose utilization pathway by oxydizing D-xylose into D-xylonolactone . Shows some activity with L-arabinose and D-lyxose, but D-xylose is clearly the best substrate . Has no activity with D-ribose, D-glucose, D-galactose or D-man... |
Q9AEM9 | MTNPVIGTPWQKLDRPVSEEAIEGMDKYWRVANYMSIGQIYLRSNPLMKEPFTRDDVKHRLVGHWGTTPGLNFLLAHINRLIADHQQNTVFIMGPGHGGPAGTAQSYIDGTYTEYYPNITKDEAGLQKFFRQFSYPGGIPSHFAPETPGSIHEGGELGYALSHAYGAIMDNPSLFVPCIIGDGEAETGPLATGWQSNKLVNPRTDGIVLPILHLNGYKIANPTILARISDEELHDFFRGMGYHPYEFVAGFDNEDHLSIHRRFAELFETIFDEICDIKAAAQTDDMTRPFYPMLIFRTPKGWTCPKFIDGKKTEGSWRAH... | Function: Phosphoketolase using both fructose 6-phosphate and xylulose 5-phosphate as substrate.
Catalytic Activity: D-xylulose 5-phosphate + phosphate = acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
Sequence Mass (Da): 92530
Sequence Length: 825
EC: 4.1.2.22
|
Q8VXZ5 | MVEGWRNGFRDATNSKPLFVTIYATVIIGVLVSSFYVFSAIYSPTNGSSSFLSFPPLSTSGRIHSLPQENATLELPVAPPPPPQALPPPVLEEAQGNSLGKIWVSPPRDKKMPPLETFKLTKELFGERVKDNVIIVTFGNYAFMDFILTWVKHLTDLDLSNILVGAMDTKLLEALYWKGVPVFDMGSHMSTVDVGWGSPTFHKMGREKVILIDSVLPFGYELLMCDTDMVWLKNPMPYLARFPDADVLTSSDQVVPTVIDDSLDIWQQVGAAYNIGIFHWRPTESAKKLAKEWKEILLADDKVWDQNGFNEIVRRQLGPS... | Function: Plays a role in the arabinosylation of cell wall components. Involved in the arabinosylation of extensin proteins in root hair cells . Extensins are structural glycoproteins present in cell walls and its arabinosylation is important for cell elongation, root hair cell development, lateral root development and... |
Q7Z9M8 | MKVSRVLALVLGAVIPAHAAFSWKNVKLGGGGGFVPGIIFHPKTKGVAYARTDIGGLYRLNADDSWTAVTDGIADNAGWHNWGIDAVALDPQDDQKVYAAVGMYTNSWDPSNGAIIRSSDRGATWSFTNLPFKVGGNMPGRGAGERLAVDPANSNIIYFGARSGNGLWKSTDGGVTFSKVSSFTATGTYIPDPSDSNGYNSDKQGLMWVTFDSTSSTTGGATSRIFVGTADNITASVYVSTNAGSTWSAVPGQPGKYFPHKAKLQPAEKALYLTYSDGTGPYDGTLGSVWRYDIAGGTWKDITPVSGSDLYFGFGGLGLD... | Function: Hydrolyzes the glucosidic bonds of unbranched Glc residues in tamarind seed xyloglucan, producing XXXG, XLXG, XXLG and XLLG. Has a low activity against beta-glucan and carboxymethylcellulose. Not active against Avicel, laminarin, xylan, galactomannan, linear and branched arabinans, galactan, polygalacturonic ... |
B9HJR7 | MGSPFKDHHHHHHPFSLAKKLIPWTFYAMIPLVLFRLYFYPYPLHNITTPILTSSSSSVSSSTPFVAEETSCDYTTGKWVRDKRGPLYNGSACGTIKEGQNCIAHGRPDMGYLYWRWKPKHCKLPRFEPNTFLQLLRNKHLAFVGDSMARNQLESLLCMLSSASAPNLVYRDGDDNKFRRWYFESHNINISVYWSPFLVKGVEKSNTGPNHNQLYLDHVDERWAADMNGIDMIVLSIGHWFLHPAVYYEGDQVLGCHYCPGLNHTEIGFYDVLRKAIKTTLKALIDRKGANSNGINAFVTTFSPAHFEGDWDKLGACPKT... | Function: Xyloglucan acetyltransferase that catalyzes the acetylation of fucosylated Gal residues on xyloglucan side chains . Predominantly catalyze 6-O-monoacetylation of Gal residues in the Fuc-Gal-Xyl trisaccharide side chains of xyloglucan oligomers .
Location Topology: Single-pass type II membrane protein
Sequence... |
B9HVC2 | MGSPFKDHHTLHPSLVRKLIPWTFYAMVPLVLFRVYLYPYPLHHTTTTILTSSPVSPPPALLEDETSCDYTDGNWVPDRRDPLYNGSTCGTIKEGQSCIAHGRPDMGYLYWRWKPKQCKLPRFEPNTFLQLLRNKHLAFVGDSMARNQLESLLCMLSSVSPPNLVYRDGEENKFRRWYFESHNFSISVYWSPFLVRGVEKSNTGLNHNQLFLDHVDERWAADMNGIDMVVLSIGHWFLHPAVYYEGDQVLGCHYCPDLNHTEIGFYDILRKAIKTTLKALVDRKGPNDNGFDALVTTFSPAHFEGDWDKLGACPKTEPCK... | Function: Xyloglucan acetyltransferase that catalyzes the acetylation of fucosylated Gal residues on xyloglucan side chains . Predominantly catalyze 6-O-monoacetylation of Gal residues in the Fuc-Gal-Xyl trisaccharide side chains of xyloglucan oligomers .
Location Topology: Single-pass type II membrane protein
Sequence... |
A0A2K1YKA4 | MNRFFYTVGLIFLFSFFILYSPKTSDLSNNVDLHQQLLISLQKEEERCDLFSGYWVQDLRGSQYTNVSCSSIPESKNCFMQGRPDAGFSQWRWKPDGCELPRFDPGTFFEIVRGKTMAFIGDSVARNHVESLLCLLSSEEMPLGIYKDTEDRTRTWYFPHSNFTLMVIWTRFLVLDEERVINGSVTGVFDLHLDKMDKNWANKLPEIDYAILSDAHWFFRKNYLYEKGKNIGCIFCGEPGIKSLDIDSALQMVIKVVLNYINNCKKCRNILTVLRTFSPAHFADGAWDTGGSCNRTHPLGEKEIDLASLDWKIRSIQVEE... | Function: Xyloglucan acetyltransferase that catalyzes the acetylation of fucosylated Gal residues on xyloglucan side chains . Predominantly catalyze 6-O-monoacetylation of Gal residues in the Fuc-Gal-Xyl trisaccharide side chains of xyloglucan oligomers .
Location Topology: Single-pass type II membrane protein
Sequence... |
Q94AA9 | MAAPRSRRCSLSLLTLFSITLILISVSLFVSTKPANKPFLDYRNQFSISISISSPLEQNTTNTSFVSASPPLSPLGQSNTTNTILASSSSSSSFSDHQNQNKSPSPTSKKIVIRKRSGLDKIESDLAKARAAIKKAASTQNYVSSLYKNPAAFHQSHTEMMNRFKVWTYTEGEVPLFHDGPVNDIYGIEGQFMDEMCVDGPKSRSRFRADRPENAHVFFIPFSVAKVIHFVYKPITSVEGFSRARLHRLIEDYVDVVATKHPYWNRSQGGDHFMVSCHDWAPDVIDGNPKLFEKFIRGLCNANTSEGFRPNVDVSIPEIY... | Function: Involved in pectin biosynthesis. Catalyzes the transfer of xylose from UDP-xylose onto oligogalacturonides and endogenous acceptors.
Catalytic Activity: Transfers a xylosyl residue from UDP-D-xylose to a D-galactose residue in xylogalacturonan, forming a beta-1,3-D-xylosyl-D-galactose linkage.
Location Topolo... |
O94218 | MKLSLLSLATLASAASLQRRSDFCGQWDTATAGDFTLYNDLWGESAGTGSQCTGVDSYSGDTIAWHTSWSWSGGSSSVKSYVNAALTFTPTQLNCISSIPTTWKWSYSGSSIVADVAYDTFLAETASGSSKYEIMVWLAALGGAGPISSTGSTIATPTIAGVNWKLYSGPNGDTTVYSFVADSTTESFSGDLNDFFTYLVDNEGVSDELYLTTLEAGTEPFTGSNAKLTVSEYSISIE | Function: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues. Specific for xyloglucan and does not hydrolyze other cell wall components.
Catalytic Activity: xyloglucan + H2O = xyloglucan oligosaccharides.
Sequence Mass (Da): 25159
S... |
A1CRJ0 | MKFNLALALSLTVATAEAATELCKQWDSIIEGNFIVYNNLWGQGNADDGGHQCTTVKSISGDTVVWSTEWAWSGGPGQVKSYANAALQFTPTTLSSVSSIDSTWKWRDSYTGSDIVANVAYDMFLSSSATGSEEYEIMVWLAALGGAGPISSTGSPIATPTINGVQWDLYLGPNGAMQVYSFVAPSSTENFAGDMKGFIDYLTSEQGLSKDLYLLDVQAGTEPFSGSDAVLTVSEYSVNLA | Function: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues. Specific for xyloglucan and does not hydrolyze other cell wall components (By similarity).
Catalytic Activity: xyloglucan + H2O = xyloglucan oligosaccharides.
Sequence Ma... |
Q8L794 | MLILRQFQISSFELFQSPKQTGFYSSSRSVPLPRTRFYSDFRVMSGNKGTNYEKLYLGMDFGTSGGRFTVIDEQGEIKAQGKREYPPFMKEESMGWASSWKATLFSLLEDIPVTVRSLVSSISLDGTSATTLILNSESGEVLCQPYLYNQSCPDALPEVKSIAPANHTVCSGTSTLCKLVSWWNTEVPNRESAVLLHQADWLLWLLHGRLGVSDYNNALKVGYDPESESYPSWLLGQPYSQLLPKVQAPGTSIGNLKESFTRQFGFPDDCIVCTGTTDSIAAFLAARATEPGKAVTSLGSTLAIKLLSTKRVDDARYGVY... | Function: Exhibits ATP hydrolysis without substrate. Can phosphorylate D-ribulose with low efficiency.
Catalytic Activity: ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+)
Sequence Mass (Da): 52468
Sequence Length: 478
Subcellular Location: Plastid
EC: 2.7.1.47
|
Q949W8 | MADLSLPPDSLFLGFDSSTQSMKATVLDSNLNIIKTELVHFDSDLPQYKTKDGVYRDTTVNGRIVSPTLMWVEAFDLILQKLSNANFDFAKVIAVSGSGQQHGSVYWSKGSSEVLRSLDSKRSLKEQLENAFSVKESPIWMDSSTTLQCKEIENAVGGAMELSKITGSRAYERFTGPQIRKLFMTQGEVYKSTERISLVSSFMASLLVGDYACIDETDAAGMNLMDIEKRCWSKAALEATATGLEEKLGKLAPAYATAGSISQYFVQRFGFEKNCVVVQWSGDNPNSLAGLTLSTPGDLAISLGTSDTVFGITKELQPSL... | Function: Mediates 1-deoxy-D-xylulose (DX) phosphorylation in the cytoplasm prior to the translocation of 1-deoxy-D-xylulose 5-phosphate into plastids. Can also phosphorylate D-xylulose (Xyl). Uses preferentially ATP as cosubstrate.
Catalytic Activity: ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+)
Sequence Mas... |
Q8EGP9 | MNKFLIIDGLNLVRRIYAAIPDENDMESLTERVSVACTKLLRIHHPTHVAVVWDGDEISWRKQLYPDYKKGRKPMPEPLAAGLIALQEHLQNLQIQSIYAAAEADDVIATLATKTAKAQGEALIVSTDKGFSQLNHPRISQWDHFNQQYLNIAELEQKLGVDRSQFLDLMALAGDSGNKIPGIPGIGPKSAAELLRTFRTLATLFSSLPNLGAKQAKKLAEGRDMARLSYKLVQLQTDLPLNINLRDFRVNSPTKASSNNL | Cofactor: Binds 2 Mg(2+) per subunit. Only one magnesium ion has a direct interaction with the protein, the other interactions are indirect.
Function: Has flap endonuclease activity. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA ... |
Q54G06 | MQRVLNKIISKDTINTMGKVAISKKVEKLRTFMKDQSLSAYIVPSEDAHQSEYICVKDKRREYISGFSGSAGCVVITLDNQLLWTDGRYWLQAEKELESNWKIMKDRVVGEPTIQDWLLSNLNKENKVGIDSRLISKGYYDSMKLVLKEKSIDIKFDEDGENLIDKVRESFKDEEEIPEYPKNSIFFLEDKFTGKQSNEKLKEIREEMKKQSADLMVVSALDEIAWLLNLRGSDISFNPVFLSYVVVEHEKVTLFVDESKLNDKTKSQLPSGIAISPYSSVFEYLRNSDKQGKKIWIDPRSSVALYNCVSISNLLEKINP... | Cofactor: Binds 2 manganese ions per subunit.
Function: Metalloaminopeptidase that catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro.
Catalytic Activity: Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or t... |
Q9NQW7 | MPPKVTSELLRQLRQAMRNSEYVTEPIQAYIIPSGDAHQSEYIAPCDCRRAFVSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDSNWTLMKMGLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLIPVKENLVDKIWTDRPERPCKPLLTLGLDYTGISWKDKVADLRLKMAERNVMWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLETIMLFIDGDRIDAPSVKEHLLLDLGLEAEYRIQVHPYKSILSELKALCADLSPREKVWVSDKASYAVSETIPKDHRCCMPYTPICIAKA... | Cofactor: Binds 2 manganese ions per subunit.
Function: Metalloaminopeptidase that catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro . Contributes to the degradation of bradykinin .
Catalytic Activity: Release of any N-terminal amino acid, including proline, that ... |
O43895 | MARAHWGCCPWLVLLCACAWGHTKPVDLGGQDVRNCSTNPPYLPVTVVNTTMSLTALRQQMQTQNLSAYIIPGTDAHMNEYIGQHDERRAWITGFTGSAGTAVVTMKKAAVWTDSRYWTQAERQMDCNWELHKEVGTTPIVTWLLTEIPAGGRVGFDPFLLSIDTWESYDLALQGSNRQLVSITTNLVDLVWGSERPPVPNQPIYALQEAFTGSTWQEKVSGVRSQMQKHQKVPTAVLLSALEETAWLFNLRASDIPYNPFFYSYTLLTDSSIRLFANKSRFSSETLSYLNSSCTGPMCVQIEDYSQVRDSIQAYSLGDV... | Function: Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin.
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Catalytic Activity: Release of any N-terminal am... |
B8YG19 | MRLGVALSTIAVLLTATSARNLDKRQWGWPNFGGGNGGNGGNGGKTINDYKREQGAGRDIHVYAPSNLAPNSPLLLSLHGMDQDPNYQQSNTHWETLADSEGFVVVYPRGGTGMSTWDIQGTKDTQWVSQIIDQMKKEYNIDTKRVYLSGFSMGGMFTYHAMSQIANKIAAFAPCSGPNVFGASKAQRPVPIFHVHGTNDDVLNYQQVEGFLKNYRDQFHCPSQADTKTNYPNRENPNATLYTWGPCDKGVYIKHLKLQGRGHSPSSADIQDIWDFVSQWTVDGPVSASGNGGGNTTPTNPSTGGNGNGNGGGNTTPTNP... | Function: Bifunctional acetylxylan esterase/xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades xylan from acetylxylan, beechwood, birchwood, and oat spelt, a... |
Q84H44 | MANDTRQVVQGVQEMTPSEAFVETMVANGVTEIFGIMGSAFMDAMDIFAPAGIKLIPVVHEQGAAHMADGFARVSGRTGVVIGQNGPGISNCVTAIAAAYWAHTPVVIVTPEAGTTGIGLGGFQEARQLPMFQEFTKYQGHVTHPARMAEYTARCFARARDEMGPAQLNIPRDYFYGKIKCEIPLPQPLDRGPGGAQSLDAAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLHNDSFPASHPLWCGPLGYQGSKAAMKLLADADVVLALGTRLGPFGTLPQHGLDYWPKNARIIQVDADSKMLGLVK... | Catalytic Activity: acetyl phosphate + H(+) + sulfite = phosphate + sulfoacetaldehyde
Sequence Mass (Da): 65108
Sequence Length: 598
Pathway: Organosulfur degradation; taurine degradation via aerobic pathway; acetyl phosphate and sulfite from taurine: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.3.15
|
Q93PS3 | MAKVKMTPSEAMTEVLVNEGVTHVTGILGSAFMDMLDLWPTAGIEFIAVRHEQTAGHMQDAYCRITGKASVCIGQNGPGVTNLVTCVAAANQAHTPMVVLGPSAGTPTVGWDGFQECDQVSIFRSITKQVLQVPHPSRAGDVLRTAFRIAYAERGPVYVDIPRNYFYGEVYEEILRPDQYRAMNVRGAGDATELARATEILAAAKNPVIISGRGVVDADAFAEVKEIAHMLTAPVAMSYLHNDTYPADDELWVGPIGYMGAKSAMYSLQDADVILAIGSRLSVFGTLPQYDINYFPENAKIIQIEVNPKQIGRRHPVTVP... | Catalytic Activity: acetyl phosphate + H(+) + sulfite = phosphate + sulfoacetaldehyde
Sequence Mass (Da): 63939
Sequence Length: 584
Pathway: Organosulfur degradation; taurine degradation via aerobic pathway; acetyl phosphate and sulfite from taurine: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.3.15
|
A3SR25 | MLFRASQPEDKPMKMTTEEAFVKTLQMHGIQHAFGIIGSAMMPISDIFGKAGITFWDCAHEGSGGMMADGYTRATGKMSMMIAQNGPGITNFVTAVKTAYWNHTPLLLVTPQAANKTMGQGGFQEVEQMAAFKDMVCYQEEVRDPTRMAEVLNRVILNAKRYSAPAQINVPRDYFTQVIDIELPKIVDFERPSGGEEALDEAAKLLSEAKFPVILNGAGVILAGAIPATAELAERLDAPVCCGYQHNDAFPGSHPLHAGPLGYNGSKAGMELISKADVVLALGTRLNPFSTLPGYGIDYWPKDAKIIQVDVKPERIGLTK... | Function: Catalyzes the degradation of sulfoacetaldehyde into sulfite and acetyl phosphate. Involved in sulfolactate degradation.
Catalytic Activity: acetyl phosphate + H(+) + sulfite = phosphate + sulfoacetaldehyde
Sequence Mass (Da): 65061
Sequence Length: 603
EC: 2.3.3.15
|
Q8PEW5 | MSNTVYIGAKEYFPGIGKIGFEGRDSDNPLAFKVYDANKTIGDKTMAEHLRFAVAYWHSFCGNGADPFGPGTRAYPWDVGDTALNRAEAKADAAFEFFTKLGVPYYCFHDIDLSPDADDITEYESNLKHMVGVAKQRQADTGIKLLWGTANLFSHPRYMNGASTNPDFNVVARAAVQVKAAIDATVALGGENYVFWGGREGYACLHNTQMKREQDNMARFLTLARDYGRSIGFKGNFLIEPKPMEPMKHQYDFDSATVIGFLRQHGLDQDFKLNIEANHATLSGHSFEHDLQVASDAGLLGSIDANRGNPQNGWDTDQFP... | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: alpha-D-xylose = alpha-D-xylulofuranose
Sequence Mass (Da): 48766
Sequence Length: 445
Subcellular Location: Cytoplasm
EC: 5.3.1.5
|
Q9FKK7 | MKKVEFFMLLLCFIAASSLVSADPPTCPADLGGKCSDSDDWQGDFFPEIPKIKYEGPSSKNPLAYRWYNAEEEILGKKMKDWFRFSVAFWHTFRGTGGDPFGAATKYWPWEDGTNSVSMAKRRMRANFEFLKKLGVDWWCFHDRDIAPDGTTLEESNKNLDEVIELAKELQKGSKIKPLWGTAQLFLHPRYMHGGATSSEVGVYAYAAAQVKKAMEVTHYLGGENYVFWGGREGYQTLLNTDMGRELDHLARFFEAAVAYKKKIGFKGTLLIEPKPQEPTKHQYDWDAATAANFLRKYGLIDEFKLNIECNHATLSGHTC... | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: alpha-D-xylose = alpha-D-xylulofuranose
Sequence Mass (Da): 53720
Sequence Length: 477
EC: 5.3.1.5
|
A2QTU5 | MYFSSFLALGALVQAAAATYFAPNSTGLRIQHGFETILIQPFGYDGFRVRAWPFRPPSGNEISFIYDPPIEGYEDTAHGMSYDTATTGTEPRTLRNGNIILRTTGWGGTTAGYRLSFYRVNDDGSETLLTNEYAPLKSLNPRYYYWPGPGAEFSAEFSFSATPDEQIYGTGTQQDHMINKKGSVIDMVNFNSYIPTPVFMSNKGYAFIWNMPAEGRMEFGTLRTRFTAASTTLVDYVIVAAQPGDYDTLQQRISALTGRAPAPPDFSLGYIQSKLRYENQTEVELLAQNFHDRNIPVSMIVIDYQSWAHQGDWALDPRLW... | Function: Catalyzes the liberation of alpha-xylose from the non-reducing terminal glucose of xyloglucan oligosaccharides.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.
Sequence Mass (Da): 82593
Sequence Length: 736
Subcellular Location: Secreted
EC: 3.2... |
P19148 | MNKYFENVSKIKYEGPKSNNPYSFKFYNPEEVIDGKTMEEHLRFSIAYWHTFTADGTDQFGKATMQRPWNHYTDPMDIAKARVEAAFEFFDKINAPYFCFHDRDIAPEGDTLRETNKNLDTIVAMIKDYLKTSKTKVLWGTANLFSNPRFVHGASTSCNADVFAYSAAQVKKALEITKELGGENYVFWGGREGYETLLNTDMEFELDNFARFLHMAVDYAKEIGFEGQFLIEPKPKEPTKHQYDFDVANVLAFLRKYDLDKYFKVNIEANHATLAFHDFQHELRYARINGVLGSIDANTGDMLLGWDTDQFPTDIRMTTL... | Cofactor: Binds 2 cobalt ions per subunit.
Catalytic Activity: alpha-D-xylose = alpha-D-xylulofuranose
Sequence Mass (Da): 50475
Sequence Length: 439
Subcellular Location: Cytoplasm
EC: 5.3.1.5
|
P46364 | SELKDIIAAVTPCKGADFELQALKIRQPQGDEVLVKXXATGM | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Oxidizes primary alcohols with an aromatic or cyclohex-1-ene ring. It is highly specific for benzyl alcohol.
Catalytic Activity: an aromatic primary alcohol + NAD(+) = an aromatic aldehyde + H(+) + NADH
Sequence Mass (Da): 4508
Sequence Length: 42
EC: 1.1.1.90
|
P12867 | MALVAGIDSSTQSCKVVIRDAETGALVRQGRASHPDGTEVHPDAWWSALQSAIEEAGGLDDVAAASVAGQQHGMVALDENGEVVRPALLWNDTRSAGAAADLIAELGGGEKWAEAVGIVPVASFTLTKLRWLARNEPANAAKVAAVCLPHDWLTWKLSGSTDIADIKTDRSDASGTLYWSAKTNEYRRDLLELGFGRDLVLPEVLGPTGIAGHLPNGAPLGPGAGDNAAAALGTGALPGDVIVSIGTSGTVFVSSDVAPVDGRGTVAGFADTTGRFLPIVVTLNAARVLDAAAKLLGVDHDELSRLALSAPAGADGMVLV... | Function: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate.
Catalytic Activity: ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+)
Sequence Mass (Da): 47866
Sequence Length: 466
EC: 2.7.1.17
|
P54271 | MALVAGIGQLDAVVQGGHSATPRPATGPAGPAAHSGRHQYDPDAWWARATGDSREAGGLGRTLAAASVAGQQQRHGALLESAVTVVRPALLWNDTRRPGAAADLIQELGGADKWAEAVGIVPVASLTLTNSGWLARHEPANAAKVAAICLPHDWLTWKLSGS | Function: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate.
Catalytic Activity: ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+)
Sequence Mass (Da): 16671
Sequence Length: 162
EC: 2.7.1.17
|
F4JG10 | MEKNTNTNHTSDDNNDKNHTNEEQEKIILNPNFEDGLNNWTGRACKIVLHESMDSGKIVPLSGKVFAAATQRKDTWNGIQQEISGRFRRKRVYEVTAVVRIFGNNVTSATVQATLWVLNANKREQYIVIANVQATDKNWVELKGKFVIHGSPSRVILYLEGPPPRADILLNSLVVQHAKRNRPSPPPFYENPGFGVNIVENSEVLDGGTKPWFTLGNCKLSVGQGAPRTLPPMARDTLGPHKPLGGNYIVVTNRTQTWMGPAQMITDKIKLFLTYQISAWVKLGVGVSGSSMSPQNVNIALSVDNQWVNGGQVEVTVGDT... | Function: Binds to and hydrolyzes insoluble and soluble xylan substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence Mass (Da): 84552
Sequence Length: 752
Domain: The GH10 domain binds to xylan.
Pathway: Glycan degradation; xylan degradation.
EC: 3.2.1.8
|
P23557 | MKQQYLLDYEATKASKNGMPVCKFDSCIPALQFCKENGIKMRGHVLVWHNQTPEWFFHKDYDVSKPLVDAATMERRLESYIKQVIEFCQKNYPGVVYCWDVVNEAILDDGSWREINNNWYTIMKEKYVEKAFYYARKYAKKDVALFYNDYNVFLPAKREAIYNLAQKLKEKGLIDGLGLQPTVGLNYPELDSDDIDSFKTTLETFAKLGLQIHITELNFEIKGDESNRTPENLKKQADRYYEMMKLLLKEDTDNGGPCNITCVTVFGICDDYPLYKNFKQCMYLWDKNCNPKPCFYSFLQAGLDWKASLLSK | Function: Could be a xylanase.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence Mass (Da): 36494
Sequence Length: 312
Pathway: Glycan degradation; xylan degradation.
EC: 3.2.1.8
|
G4NA54 | MVSFTTILVAATAALVAANPVPPSIDEMREIYVKSRDLHARGGTPSSTGTHDGFYYSWWTDNGAQATYTNNAGGSYSITWSGNGNLVGGKGWNPGSARNVTYSANYRPNGNSYLSVYGWTRNPLVEYYVVENFGTYDPSSQASRKGTINVDGATYQVAQSTRTNQPSIDGTRTFQQYWSVRQQKRSSGTVDMKKHFDAWASMGMKLGTHDYQIVATEGYFSSGSSTVTIQR | Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence ... |
Q84WT5 | MNSIKNGFFLCMIFLLWCHVDSGVSIDPFSHSHSLNTECVMKPPRSSETKGLLQFSRSLEDDSDEEWKIDGNGFIREMAQRIQLHQGNIYSFSAWVKLREGNDKKVGVVFRTENGRLVHGGEVRANQECWTLLKGGIVPDFSGPVDIFFESENRGAKISAHNVLLKQFSKEEWKLKQDQLIEKIRKSKVRFEVTYENKTAVKGVVISLKQTKSSFLLGCGMNFRILQSQGYRKWFASRFKITSFTNEMKWYATEKARGQENYTVADSMLKFAEDNGILVRGHTVLWDNPKMQPSWVKNIKDPNDVMNVTLNRINSVMKRY... | Function: Binds to and hydrolyzes insoluble and soluble xylan substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence Mass (Da): 64941
Sequence Length: 570
Domain: The GH10 domain binds to xylan.
Pathway: Glycan degradation; xylan degradation.
EC: 3.2.1.8
|
A0A1P8B8F8 | MKNINNGFFLCMLLLLWCFVHSGISIDPFSPSDSLKTECVMKPPRSSETKGLLQFSRSVEDDSDEEWKIDGSGSIREMTQRIQLHEGNIYSFSAWVKLREGNNKKVGVVFRTENGRFVHGGEVRAKKRCWTLLKGGIVPDVSGSVDIFFESDDKEAKISASDVSLKQFSKQEWKLKQDQLIEKIRKSKVRFEVTYQNKTAVKGAVISIEQTKPSFLLGCAMNFRILQSEGYRNWFASRFKITSFTNEMKWYTTEKERGHENYTAADSMLKFAEENGILVRGHTVLWDDPLMQPTWVPKIEDPNDLMNVTLNRINSVMTRY... | Function: Binds to and hydrolyzes insoluble and soluble xylan substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence Mass (Da): 64947
Sequence Length: 569
Domain: The GH10 domain binds to xylan.
Pathway: Glycan degradation; xylan degradation.
EC: 3.2.1.8
|
G4MLU0 | MTRLATLITLAGLLAVSPGAYAQRNRNDTGGSTGAEGLNSLAVKAGLLYFGTASDTRNFADEPYMSVVNNTNEFGMIVPENSMKWEATEKEPGRFSFANADRVRALTKANGQMLRCHALTWHSQLPNFVKTTAWTRDTLTAAIESHISNEVGHFAGDCYAWDVVNEAVNENGSFRDSPFHRTLGTDFLAISFRAAAAADPNAKLYYNDFNIETPGPKANAAMGIVRLLKEQGVRIDGVGFQGHLTVGSTPSRAQLASQLQRFADLGVEVTYTELDIRHKSLPVSSRAAQDQARDYVSVIGSCLDVTACVGVMVWQPTDKY... | Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Location ... |
I1S3C6 | MHFLGLVVAFAPAALAQSAIWGQCGGTGWSGSTTCQSGLKCEKINDFYYQCIPGSDNGGGTTPDPGTPSPGNGNADATGLDAKIRAKGKIYFGTEIDHYHLSNNPLINIVKKDFGQVTNENSMKWDAIEPSRGQFTFSNADKVVDFAQANGKKIRGHTLLWYSQLPQWVKNIRDRATMTSVIENHVKTVVTRYKGKILHWDVVNEIFAEDGNMRNSEFYQVLGEDFVGIAFRAARAADPAAKLYINDYNLDIANYAKVTRGMVDHVNKWVSQGIPIDGIGSQAHLAKPGGWNPASGFPAALKVLAGANVKEVAITELDID... | Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Plays an important role in causing fusarium head blight (FHB) on cereal crops.
Catalytic Ac... |
P45796 | MIRKCLVLFLSFALLLSVFPMLNVDAANRPLAKIPGNSNPLMDHKLGADPYSLVYDGRVYIFMSSDTYVYNKDGSIKENDFSALDRIQVISSTDMVNWTDHGTIPVAGANNKNSGRGIAKWASNSWAPAVAHKKINGRDKFFLYFANGGAGIGVLTADTPIGPWTDPLGKALVTHSTPGMAGVTWLFDPAVLVDDDGTGYLYSGGGIPNESDPASIANPKTARVIKLGADMTSVIGSATTIDAPYLFEDSGIHKYNGKYYYSYCINFAGTHPQQYPAGEIGYMVSDNPMGPFTYKGHFLKNPYTFFGVGGNNHHAVFNFK... | Function: Cleaves arabinose units from O-2- or O-3-monosubstituted xylose residues, thereby assisting in arabinoxylan (AX) and short-chain arabinoxylo-oligosaccharide (AXOS) degradation (By similarity). Preferres wheat flour xylan over oat spelt xylan as substrate. Does not display endoxylanase activity.
Catalytic Acti... |
Q53317 | MKKSIFKRYAAAVGLMASVLMFTAVPTTSNAADDQKTGKVGGFDWEMWNQNYTGTVSMNPGAGSFTCSWSGIENFLARMGKNYDDQKKNYKAFGDIVLTYDVEYTPRGNSYMCIYGWTRNPLMEYYIVEGWGDWEPPGNDGVDNFGTTTIDGKTYKIRKSMRYNQPSIEGTKTFPQYWSVRTTSGSRNNTTNYMKDQVSVTKHFDAWSKAGLDMSGTLYEVSLNIEGYRSNGSANVKSISFDGGIDIPDPEPIKPDENGYYLKENFESGEGNWSGRGSAKVKSSSGYDGTKGIFVSGREDTWNGASINLDELTFKAGETY... | Function: Contains two catalytic domains with xylanase and endo-beta-1,3-1,4 glucanase activities.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence Mass (Da): 89091
Sequence Length: 802
Pathway: Glycan degradation; xylan degradation.
|
Q5ZNB1 | MTLVKSILLALAAGHVAQAQLNTAAKAAGLLYFGTAVDNPDLSDSKYLVNLETADFGQITPANAMKWQPTEPSQGSYTFTQGDQIASLAKSNNDYLRCHNLVWYNQLPSYITSGSWTNATLIAALKEHINGVVTHYKGQCYAWDVVNEALNEDGTYRQNVFYQHIGEAYIPIAFAAAAAADPNAKLYYNDYNIEYAGAKATGAQGIVKLIQAAGGRIDGVGLQSHFIVGQTPSLATQKANMAAFTALGVDVAITELDIRMTLPDTSALQTQQSTDYQTTTTACVQTKGCVGITLWDYTDKYSWVPGTFSGQGDACPWDSN... | Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Shows an endo-mode of action on xylan forming mainly xylobiose and short-chain xylooligosac... |
O94163 | MVHLKALASGTLFASLASSAVISRQAAASINDAFVAHGKKYFGTCSDQALLQNSQNEAIVRADFGQLTPENSMKWDALEPSQGSFSFAGADFLADYAKTNNKLVRGHTLVWHSQLPSWVQGITDKDTLTEVIKNHITTIMQRYKGQIYAWDVVNEIFDEDGTLRDSVFSQVLGEDFVRIAFETAREADPNAKLYINDYNLDSADYAKTKGMVSYVKKWLDAGVPIDGIGSQSHYSANGFPVSGAKGALTALASTGVSEVAVTELDIEGASSESYLEVVNACLDVSSCVGITVWGVSDKDSWRSSTSPLLFDSNYQAKDAY... | Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence ... |
Q96VB6 | MVHLKSLAGILLYTSLCIASSQQAPASINNAFVAKGKKYFGTCADQGTLSDGTNSGIIKADFGQLTPENSMKWDATEPSQGKFSFSGADYLVNYAATNNKLIRGHTLVWHSQLPSWVQGITDKNTLTSVLKNHITTVMNRYKGKVYAWDVVNEIFNEDGTLRSSVFYNVLGEDFVRIAFETARAADPQAKLYINDYNLDSANYGKTTGLANHVKKWIAQGIPIDGIGSQTHLSAGGSSGVKGALNTLAASGVSEVAITELDIAGASSNDYVNVVEACLEVSKCVGITVWGVSDKNSWRSAESPLLFDGNYQPKSAYNAIL... | Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence ... |
Q6PRW6 | MIPNITQLKTAALVMLFAGQALSGPVESRQASESIDAKFKAHGKKYLGNIADQGTLNGNPKTPAIIKANFGQLSPENSMKWDATEPSQGQFSFAGSDYFVEFAETNGKLIRGHTLVWHSQLPSWVSSITDKTTLTDVMKNHITTVMKQYKGKVYAWDVVNEIFEEDGTLRDSVFSRVLGEDFVRIAFETAREADPEAKLYINDYNLDSATSAKLQGMVSHVKKWIAAGVPIDGIGSQTHLGAGAGAAASGALNALASAGTEEVAVTELDIAGASSTDYVDVVNACLDQPKCVGITVWGVADPDSWRADESPLLFDASYNP... | Function: Cold active endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylan... |
O97402 | MQFLIPVVILCVSLVDSQKVLYNNEIGFNNGFYYAFWKDSGSATFTLESGGRYAGNWTTSTNNWVGGKGWNPGNSWRTVNYSGYYGINEYANSYLSLYGWTTNPLIEYYVVESYGSYSPLNCPGGTDEGSFTSGGATYQVRKCRRTNAPSIIGTQSFDQYFSVRTPKKGFGQVSGSVNFADHVQYWASKGLPLGTHAHQIFATEGYQSSGFADITVS | Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence Mass (Da): 23942
Sequence Length: 217
Pathway: Glycan degradation; xylan degradation.
Subcellular Location: Secreted
EC: 3.2.1.8
|
Q9ZBU1 | MSDITVTNWAGNITYTAKELLRPHSLDALRALVADSARVRVLGSGHSFNEIAEPGDGGVLLSLAGLPSVVDVDTAARTVRVGGGVRYAELARVVHARGLALPNMASLPHISVAGSVATGTHGSGVGNGSLASVVREVELVTADGSTVVIARGDERFGGAVTSLGALGVVTSLTLDLEPAYEMEQHVFTELPLAGLDPATFETVMAAAYSVSLFTDWRAPGFRQVWLKRRTDRPLDGFPYAAPAAEKMHPVPGMPAVNCTEQFGVPGPWHERLPHFRAEFTPSSGAELQSEYLMPREHALAALHAMDAIRETLAPVLQTCE... | Cofactor: Binds 1 FAD covalently per subunit.
Function: Oxidase that performs selective oxidation of the terminal primary hydroxyl group of several alditols, with a reduction of O2 to H2O2. Shows highest activity on xylitol and D-sorbitol, and a poor efficiency with D-mannitol and L-threitol.
Catalytic Activity: an ald... |
Q6YRJ4 | MPKPLIIFKDFSFQYYSQQTPTLNQINLTIYEGQKVLIVGKNGSGKSTFLKCINGLIPHSYQGKITGTAIIKDKVLTQTNIFDLSLDVGTIMQDTDNQFVGLTVAEDIAFALENDDLPQSEIYQKVNMWAQDLGLQSFLDYKPQELSEGHKQLASMAGVLIYNPSILLFDESLSNLDPVSRAKMTALIKTIHQKYHSTILVIEHYLEDILDDSFDRVIVFEDEKIIYDNSPQKLILENILTKQGIQEPTYISALKKVGINLGSLPYLLNLPALQSLDFVQYFSNQLTNLKKCAISQNDPTQLLPFFPKQFAPFCPILQLQ... | Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66174
Sequence Length: 588
Subcellular Location: Cell membrane
EC: 7.-.-.-
|
Q9RVK3 | MIDPRYPLGPMPQPRDLSDDERQEARAALRALPGELRAAVAGLSEPQLDTPYREGGWTVRQVVHHVADRHLNAYVHTARVLSGGEALAQPAHEEAWAALPASSFATELSLLLLERLHIHWDEVLADVTDWQQAGLRPDGSEWTLDGLLGQAAWHGRHHTAHITRLREREGW | Cofactor: Binds 1 zinc ion per subunit.
Function: Possible metal-dependent hydrolase.
Sequence Mass (Da): 19138
Sequence Length: 171
Subcellular Location: Cytoplasm
EC: 3.-.-.-
|
Q9RVK2 | MEHDERTHVPVELRAAGVVLLNERGDILLVQEKGIPGHPEKAGLWHIPSGAVEDGENPQDAAVREACEETGLRVRPVKFLGAYLGRFPDGVLILRHVWLAEPEPGQTLAPAFTDEIAEASFVSREDFAQLYAAGQIRMYQTKLFYADALREKGFPALPV | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Hydrolase that can act as a nucleoside triphosphatase and a dinucleoside polyphosphate pyrophosphatase. The best substrates are 8-oxo-dGTP and 8-oxo-GTP. Other substrates include Ap4A, dGTP and GTP. May be involved in protection from damage caused by radiation.
Catal... |
Q57571 | MREIMKILIITGKLAERKVKDAVKKYDFIDVHVANISVAAFLTPNLIIKEIKKLENKLGKKLKDIYDFVLVTGLIRHDLKNVEEETGIKCFKSTREASDIPILIENLDKIKLSTKEYADLQLLEIIRKKCEEEIKKAEEQELGEGDIKIGKLKVGDKFPMRVLGEIVHAPWLKEKELEEKIIYYLESGADMIDLGMVSNENNADKIKDMLKIARDLTDNPISVDTLNTKELIEAINLGADMILSVDAGNLDELIPYLKDSETAVVVLPTNYKTNYVPETIEGKIKSLEENIKKLIDAGIEKIVADPILEPINNAGCSFIE... | Function: Unknown. Does not possess dihydropteroate synthase (DHPS) activity since it does not catalyze the condensation of 6-hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4-aminobenzoate to form 7,8-dihydropteroate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59645
Sequence Length: 52... |
Q54F34 | MAGSLDDSIYNNGRSGGGGGGFKFSKGFNKDSISKRIIMMLFFSKGIRAWSCIILLYFLQSSISIISASFYMCLFSAIFSVVVEKPWNLLSSLRPSQIKKIIYHSIFNLLIIITWNSSIKFIGPIGSILASDYTFSTYPLIFNSLLQGNFLATDMSRGSIMLMIGYFLIPLFGISNRLDILGYTSSQVFMIGLFSLIVHNVLVLWKKTIVRSWNSGSSGGKNKLSSLGSCVSTIILFVFKLFEGFSSGSSGSDSINQVSYSQLFVIAIITFILYSLNQFIDDVSEKELTFNVLSKVSLTSSVIFGLLAALFIGFKDFFHP... | Function: May be involved in zinc transport from the cytoplasm to either intracellular organelles or extracellular spaces.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85330
Sequence Length: 770
Subcellular Location: Membrane
|
O27262 | MVIIHSPSYDLHNHEGHVENSGRTRAILRAIESSDLSPRFVEPGMAGIDDILMVHSSTHVEYLEVFAGRGGGWLDYDTYMTPESFSVARLSAGGAMLAAEEALRDGWSYSLGRPPGHHATYDRSMGFCIFNNIAIAIEHARRNLGVSRPLVLDFDVHHGNGTSSIFYRDRDVMYISIHQDPRTLFPGTGFIDETGSGEGEGFNLNIPMPRGSGNREYLWILGMILPAVLEGFRPDMIFVSAGFDAHRRDPLAEIMVDEEFFSWIGWFIHQTGLPCTAVLEGGYDPEALGRSNIAFMRGLDGEEYEPETAAPGGVSEIFSQ... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable deacetylase.
Sequence Mass (Da): 36722
Sequence Length: 331
EC: 3.5.1.-
|
O58967 | MRRISPTRFLLYIVLIFLAAWYLLPIWSAITTSTKTGEQVALTTPVQFVFPPTFDPYREAFRELKRPILNSLIFTTFATIFSTILGSIAGFTIAKLVRGRVSRQLLALISFGIFLPYQSILIPLVKIISSLGLYNRILGLILTHTAYGIPITTLLFTNYYYEIPDELVEAAKIDGADPWKIYTKVILPLSKAPFVVTGIYQFTNIWNDYLFGVVLTRGEEAMPATVKLANLKGSFVANWNIQMAGALIVALPTLLIMIALGKYLIRGYTSGALKG | Function: Probably part of a binding-protein-dependent transport system PH1214/15/16. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30683
Sequence Length: 275
Subcellular Location: Cell membrane
|
P45114 | MKKAIKLNLITLGLINTIGMTITQAQAEETLGQIDVVEKVISNDKKPFTEAKAKSTRENVFKETQTIDQVIRSIPGAFTQQDKGSGVVSVNIRGENGLGRVNTMVDGVTQTFYSTALDSGQSGGSSQFGAAIDPNFIAGVDVNKSNFSGASGINALAGSANFRTLGVNDVITDDKPFGIILKGMTGSNATKSNFMTMAAGRKWLDNGGYVGVVYGYSQREVSQDYRIGGGERLASLGQDILAKEKEAYFRNAGYILNPEGQWTPDLSKKHWSCNKPDYQKNGDCSYYRIGSAAKTRREILQELLTNGKKPKDIEKLQKGN... | Function: Probable receptor, TonB-dependent.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 102768
Sequence Length: 913
Subcellular Location: Cell outer membrane
|
Q57251 | MLSFILSIFPIVLLIYLMVKRNALPSYVALPWVATLVMGVHLLHFNTDIVTISANVVSAIIAVQTPITVIFGAILFNRFSEISGATNIMRKWLGNINPNPVAQLMIIGWAFAFMIEGASGFGTPAAIAAPILVGLGFHPLKVAMLALIMNSVPVSFGAVGTPTWFGFGALKLSEDMILEIGSITAFIHSIAALIIPLLALRILVNWDDIRKNIVFIYISVLGCVVPYFLIAQVNYEFPSLVGGAIGLFISVWAANRNIGLAKVTNTLDNNAVSAGEVVKALFPTGLLIAFLIVTRIHQLPFKAMMNDATIWFSTTLGSLG... | Function: May play a role in L-lactate transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56885
Sequence Length: 532
Subcellular Location: Cell inner membrane
|
Q57223 | MKVYKSFLIATASLFLFACSSFQNDDYAMNYKGQIGEPIMAIAMLSEQQHEWAGTPYVLGGVSRRGVDCSGFVQKTFFDRFNLRLPRSTVEQANYGKHVRKEDIQTGDLIFFKTGRGPNGYHVGIYVKEDKFLHASTRGGVVYSSMNNPYWSKAFWQVRRI | Location Topology: Lipid-anchor
Sequence Mass (Da): 18388
Sequence Length: 161
Subcellular Location: Cell membrane
EC: 3.4.-.-
|
Q58774 | MKTLSEIKEILRKHKKILKDKYKVKSIALFGSYARGEQTEESDIDIMVEFDENNYPSFSEYLELIEYLEKILGLKVDLITKKSIHNPYVKKSIEEDLIYV | Cofactor: Binds 2 Mg(2+) ions.
Function: Probable antitoxin component of a putative type VII toxin-antitoxin (TA) system. Neutralizes cognate toxic MJ1380 by di-AMPylation.
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 11819
Sequence Length: 100
EC... |
P45268 | MEIISQYGSWLVWITAVFGFFMAFGIGANDVSNSMGTSVGSGTITAKQAIIIALIFESAGAYLAGGEVTQTIKSGVIEPIQFVDTPDILALGMLSTLFASGAWLFIATKMGWPVSGTHTIIGAIIGFACITIGPSSVDWSKIGSIVGSWFVTPVIAGILAYAIFASTQKLIFDTEQPLKNAQKYGPYYMGITVFVLCIVTMKKGLKHVGLNLSNSETLIISLAISLIGMFFFHFYFKSKIFTQSANKGTFGAVEKVFSILMLLTACAMAFAHGSNDVANAIGPLSAVVSIVNEGGKIVSGGALTWWILPLGALGIAVGLI... | Function: Potential transporter for phosphate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44026
Sequence Length: 420
Subcellular Location: Cell inner membrane
|
Q9HPH7 | MIETTTLRFSHGDTTVLDGVDFTAETGDVTVLFGRNGAGKSTLLRHFNGLLEPDAGTVSVGGTPIAYDDDSLTELRLRVGLIFQNPDDQLVAPTVQQDIAFGPRNAGIEDTDRIEDVVSTFDLSEQAERLCNTLSGGEKKRVSLAGVLAMDPEYVLLDEPTAGLDGAGCRTIVEFVSSLAADGITTVIATHDVGFGLTVADTVTVLEDGVIDYRGDTLSQSLAAEYDLRSYVFDDWSDVSVE | Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25844
Sequence Length: 242
Subcellular Location: Cell membrane
EC: 7.-.-.-
|
Q59026 | MLNTLMLREWLRSMLRSCISKIFGDLMLISHISLSDKITLLTYGCNFKCKYCFFKPLSCKKYSVDEILNKILEVNENYKLDKILIAGGEPTLQNDLSELTKLLKDEGFYLMLSTNGYYLKDMLDKLEVDEIHIDLKAYDENKHIYLTSCSNKKVLDCISYIGKYRDEFNFKVEIDTVLIPNIVDLDEIEKIAKFLSNWDLPYRITGYVKYNNNLNAEKPDEDKILKAKEIALKYLSNVSCSLDFKRHKKSKKVII | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalytic Activity: glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+) + L-methionine + semiquinone [flavodoxin]
Sequence... |
C0LGH8 | MRSKYFCSLALVLGLFFVSCDGFASNEVQALRRFKEAIYEDPLLVMSNWNDPNSDPCDWTGIYCSPSKDHVIKINISASSIKGFLAPELGQITYLQELILHGNILIGTIPKEIGNLKNLKILDLGNNHLMGPIPAEIGSLSGIMIINLQSNGLTGKLPAELGNLKYLRELHIDRNRLQGSLLVAGASGYQSKVYSSNSSANIAGLCKSLKVADFSYNFFVGNIPKCLENLPRTSFQGNCMQNKDLKHRSSSQCANAQLVKTHGSPSAAPKHQSAQMVAKHHRASKPKWLLALEIVTGSMVGLLLLVALFSAVHRWNNRST... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 73910
Sequence Length: 664
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q8XJR2 | MYIIFALLAFSALILVHELGHFIVAKLNGIYVEEFAIGMGPKLFGVKVGETEYNLRILPFGGFVKMLGEEDESDDSRSLNAKTPIQRILVMGAGAFMNYVLALIIFIGLAMSSGFAENKVASVVPNSPAQEIGIEQGDEFLKIDGNKIHTTDDFRMGLALAKGNPVELEIKRGNDVLTKTVQPILNESGMYQVGISYALVEKPTLLQGIKQGFNETRSLVSQSFIALKTIVTGEANLKTDVGGPVTIIKMSGQAAKAGANTLLWFMAFLSVQLAVFNLLPFPALDGGRIFIELIQMIIRKEIPAKYIEAVNTVGFMLLMG... | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36491
Sequence Length: 335
Subcellular Location: Cell membrane
EC: 3.4.24.-
|
Q8TYV9 | MTHEYPDGTCAVCGLSLRVKEGESVVVLGPNGSGKTTLLHHILGLLTPTKGHIRVLGHDLPDGVREVRKRIGVVFQDVDDQLIMPTVLEDVAFGLVNRGMPREEAFERAREILERLGIEDLEDRPPQFLSGGQKRLVALAGAVAPEPDLLILDEPTSGLDFRATRLFVRLIRELKEELGFTMILTTFDVDIAAALAERVVVIREGKTVAEGSPEDILTDVDLIRESGLKPPEHVELLRRLGIENPPLDISEAEELLVAMLGEESRGNP | Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29422
Sequence Length: 268
Subcellular Location: Cell membrane
EC: 7.-.-.-
|
Q0V7T5 | MCLLRHLLPIWVLLGFFFFSTATKSQESSVVYVSGASPEIPISQASPRMGAQSPGPPIVKVVLRQDLNKKILIALIVSSSLLCVTVMFLVYLLLWRYRNMKNSFTGIKRKSDSVKSVTTKPTVHKIDSVRKGTIPVYEYQLLESATNKFSDSNVLSRGGRGCLYRACLDEKSSVTVKKLDGGGETDIEKQFETEVDWLAKIRHQNIVSLLGFCVYRQTSCIVYELMQNGSLESQLHGPSQGSGLTWQLRMKIAVDIARGLEYLHEHCHPPVVHRDLKSSSILLDSDFNAKISDFGFATVLTTQNKNLIHKASEDLLDGKV... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 47373
Sequence Length: 427
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q86JM5 | METIQSVITEWSDSKSWDHLFQHNFKDSNWSELFDPVNFKFKFGTTPFSQFQILPSVISLYLVIIFSIKFLMRNRKPFSLKYVSILHNAILCIWSLVMCVGILYEVIKRITAEGPLFTVCETVSGFDKGPAYYWSYIFYISKFYELLDTVIIVLKKKPLIFLHVYHHCIVVWLCWYFMYSGWNLQLWVVFLNTFVHVFMYYFYFQTGRGKTVWWKKYITMIQIIQFICLGIAGLLHSAAINLNSSPCFTHYPAFISAYLINFSFLFLFSQFFVKSYSNKPTSSSSTTTPTKTKKID | Function: Could be implicated in synthesis of very long chain fatty acids.
Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34929
Sequence Length: 296
Subcellular Location: Membrane
EC: 2.... |
O22891 | MATETNKELFVGGFAKILKEQRQVDVRLKAGDSGDEGASTSAHKLVLSARSEVFKKMLESDEIKASAQLETITLCEMKHEELEAFIEFIYSDGSMLSAKEKQHVRSLYIAGDKYEIPHLRDLCRIELISSLKSSNALDILELAQIPFDKALHDSAFFFFFFFFFG | Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence Mass (Da): 18683
Sequence Length: 165
Domain: The BTB/POZ domain mediates the interaction with some component ... |
C0LGK4 | MVDQRRSALGFVLLLLCLVLFFDCVVVGQTQSRFSEKLILLNLRSSLGLRGTDWPIKGDPCVDWRGIQCENGSIIGINISGFRRTRIGKLNPQFSVDPLRNLTRLSYFNASGLALPGTIPEWFGVSLLALEVLDLSSCSVNGVVPFTLGNLTSLRTLNLSQNSLTSLVPSSLGQLLNLSQLDLSRNSFTGVLPQSFSSLKNLLTLDVSSNYLTGPIPPGLGALSKLIHLNFSSNSFSSPIPSELGDLVNLVDFDLSINSLSGSVPQELRKLSKLQLMAIGDNLLSGTLPVDLFSAESQLQTLVLRENGFSGSLPDVCWSL... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 99704
Sequence Length: 915
Subcellular Location: Membrane
EC: 2.7.11.1
|
C0LGL4 | MEGRRQRLLVFIFGALAITHLVQAQPPDQRGFISLDCGLPVNESPYTDPRTGLTFSSDADFILSGLRGEAGDDNTYIYRQYKDLRYFPDGIRNCYNLKVEQGINYLIRAGFGYGNYDGLNVYPKFDLHVGPNMWIAVDLEFGKDREIIYMTTSNLLQICLVKTGSTIPMISTLELRPLRNDSYLTQFGPLDLIYRRAYSSNSTGFIRYPDDIFDRKWDRYNEFETDVNTTLNVRSSSPFQVPEAVSRMGITPENASLPLRFYVSLDDDSDKVNVYFHFAEIQALRGNETREFDIELEEDIIQSAYSPTMLQSDTKYNLSP... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 98965
Sequence Length: 880
Subcellular Location: Membrane
EC: 2.7.11.1
|
Q9KXJ6 | MIRFEDVSVTYDGATEPTVRAVDFEVPEGELVLLAGPSGVGKSTVLGAVGGLVPHFTGGTLRGRVTVAGRDTRTHKPRELADVVGTVGQDPLSHFVTDTVEDELAYGMESLGLPPDVMRRRVEETLDLLGLSDLRSRPIATLSGGQQQRVAIGSVLTPHPDVLVLDEPTSALDPAAAEEVLAVLQRLVHDLGTTVLMAEHRLERVIQYADQVVLLPAPGEAPLIGAPAEVMAVSPVYPPVVGLGRLAGWSPLPLTIRNARRRAAPLRERLAGREIPDHTPPPSAPLPAPPAPRPVTSRWRRRGKRPENPSAPTPYAAEVR... | Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59587
Sequence Length: 563
Subcellular Location: Cell membrane
EC: 7.-.-.-
|
O30238 | MRRERYLEKIEYIVEALSEIPERVKTPIEVSGVFYNLLTSIESAMDISAMLVKDLGGRVEDDYSNVEMLKELGIIDEELAEGLKKCNGLRNWLVHRYNRVDKELVLSSVEEVKALLLKFIQRVEDVLEKIEP | Function: Probable toxic component of a putative type VII toxin-antitoxin (TA) system, probably an RNase. Probably neutralized by cognate antitoxin AF_2432. Neutralization may be due to AMPylation by AF_2432.
PTM: Modified by cognate antitoxin AF_2432; probably at least 2 successive AMPylation events occur on Tyr-97.
S... |
Q7A342 | MTEPIISFKDFSFQYHSQATPTLQNINVDIYPGEKVLVVGASGSGKSTFANCINGLIPFKTKGNITGELYINNQDATVSCLHDRSNVVGTVLQDTDGQFIGLTAAEDMAFLLENNCVEQDDMKKNVSYWAEKVGMIEHLNHRPQDLSGGQKQRVSLGGILIHRTPILILDEPLANLDPATGHETLRLLNNIHEETKSTMIIVEHRLEESLDDTFDRVLLFKDGKIIANTTPSDLLKSSKLKEAGIREPLYCTALKYAEVDVESIDNLANLRDVCMSEHVKFKVKKWIDETSANNDNKYKSEPLLELNEVCVQYSDYSNSV... | Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 64158
Sequence Length: 570
Subcellular Location: Cell membrane
EC: 7.-.-.-
|
P9WL78 | MRWARQAVAVNGMPVDDGALPGLQRIGLVRSVRAPQFDGITFHEVLCKSALNKVPNAAALPFRYTVNGYRGCSHACRYCFARPTHEYLDFNPGTDFDTQVVVKTNVAAVLRHELRRPSWRRETVALGTNTDPYQRAEGRYALMPGIIGALAASGTPLSILTKGTLLRRDLPLIAEAAQQVPVSVAVSLAVGDPELHRDVESGTPTPQARLALITAIRAAGLDCHVMVAPVLPQLTDSGEHLDQLLGQIAAAGATGVTVFGLHLRGSTRGWFMCWLARAHPELVSRYRELYRRGPYLPPSYREMLRERVAPLIAKYRLAGD... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37176
Sequence Length: 340
Subcellular Location: Cell membrane
|
O82343 | MRGSNNTDLFDPKTEMDSNFSRHGSSSEGDFGFAFNDSNFSDRLLRIEILGGPSDSRSDAEGCTSIADWARHRKRRREDNKKDNGVAISDIVACAEEQILTDNNQPDMDDAPGGDNLDDEGEAMVEEALSGDDDASSEPNWGIDCSTVVRVKELHISSPILAAKSPFFYKLFSNGMRESEQRHVTLRISAQEEGALMELLNFMYSNSLSVTTAPALLDVLMAADKFEVASCMRYCSRLLRNMPMTPDSALLYLELPSSVLMAEAVQPLTDAAKQFLASRYKDITKFHDEVMALPLAGIEAILSSDDLQIASEDAVYDFVL... | Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence Mass (Da): 63037
Sequence Length: 561
Domain: The BTB/POZ domain mediates the interaction with some component ... |
P77868 | MLDLTPQSKKISIQIGGMTCQSCANRIEKVLNKKPFVQQAGVNFAAEEAQVVFDATQASEAQIIEIIHKTGFSAHIKQANELPIEENTSIPWRLIVLWIINIPFLIGMLGMIGGSHNLMLPPIWQFALASIVQLWLAIPFYRGAIGSIRGGLTNMDVLVSTGTLTIYLYSAFMLFYHANHAMGHVYFEASVMVIGFVSLGKFLEDRTKKHSLNSLSMLLQLTPKKVTVLRNEKWIEIALDQVNIGEIIRANQGERIAADGVIESGNGWCDESHLTGESRPEEKQKGGKVLAGAMVTEGSIIYRANQLGSQTLLGDMMNAL... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 78072
Sequence Length: 722
Subcellular Location: Cell membrane
EC: 7.2.2.-
|
P9WKA9 | MAQLTALDAGFLKSRDPERHPGLAIGAVAVVNGAAPSYDQLKTVLTERIKSIPRCTQVLATEWIDYPGFDLTQHVRRVALPRPGDEAELFRAIALALERPLDPDRPLWECWIIEGLNGNRWAILIKIHHCMAGAMSAAHLLARLCDDADGSAFANNVDIKQIPPYGDARSWAETLWRMSVSIAGAVCTAAARAVSWPAVTSPAGPVTTRRRYQAVRVPRDAVDAVCHKFGVTANDVALAAITEGFRTVLLHRGQQPRADSLRTLEKTDGSSAMLPYLPVEYDDPVRRLRTVHNRSQQSGRRQPDSLSDYTPLMLCAKMIH... | Function: Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for storage lipid synthesis.
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Mass (Da): 48847
Sequence Length: 446
Pa... |
Q576D9 | MNARLTGLGLNLLSFAVGIGGWYLLTATGAVVLPGPVDVLERAVTLLLNGQLVGDIFASLRRVLSGFVLGVALAIPVGFLMGWYRIARSLIEPWVQFFRMIPPLAVIPLAIVTLGIDESPKIFVIFLASFLSSVVATYQGVISVDRTLINAARVLGAKDATIFARVIVPASVPFILVGVRIGLGSAWATVVAAELIAAQSGLGYRMQQAQLYYDLPTIFVSLVTIGILGLFMDRLLQAADRRLTQWQERA | Function: Probably part of an ABC transporter complex. Probably responsible for the translocation of the substrate across the membrane (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26895
Sequence Length: 250
Subcellular Location: Cell inner membrane
|
Q9FYC8 | MSPVAKVSEFHREGNDWFCKTGLSSDITVVVDDVKFHLHKFPLVSKCGKLARMYEDSKSTDKQSLWTTVLEEFPGGADNFLIVARFCYGARVDITSKNLVSIHCAAEYLEMTNEYGEDNLISQVETFLHKHVLRNWKDCILALQSSSPVLKSAEKLQMIPKLMNAVSTMVCTDPSLFGWPMMMYGTLQSPGGSILWNGINTGARMRSSGSDWWYEDISYLSVDLFKRLIKTMETKGIRAESLAGAMMYYARKYLPGLGRWQSGTSDSSKSRRRVVSFNLAKASSPSSMPPLDQIALLETILSLLPEKRGRSFCKFLLGLL... | Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence Mass (Da): 72965
Sequence Length: 651
Domain: The BTB/POZ domain mediates the interaction with some component ... |
Q54QU8 | MENFKNNELESSPIINKNNSSHSINNEDNNYYSHNLEHNDNNNNDNNNTITNSHINNHDHKHNHEHEHKHKHNHDHNHDHDHNHEEEYGHGNELEHNNDQEHNVGNKNLLTNNNNQSKKKKHGHSHGGGEDGSSSGGGGGRHGHGHSHGGGSGSDHNHGSSDEDDEESKPLNQLRNLDSKKKARYSLILALTLTTIFMVGEIVGGYFANSLAIMTDAAHLLTDIGAMFLSLFAMWISQHPPTSSMSFGFHRAEILGALVSVLMIWALTGVLVYEAIQRILYPPDAVDGKIMFIIASCGLFINIIDAIILHWGSGGHGHSH... | Function: May be involved in zinc transport from the cytoplasm to either intracellular organelles or extracellular spaces.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59836
Sequence Length: 543
Subcellular Location: Membrane
|
Q9T020 | MEIRKKPNIFTVLVIDFSSKPSMALLLAILLFLSGPSASAVAAAAVGPATGFKPADDILIDCGSKSSSKTPDGRVFKSDQETIQYIEAKEDIQVSAPPSDKVASPIYLTARIFREEATYKFHLTRPGWHWVRLHFLAFPNDKFDLQQATFSVLTEKYVLLHNFKISNNNNDSQAAVQKEYLVNMTDAQFALRFRPMKSSAAFINAIEVVSAPDELISDSGTALFPVIGFSGLSDYAYQSVYRVNVGGPLIMPQNDTLGRTWIPDKEFLKDENLAKDVKTTPSAIKYPPEVTPLIAPQTVYATAVEMANSLTIDPNFNVSW... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 96505
Sequence Length: 878
Subcellular Location: Membrane
EC: 2.7.11.-
|
Q97SA3 | MKEAIIEWKDFSFRYETQQEPTLQGIDLTIYKGEKVLIVGPSGSGKSTLGQCLNGIIPNIYKGQTYGEFLIKGQVAFDMSIYDKSHLVSTVLQDTDGQFIGLSVAEDLAFALENDVTALDEMKGRVYKWAEKLDLLPLLDQRPQDLSGGQKQRVSLAGVLIDESPILLFDEPLANLDPKSGQDIIELIDQIHKEEGTTTLIIEHRLEDVLHRPVDRIVLINDGRILFNGSPDQLLATDLLTQNGIREPLYLTTLRQLGVDLVKEEQLANLDNLSISKGQVQLQNELAKETPALQSLFRLEEVSFSYDDRPILKSLHLDIK... | Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 62873
Sequence Length: 560
Subcellular Location: Cell membrane
EC: 7.-.-.-
|
Q92IC3 | MSKSKAIENNGISNTNSPNGKYMAPRPEGVKPTCVVITYSVSKDIKAVREVLDERGASVHYIIDKDGTQKEYHNDLTDQAFYAGKSSWKGEVGVNKFGIGVMLINDAKSDFPAEQIGKLKEFLKDVTERYPNLDLKHDLVGLGEVTVNREGNAHIAPGSKFPWKELAEAGFGRYFETTQEQKSKLLLSLDSTGEKVNTLQENLKEYGYGVESTSTFDQFTQQAVRVFNDRYGTGLPNEEPPVSWTEAGQDVLSQLLGQTVLEQTENA | Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 29592
Sequence Length: 267
Subcellular Location: Secreted
EC: 3.5.1.28
|
P55569 | MTKTIIDQAGATPGAIRTREGLVSAYRTELAIAGAIVLLVLAVGTQVPQAMSWGNFANITQAGAPLIIMSLGVLLVVITGGIDLSVGSVFSLTGMVTAQAMASGLDVSAALIGLGVGLVFGSINGFLVTVAGLAPFVVTLITFAVAGSLAFIVTNGRSMPIGDPDFWLLNSGSLIPGVPNYILFCIVLLVVIEIFLKKMVAGRWFYAVGSSAAAARLLGIPVKRTQFFAYVASSLLASFSGLLTISYILNAESTAGSSLMLQAIAAVVIGGASLLGGTGTAVGAVLGALMITVIQNGVNLIGINSFWQGSVTGLAILIAV... | Function: Probably part of the binding-protein-dependent transport system y4mIJK. This system probably transports a sugar. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33907
Sequence Length: 333
Subcellular Location: ... |
P55570 | MTDASKDIVSVRSLTKSYGATVVLKGVDFSVARGEIHALLGGNGAGKSTLIRVITGTAAKDGGELVFRDMAGNILTEADGRRKVAVVHQELALLPHLTVAESIALPHFRKGSRVYDGRTAGSQAYAALSMIDRDFAGTALNRLVGDLSLHEGQMVEIARALSSGAELILLDEPTANLTAAETERLFGVLRKLTRGNGLSVVFVSHRMKEIRQIAHVCSIIRDGRTVVGNVPTAELSDLAIIEHMGQAQATAVAHSARPAPVASLSDEPLTIAETGFSVTLQPGTILGVAGAPAGPETLIAALIGAAHERRWTVTRAGWPD... | Function: Probably part of the binding-protein-dependent transport system y4mIJK. This system probably transports a sugar. Probably responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53193
Sequence Length: 497
Subcellular Location: Cell membrane
|
P55572 | MTKTVTRAGGASGPQQFQSGGETMKYEITRRRFLAASSAVLAAPAIVTMVRPARAGTTLTLGHGAAPGNPRTVAAAKFAELVAEKTAGRVTINVAGAETLGSDAAMLTSLRTGALDVTANSQGATSALVPELAALGLPFLFENTAKAMQVLGGPVGAELVKRFEAVGVVPLDWWDNGIRHLTNSKRKVAAPAEVSGMKIRTPADPMTMDIFQALGAATEQIAFGELYVALQQGVVDGQENPLANIDSSKLYEVNKYISLTGHKWESTPFLMSQIAQARLGGDLEAVKAAAKEAGELQRKLSADKDAEVLAAFRRISAIEV... | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57124
Sequence Length: 541
Subcellular Location: Cell membrane
|
P55574 | MAQIGHNISLPERARRIRRHALRMGEVQGQGYIAQALGIADVLAVAYFHATTYRPDDPEWEGRDRFLLSIGHYAIALYAALIEAKIIPEDELETYGADDSRLPMSGMAAYTPGMEITGGSLGHGLGIAVGMSLALKRKGSRSFVYNLFSDGELDEGSTWEAAMSAGSYKLDNLIGIVDVNQMQADGPSLGVLNFEPLGPKFEAFGWYVQRIDGNDIDALVDAFDNARQHRHPQPRIIICDTKMAKGVPFLEARERNHFLRVEPQEWAEAIRIIDAGVTA | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30743
Sequence Length: 279
Subcellular Location: Cell membrane
|
Q87G35 | MTIEFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGETSGTLTIYGQDTAPFDMHQYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLTSNIDMYPLVKATAKMVDLEQMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLAALDPKTGKKTIEIIDDLHRETGKTIVIIEHRLEDVLHRSVDRIILMESGEIIADTTPDEILASPLLEDYGIREPLYISALKEAGCAIEGDAKPSSLTTLPLEQYKPTVQAWFDGSTAQPPKTPAETLLEVRGLTYSYDGEKNALEDVSF... | Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 64053
Sequence Length: 579
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
|
C0LGV0 | MLFWVLLSSFCVFCFSSPDGFLSLSCGGSSYTAAYNISWVSDNDYIETGNTTTVTYAEGNSTSSVPIRLFPDPQGRQCYKLPVRKDLSSVLIRATFVYRNYDSQNSPPAFHVSLGRRITSTVDLRTNDPWIEELVWPVNNDSLLLCLLAVKGRGIPVISSLEVRPLPLGSYKYSLEGSPDIILRRSYRINSGYTNGTIRYPSDPFDRIWDPDQSYSPFHASWSFNGLTKLNSFNITENPPASVLKTARILARKESLSYTLSLHTPGDYYIILYFAGILSLSPSFSVTINDEVKQSDYTVTSSEAGTLYFTQKGISKLNIT... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 99613
Sequence Length: 895
Subcellular Location: Membrane
EC: 2.7.11.1
|
R8NBR0 | MLEKQNSEENIELLRAMRYCYNKSKIFYAVRISISILIPILSISIYLFNRGSTGTSNTGVWFSVIGSIWLLIAYQIEKLEGGYIEKGAKIQEKFDINLFNIRWNNVLVGNQISPEDIRDFSSKFKGDEEKLKNWYGGLSSKHFYVNVILAQRSNLMWAISLKRNFSILLFTVSVLYLFLTIAFGFFVNMSMQEYIIKILLPSMSILIYGFKTSDELKKQSNKLEALGNSIISKFDTGNLSEINASACREYQDAIFVYNRIRSILIPEWLYWLRQQKDDEKMIQINIRLTKKSNLF | Function: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell ... |
Q9LVM0 | MMQFHFQFYVGPVFTLRPSKGFLSTCLVSFLFVTTTFCSYAIADLNSDRQALLAFAASVPHLRRLNWNSTNHICKSWVGVTCTSDGTSVHALRLPGIGLLGPIPPNTLGKLESLRILSLRSNLLSGNLPPDIHSLPSLDYIYLQHNNFSGEVPSFVSRQLNILDLSFNSFTGKIPATFQNLKQLTGLSLQNNKLSGPVPNLDTVSLRRLNLSNNHLNGSIPSALGGFPSSSFSGNTLLCGLPLQPCATSSPPPSLTPHISTPPLPPFPHKEGSKRKLHVSTIIPIAAGGAALLLLITVIILCCCIKKKDKREDSIVKVKT... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 71899
Sequence Length: 654
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Membrane
|
A0R4H4 | MADADVIVVGAGLAGLVAACELVERGHSVIIVDQENAANIGGQAFWSFGGLFFVNSPEQRRLGIRDSQELALQDWLGTAGFDRPEDHWPREWAHAYVDFAAGEKRSWLRARGLQTFPLVGWAERGGYDALGHGNSVPRFHITWGTGPALVEIFARRIRDSVRVRFAHRHRVDELIVNAGLVAGVRGSILEPSNAPRGVASSRKVVGDFEFRASAVIVASGGIGGNLELVRKNWPARLGRVPDQLISGVPAHVDGRMIGIAESAGAHVINNDRMWHYTEGITNYDPVWPNHGIRILPGPSSLWLDANGDRLPVPLYPGYDT... | Function: Able to catalyze the elimination of the C-1 and C-2 hydrogen atoms of the A-ring from the polycyclic ring structure of 3-ketosteroids, but the ketosteroid dehydrogenase activity is low compared to KsdD in the cholesterol degradation process. The low activity could be due to different substrate specificity.
Se... |
Q9ASS4 | MMMGRLVFVIWLYNCLCLLLLSSLVDADQANIDCLRTFKSQVEDPNRYLSTWVFGNETAGYICKFSGVTCWHDDENRVLSIKLSGYGLRGVFPPAVKLCADLTGLDLSRNNFSGPLPANISTLIPLVTILDLSYNSFSGEIPMLISNITFLNTLMLQHNQFTGTLPPQLAQLGRLKTFSVSDNRLVGPIPNFNQTLQFKQELFANNLDLCGKPLDDCKSASSSRGKVVIIAAVGGLTAAALVVGVVLFFYFRKLGAVRKKQDDPEGNRWAKSLKGQKGVKVFMFKKSVSKMKLSDLMKATEEFKKDNIIATGRTGTMYKG... | Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 69142
Sequence Length: 620
Domain: The protein kinase domain is predicted to be catalytically inactive. Lacks the conserved Asp active site at position 429, which is replaced by an Asn residue.
Subcellular Location: Cell membrane
|
Q5L2C9 | MATVDPIRYPIGTFQAPQQFEAGEVQEWIAAIRGLPSDLRTAVSGLNDEQLNTPYREGGWTVAQVVHHLADASMNAFLRTKWGVTEDGPTVKPFAESEWAKTADACLLPIEPSLLLLDGLHARWAALLESMTEADFHRTVRPEGAAGEMPLYVLTALYAWHGKHHTAQVASLRKRKGW | Cofactor: Binds 1 zinc ion per subunit.
Function: Possible metal-dependent hydrolase.
Sequence Mass (Da): 19713
Sequence Length: 178
Subcellular Location: Cytoplasm
EC: 3.-.-.-
|
B1W5S5 | MLLLISPDGVEEALACATAAEHLDIVDVKKPDEGSLGANFPWVIREIRAAVPADKPVSATVGDVPYKPGTVAQAALGAAVSGATYIKVGLYGCATPDQAIDVMRGVVRAVKDFRADAFVVASGYADAHRIGCVNPLALPDIARRAGADAAMLDTAIKDGTRLFDHVPPEGCAEFVRLAHEAGLLAALAGSVKAADLATLTRIGTDIVGVRGAVCEGGDRDAGRIQPRLVAAFRAEMDRHARAFAAAPAAS | Function: Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P).
Catalytic Activity: 2 D-glyceraldehyde 3-phosphate = 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate + 2 H2O + phosphate
Sequence Mass (Da): 25746
Sequence Length: 250
EC... |
Q54LH8 | MTDKYNDWVKNKKHNNYNMAEDPLYYIKSNWVIERQLSKGSFGQVYKAHKKLDPNFVCAIKVIQYCKFTMKEVDYLKKLNDPKFVKYYSLEFNNSKTYAYIIMEFIEGESMKSIIENKKFSDIEIKEIIKELLKALVYLNDKGIMHRDLKPENIMFQNQNQNQNQNNKINLKLIDFGLSKAINENIINKTVKLQTISSVGTTLYMAPEILLNNKGSNSSLDIWSLGCIIVEMKWGLNQLCLQRPNNIPVFPVNSLFTEILNLCFQTEPSKRIKSHQLIKHPFFNDENEQFYNDNKEYFDFLKENERDSYIEIHNTESIGS... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 77102
Sequence Length: 671
Subcellular Location: Membrane
EC: 2.7.11.1
|
O29527 | MIEAVDLHFCYGDAEVLKGVNFKAERGKVTVLMGRNGAGKTTLLKHLNGLLRPKSGKVIIDGRELKYDRKSLLEVRKRVFYVFQNPDDQILSPTVWQDVAFGPRNLGLKGERLERVVRNALEAVGLSGYEKRLCSTLSGGEKRRLAIASALAMNPDYCIMDEPSANVDGEGLRMIAEIIRKLREEGKGVVVSTHDADLAKEVGDYFYFMDDGKIVWEGEEFSYSVARKLGIRSFSLGKVILAESKIDDHPCFSADELERAVLKAFEGETVVVLGRDDWVIKELEKYPLEVERL | Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32858
Sequence Length: 293
Subcellular Location: Cell membrane
EC: 7.-.-.-
|
Q55624 | MTEVLRVGQPAPDFTATAIVDQSFQTVKLSTYRGKYLVLFFYPLDFTFVCPTEIIAFSDRHSEFTALDTEVVGISVDSEFSHLAWIQTERKMGGIGNINYPLVSDLKKEISQAYNVLEPDAGIALRGLFIIDREGILQYATVNNLSFGRSVDETLRVLKAIRHVQSHPNEVCPVDWQEGDKTMIPDPEKAKTYFETVAEP | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide +... |
Q8ES61 | MNEKYPIGEFQFDGEITNIIINEWINEIEDLPRLLKNTVIDLNNEQLDTSYRSGGWTVRQVIHHLADSHMNAYIRLKLAITEENPVIKPYDEKEWAELYDYNLPIEISLSLIEALHKRWCSLLRDLSPTDMERTFKHPESGSISIGKNIGIYAWHGKHHLAHITSLCKRKDW | Cofactor: Binds 1 zinc ion per subunit.
Function: Possible metal-dependent hydrolase.
Sequence Mass (Da): 20166
Sequence Length: 172
Subcellular Location: Cytoplasm
EC: 3.-.-.-
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.