ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q16549 | MPKGRQKVPHLDAPLGLPTCLWLELAGLFLLVPWVMGLAGTGGPDGQGTGGPSWAVHLESLEGDGEEETLEQQADALAQAAGLVNAGRIGELQGHYLFVQPAGHRPALEVEAIRQQVEAVLAGHEAVRWHSEQRLLRRAKRSVHFNDPKYPQQWHLNNRRSPGRDINVTGVWERNVTGRGVTVVVVDDGVEHTIQDIAPNYSPEGSYDLNSNDPDPMPHPDVENGNHHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLDGPLTDSMEAVAFNKHYQINDIYSCSWGPDDDGKTVDGPHQLGKAALQHGVIAGRQGFG... | Function: Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive secretory pathway.
PTM: Cysteine residues in the cytoplasmic tail are probably palmitoylated.
Location Topology: Single-pass type I me... |
O75340 | MAAYSYRPGPGAGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDTELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKNELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV | Function: Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair. Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of ... |
P12815 | MAAYSYRPGPGGGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDNELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKNELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV | Function: Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair . Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of... |
G3V7W1 | MAAYSYRPGPGAGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDNELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKHELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV | Function: Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair (By similarity). Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding trigg... |
Q0VCW8 | MQDPNADTEWNDILRKKGILPSKEDLKDLEKEAEEEEQRILQQSIVKTYEDMTLEELEDNEDEFNEEDERAIEMYRQQRLAEWKATQLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSALARKFPDVKFIKAISTTCIPSYPDRNLPTVFVYLEGDIKAQFIGPLVFGGMNLTLDELEWKLSESGAIKTSLEENPKKPVEDVLLSAVRCSVPAKRDSDSEDD | Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (By similarity). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts a... |
Q9H2J4 | MQDPNADTEWNDILRKKGILPPKESLKELEEEAEEEQRILQQSVVKTYEDMTLEELEDHEDEFNEEDERAIEMYRRRRLAEWKATKLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSGLARKFPDVKFIKAISTTCIPNYPDRNLPTIFVYLEGDIKAQFIGPLVFGGMNLTRDELEWKLSESGAIMTDLEENPKKPIEDVLLSSVRRSVLMKRDSDSEGD | Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation . Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding . Acts as a chaperone during heat shoc... |
Q8BVF2 | MQDPNADTEWNDILRKKGILPPKESLKELEEEEAEKEEQLLQQSVVKTYEDMTLEELEENEDEFSEEDERAIEMYRQQRLAEWKATQLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCSLINHHLSGLARKFPDVKFIKAISTTCIPNYPDRNLPTVFVYREGDIKAQFIGPLVFGGMNLTIDELEWKLSESGAIKTALEENPKKPIQDLLLSSVRGPVPMRRDSDSEDD | Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation . Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone d... |
P80284 | MAISKVWISLLLALAVVLSAPAARAEEAAAAEEAAAPEAVLTLHADNFDDAIGQHPFILVEFYAPWCGHCKSLAPEYEKAAQLLSKHDPAIVLAKVDANDEKNKPLAGKYEVQGFPTLKIFRNGGKSIQEYKGPREAEGIVEYLKKQVGPASKEIKAPEDATYLEDGKIHIVGVFTEFSGPEFTNFLEVAEKLRSYYDFGHTVHANHLPRGDAAVERPVVRLFKPFDELVVDSKDFDVSALEKFIDASSTPKVVIFDKNPDNHPYLLKFFQSNAPKAMLFLNFSTGPFESFKSAYYGAVEEFSGKDVKFLIGDIESSQGA... | Function: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 56463
Sequence Length: 513
Subcellular Location: Endoplasmic ret... |
P55059 | MHKAQKFALGLLAAAAVATASDVVQLKKDTFDDFIKTNDLVLAEFFAPWCGHCKALAPEYEEAATTLKEKNIKLAKVDCTEETDLCQQHGVEGYPTLKVFRGLDNVSPYKGQRKAAAITSYMIKQSLPAVSEVTKDNLEEFKKADKAVLVAYVDASDKASSEVFTQVAEKLRDNYPFGSSSDAALAEAEGVKAPAIVLYKDFDEGKAVFSEKFEVEAIEKFAKTGATPLIGEIGPETYSDYMSAGIPLAYIFAETAEERKELSDKLKPIAEAQRGVINFGTIDAKAFGAHAGNLNLKTDKFPAFAIQEVAKNQKFPFDQE... | Function: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 55114
Sequence Length: 505
Subcellular Location: Endoplasmic ret... |
P17967 | MKFSAGAVLSWSSLLLASSVFAQQEAVAPEDSAVVKLATDSFNEYIQSHDLVLAEFFAPWCGHCKNMAPEYVKAAETLVEKNITLAQIDCTENQDLCMEHNIPGFPSLKIFKNSDVNNSIDYEGPRTAEAIVQFMIKQSQPAVAVVADLPAYLANETFVTPVIVQSGKIDADFNATFYSMANKHFNDYDFVSAENADDDFKLSIYLPSAMDEPVVYNGKKADIADADVFEKWLQVEALPYFGEIDGSVFAQYVESGLPLGYLFYNDEEELEEYKPLFTELAKKNRGLMNFVSIDARKFGRHAGNLNMKEQFPLFAIHDMT... | Function: Protein disulfide isomerase of ER lumen required for formation of disulfide bonds in secretory and cell-surface proteins and which unscrambles non-native disulfide bonds. Forms a complex with MNL1 to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded ... |
Q32PP3 | MVSSQAKYELIQEVGRGSYGVVYEAVVRQTGARVAVEKIRCHSPENVELALREFWALSSIQSQHPNVIHLEECVLQRDALAQRMSHGSSSSLYLELVETSLKGEITFDPCCAYYMWFVMDFCDGGDMNAYLLSRKPSRKTNTSFMLQLGSALAFLHRNQIIHRDLKPDNILISQGRTPAGSPEPTLKVADFGLSKVCSGSGLNPEEPASVNKCFLSTACGTDFYMAPEVWEGHYTAKADIFALGVIIWAMVERITFVDVETQKELLGSYVQQGEDIVPLGEALLENPKMELNIPARKKSMNASMKQLIREMLSANPQERP... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 38205
Sequence Length: 341
Subcellular Location: Nucleus
EC: 2.7.11.1
|
Q8N165 | MVSSQPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIHLEECILQKDGMVQKMSHGSNSSLYLQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRLDTSDLEPTLKVADFGLSKVCSASGQNPEEPVSVNKCFLSTACGTDFYMAPEVWEGHYTAKADIFALGIIIWAMLERITFIDTETKKELLGSYVKQGTEIVPVGEALLENPKMELLIPVKKKSMNGRMKQLIKEMLAANPQDRP... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 38546
Sequence Length: 341
Subcellular Location: Nucleus
EC: 2.7.11.1
|
Q8QZR7 | MVSSQPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIHLEECILQKDGMVQKMSHGSNSSLYLQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQSRMDTSDLEPTLKVADFGLSKVCSASGQNPEEPVSVNKCFLSTACGTDFYMAPEVWEGHYTAKADIFALGIIIWAMLERITFIDTETKKELLGSYVKQGTEIVPVGEALLENPKMELLIPVKKKSMNGRMKQLIKEMLAANPQDRP... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 38550
Sequence Length: 341
Subcellular Location: Nucleus
EC: 2.7.11.1
|
Q15118 | MRLARLLRGAALAGPGPGLRAAGFSRSFSSDSGSSPASERGVPGQVDFYARFSPSPLSMKQFLDFGSVNACEKTSFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAKAIYDFTDTVIRIRNRHNDVIPTMAQGVIEYKESFGVDPVTSQNVQYFLDRFYMSRISIRMLLNQHSLLFGGKGKGSPSHRKHIGSINPNCNVLEVIKDGYENARRLCDLYYINSPELELEELNAKSPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHHANRGVYPPIQVHVTLGNEDLTVKMSDRG... | Function: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates ... |
Q63065 | MRLARLLRGGTSVRPLCAVPCASRSLASDSASGSGPASESGVPGQVDFYARFSPSPLSMKQFLDFGSVNACEKTSFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAKTIYEFTDTVIRIRNRHNDVIPTMAQGVTEYKESFGVDPVTSQNVQYFLDRFYMSRISIRMLLNQHSLLFGGKGSPSHRKHIGSINPNCDVVEVIKDGYENARRLCDLYYVNSPELELEELNAKSPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHHADKGVYPPIQVHVTLGEEDLTVKMSDRGGG... | Function: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates ... |
Q38WI8 | MTAIPIFIISDSIGETARTVIAAVNAQFPASVTLKIQRFPFITDQKTLTPILQDAHQEQAIIVSTLVNHTLQETVTQFCQAKHLTLIDLLSPLTTAISERSQTASLETPGSLRKLDEHYFHRISAMEFAVRYDDGQDPRGLLEADIVLLGVSRTSKTPLSMYLANQNYRVANLPLIPNVPLPKELFKVPAHKIIGLTMPLSTLLKIRQERLATLGLPQTTNYSNMTTVGDELAYANQIFEQLNATTINVADRSIEETASLIQTLI | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-hist... |
Q8Y634 | MENPVIIYVISDAIGETAQHIIRAVTAQFSLNKPADIRRHAFIRDESALLETLEEAKATDGIVVQTLVQAKLAEYATNFCVQNNIPNVDLLHTLTAAVEAKTGLKSKQDPGNMRRLDSNYFDRIAAIEFAVKYDDCKDPRGLLDADIVLVGVSRTSKTPLSSFLANQNWKVANVPLVPEIPIPAELFQIPAERIIGLTTTPEKLAQIRKVRLRSIGLDEASSYSSEKRILEELEYGYDTFKKLGCQVIHVEDKAIEETAALITEIITSYH | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-hist... |
Q8UJC7 | MENKKSFFHLHLISDSTGETLMSAGRAVSAQFHTSMPVEHVYPMIRNQKQLAQVIDLIDKEPGIVLYTIVDQQLAEFLDLRCHAIGVPCVNVLEPIIGIFQTYLGAPSRRRVGAQHALNADYFARIEALNFAMDHDDGQMPETYDDADVVIIGISRTSKTPTSIYLANRGIKTANIPVVPNVPLPESLYAATRPLIVGLVATSDRISQVRENRDLGTTGGFDGGRYTDRATIMEELKYARALCARNNWPLIDVTRRSIEETAAAILALRPRTR | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-hist... |
Q2GFU3 | MSTSVTLNLHLISDSTCETVASVARSALEHFRSVEVNEFVWSFINNNEQIDKIMSLIEKDKYNFIMYTMFDDELRRYLKQKAGAQEIPCIPVLSHVIREISCYLHIKKDPYISTNIGLDDEYFTRIDAINYTIAHDDGQNLWDIDQADIIILGVSRTSKSPTSIYLAYRGYRVVNIPLVHSINLSVDLSNMKNKLIVGLTIDIDRLIEIRRTRLVSMKNQNNYQYVDYEHVLMEIKETKRICVQNGWPIIDVTQKSVEEIAATIIQYFNKMQH | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-hist... |
Q5HBX0 | MSNPVVLNLHLISDSTCETVAAVARSALEHFKSVEVNEFVWSCINSYEQIDKIMLTIEKDKYNFIMYTMFDDDIRKYLKQKAGIHEIPCIPILSHVIREISCYLNIKKDPYINTSIGLDDEYFTRIDAINYTIAHDDGQNLWDIDQADIIILGVSRTSKSPTSIYLAYRGYRVVNIPLINSIELSVDLSKMKNKLIVGLTIDIDRLIEIRRARLVSMKNQNNYGYVDYEHVLMEIRETKKICAKNGWPIIDVTQKSVEEIAATIIQYFTKMQH | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-hist... |
Q2N6J9 | MKRIHLHLLSDSTGETLEMIAKAALAQFENADVVRHFWPMVRSRQHLERIVPELSNNPGLVLFTLVNAETRRALRDHCRRLSLPAVDALDEVTAALEVQLGQEAHGRPGRQHKMDEAYFKRVEAIQFTIAHDDGVGWENWEEADIVLAGVSRSSKTPTSIYLANRGYKVANIPLVMESPPPPALYELKNPMVVGLTTAPERLVQIRRNRLLTLNEQAETSYVEKDRVTEEVKFARRLFSDNNWPVIDVTRRSIEETAAAVIRLHNERHARVKPGEKPI | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-hist... |
Q74G02 | MKRSIKHIYLLSDATGETVERVVRAALSQFRDVEARFHRVTRIRSREDVIWALEEVLREPGMVVYTLVDTELAQLLRDEAEAHGLDAIDLISPLLFKLSDFFGEAPQKEPGLLHQINSEYHKRVDAVDFTVKHDDGQDPRGLAKADFILVGVSRSSKTPLSMYLAHKGYKVANVPIVKGIDPPPELYKVDQKRVVGLIIDAERLVQIRTARLRNLGQMPKGSYADYERIEEELEFCRRLYRRNPQWLVIDVTKKSVEESAAEIIQKLAG | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-hist... |
Q0BWA1 | MLKDGRETGKWIRVMTAHRMNLHLVSDATGETLNSIARATVSQFEHAQIIYHRWSLIRTRFQLHRVLEGIEAEPGPVLSTLIEPGLRSELENFCSRIGIAVVHVLDPVLSLLQHHIGEQAIARPGRQYVLDADYFRRIDAMHFVLAHDDGQAQVGINEADLCLVGVSRSSKTPTSFYLANRGVKAANIPLVPGLPEPPGLEAPIVPVIGLTIDPEALIEIRRHRLKLIGGQPNVQQNTAYVDLESVKAELIWARRLCARKGWPVIDVTRRSIEETAATVLQLVEAWHERRRSLPPGG | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-hist... |
B8CXH4 | MTEKPRIFIVSDSIGETAQYVVDATVSQFNGYLDSKRFSYVQTTRELNNIIKKATEQKTLIAYTLIDPRLREEIATLARKNNIYAVDIMGPMMEAFEEFFQKKPRLQPGLVHRLDKDYFKRVEAMEFTVKYDDSNDDRGVKEADVVLIGVSRTSKTPMCIYLSYRGYKAANIPLVPEVEPTPLIYENPDNKVIGLTIDPLLLNEIRQERLKSLGIDPESSYASIDRINVELEYAEKTMEKIGCPVIDVTNKSIEESANEVIDYLNG | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-hist... |
Q0C6A8 | MTQPQRPSIYFNVHLVSDSTGETLNAIQRAACAQFENVQPLEHNYYLVRSERQLERVMKEIEAAPGVVWYTISDGALRGRLEAFCRERSIPTLPVLDPSIAMLSRHLGVAPNNRVAGQHALDEDYFERMEAINFTLAHDDGQNVESLIGADVILLGVSRTSKTPTCVYLANRKVRAGNIPLVPGVPLPDFMEKMGDKGPLVVGLKISAERLVQIRRQRLISLNQDEITEYADEEAVRDEITQANRLFQRNGWKTIDVSRRSVEETAAGILNMLHERWGHS | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-hist... |
Q9XDM9 | MSTAINSVEMSLSADEIRERVRAAGVVGAGGAGFPAHVKLQAQVEIFLVNAAECEPMLKVDQQLMWQQAARLVRGVQYAMTATGAREGVIALKEKYRRAIDALTPLLPDGIRLHILPDVYPAGDEVLTIWMATGRRVAPAALPASVGVVVNNVQTVLNIARAVEQRFPVTRRTLTVNGAVARPLTVTVPIGMSLREVLALAGGATVDDPGFINGGPMMGGLITSLDNPVTKTTGGLLVLPKSHPLIQRRMQDERTVLSVARTVCEQCRLCTDLCPRHLIGHELSPHLLVRAVNFHQAATPQLLLSALTCSECNVCESVAC... | Cofactor: Binds 2 [4Fe-4S] clusters (By similarity). The two centers are coupled but must possess different redox potentials (By similarity).
Function: A protein that aids in conversion of cob(III)alamin to cob(II)alamin and then to cob(I)alamin in the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-... |
Q9XDM8 | MSQAIGILELTSIAKGMELGDAMLKSANVDLLVSKTICPGKFLLMLGGDIGAIQQAIETGTSQAGEMLVDSLVLANIHPSVLPAISGLNSVDKRQAVGIVETWSVAACISAADRAVKGSNVTLVRVHMAFGIGGKCYMVVAGDVSDVNNAVTVASESAGEKGLLVYRSVIPRPHEAMWRQMVEG | Cofactor: Probably bound by a single Cys residue from each subunit; which protein provides the fourth ligand is unknown.
Function: A minor shell protein of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approxi... |
P0DUV8 | MERQPTTDRMIQEYVPGKQVTLAHLIANPGKDLFKKLGLPESVSAIGILTITPSEASIIACDIATKSGAVEIGFLDRFTGAVVLTGDVSAVEYALKQVTRTLGEMMRFTACPITRT | Function: A minor shell protein of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. May selectively transport specific metabolites (By similarity). Not absolutely required to make artificial BMCs . Proteins such as this one with circularly permuted BMC domains may play a key role ... |
B1VB80 | MKRIMLIGPSQCGKTSLTQCMRGEALHYQKTQAIVWSPTTIDTPGEYLENRCLYSALLASACEADIIALVLNADAPWSPFSPGFTGPMNRPVIGLVTKADLASPQRISLVESWLVQAGAQKVFFTSALENTGVDEMFIFLNAKESSCLTK | Function: May play a role in the spatial distribution of the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation, perhaps being involved in cytoskeleton dynamics; might bind GTP (Probable). This subunit is directly targeted to the BMC .
Sequence Mass (Da): 16332
Sequence Length: 150
Domain: The N-terminus ... |
A6TDE9 | MTYKIMAINAGSSSLKFQLLNMPQGALLCQGLIERIGLPEARFTLKTSAQKWQETLPIADHHEAVTLLLEALTGRGILSSLQEIDGVGHRVAHGGERFKDAALVCDDTLREIERLAELAPLHNPVNALGIRLFRQLLPAVPAVAVFDTAFHQTLAPEAWLYPLPWRYYAELGIRRYGFHGTSHHYVSSALAEKLGVPLSALRVVSCHLGNGCSVCAIKGGQSVNTSMGFTPQSGVMMGTRSGDLDPSILPWLVEKEGKSAQQLSQLLNNESGLLGVSGVSSDYRDVEQAADAGNERAALALSLFAERIRATIGSYIMQMG... | Function: Works with phosphate acetyltransferase (pta) to capture exogenous propionate and regenerate propionyl-CoA during degradation of 1,2-propanediol (1,2-PD).
Catalytic Activity: ATP + propanoate = ADP + propanoyl phosphate
Sequence Mass (Da): 43619
Sequence Length: 404
Pathway: Polyol metabolism; 1,2-propanediol ... |
P74879 | MSYKIMAINAGSSSLKFQLLEMPQGDMLCQGLIERIGMADAQVTIKTHSQKWQETVPVADHRDAVTLLLEKLLGYQIINSLRDIDGVGHRVAHGGEFFKDSTLVTDETLAQIERLAELAPLHNPVNALGIHVFRQLLPDAPSVAVFDTAFHQTLDEPAYIYPLPWHYYAELGIRRYGFHGTSHKYVSGVLAEKLGVPLSALRVICCHLGNGSSICAIKNGRSVNTSMGFTPQSGVMMGTRSGDIDPSILPWIAQRESKTPQQLNQLLNNESGLLGVSGVSSDYRDVEQAANTGNRQAKLALTLFAERIRATIGSYIMQMG... | Function: Works with phosphate acetyltransferase (pta) to capture exogenous propionate and regenerate propionyl-CoA during degradation of propionate and 1,2-propanediol (1,2-PD). Ectopic expression partially complements a cobB deletion allowing some growth on propionate . Restores growth to an eutQ deletion on ethanola... |
B1VB82 | MAVAQCPASCGELIQGWILGSEKLVSCPVEWYSTVEVTSGSPLTDERPLSRAMVDRLLQHWQYPAHLSQDIRIDVQSTIPIAKGMASSTADIAATAIAAAHYLGHQLDEPTLAQLCVSLEPTDSTVFRKLTLFDHNNASTQIGCEAQPQLDLLVLESPETLRTADYHRIPRHSGLQAGAAALQRAWEKVQEACISQNPYRLGEAATLSAIASQLLLPKPDFDSLLALVEECDLYGVNVAHSGSVVGLMLDRNRHDVDYIKWMLTQKKLTIHWPEQHLLRMVTGGVELQ | Function: L-threonine kinase that catalyzes the conversion of L-threonine to L-threonine-O-3-phosphate. Involved in the de novo synthesis of adenosylcobalamin (coenzyme B12) and the assimilation of cobyric acid.
Catalytic Activity: ATP + L-threonine = ADP + H(+) + O-phospho-L-threonine
Sequence Mass (Da): 31681
Sequenc... |
Q164G2 | MSPATAPVLISCGEPAGIGPEIAVAAWDALQGTIPLAWVGDPRHLPASTTFTAITHPRAVADVPTGSLPVLVHDFAAPSTPGHPDPANAQGVIDVIAACVAWVQEGAAAALCTAPIHKKALIDGADFKHPGHTEYLQALAGGRSRAVMMLASDALRVVPTTIHIALEDVPRVLTPALLRETITITHAALQRQFGIQAPRIVVAGLNPHAGEGGAMGLEEQDWIADVISALAASGMNLRGPLPADTMFHARAREGYDAAIAMYHDQALIPIKTLDFDRGVNVTLGLPFIRTSPDHGTAFDIAGKGIANPTSMIEAIKLAAH... | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Cataly... |
Q1GI38 | MTGAPQVIALSCGEPAGIGPEIAVAAWDQLRADCPFVWIGDPRHLPSSHPWQPVSAPAEALQVSADALPVWPLEFAGNTTKGEADPQNASGVIQSIKTGVELVTSGKAAALCTAPIHKKALIDGAGFAYPGHTEFLAALGGVDHVVMMLASAALRVVPATIHIPLSAVPEVLTPDHLRRVITLTDRGLRDQFGLTAPRIAVTGLNPHAGEGGAMGQEEGDWIEALIREMQTEGYRLTGPHPADTLFHAAARARYDAAIAMYHDQALIPIKTLDFDKGVNVTLGLPFIRTSPDHGTAFDIAGKGLANPSSLIEALRLAQTM... | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Cataly... |
P58717 | MSSAQRVVITPGEPAGSGPDLVVQLAQRAWPIELVVCADGALLTERAAMLGLPLSLLPYSPDVPAAPQPAGTLTLLPVSLRAPAISGQLTVENGPYVVETLARACDGCLNGEFAALITGPVHKGVINDAGISFTGHTEFFEERSQAKKVVMMLATEELRVALATTHLPLRAIADAITPALLHEVIAILHHDLRTKFGIAEPRILVCGLNPHAGEGGHMGTEEIDTIIPVLDELRAQGMKLNGPLPADTLFQPKYLDNADAVLAMYHDQGLPVLKYQGFGRGVNITLGLPFIRTSVDHGTALELAGRGKADVGSFITALNL... | Cofactor: Binds 1 divalent metal cation per subunit. Can probably use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP... |
Q5PBF2 | MIDFFEGVSWLIMPFSGVCVREADSSPMDVFGLWYSEMLRATGAHMREPSAMVLATCDVQNRPSARVVLLKKYGEAGFEFVTNFNSRKGREIADNPQVALVFDWRHIGRQVRVEGLATLMDASESDAYHASRSRESKISAWCSQQSAVLESRKLLLEQFERERQRFDGQEIPRPGHWGGVRVVPHVVEFWEDGAHRLHSRKQYSRGDSGSWSCVDLYP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24885
Sequence Length: ... |
A8HRJ3 | MSDSAMEPQNPLTSGDFTAADEPFRLFSEWLKDAERSEPNDPNAMTLATVDPDGLPDARMVLLKGLDDRGFVFYTNTESAKGRELTAHPKAALVFHWKSLRRQVRVRGPVERVTDAEADAYFATRPRLSQIGAWASQQSRPLEGRFALEAAVATTTARYAVGSVPRPPHWTGFRILPVQIEFWHDRPFRLHDRVVFKRENPEIDWEKSRLYP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24177
Sequence Length: ... |
Q8A7E7 | MKNIADIRQEYTKSGLRESELPCDPLSLFSRWLQEAIDANVEEPTAIIVGTVSPEGRPSTRTVLLKGLHDGKFIFYTNYESRKGRQLAQNPYISLSFVWHELERQVHIEGTAAKVSPEESDEYFRKRPYKSRIGARISPQSQPIASRMQLIRAFVKEAARWLGKEVERPDNWGGYAVTPTRMEFWQGRPNRLHDRFLYTLKTDGKWEINRLSP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24724
Sequence Length: ... |
Q6G4D7 | MGNTVQTDNDFMQMQKPFALFAKWLEEATVSEINDPNAMALATVDKTGFPNVRMVLLKDFSPQGFVFYTNYESPKGQEILKSMKASLVFHWKSLRRQVRIRGIVEKVTPQEADAYFQSRPRDSRIGAWASKQSQPLESRFVLEKAIARYTTRYAVGNIPRPPYWSGFRVKPLSIEFWCDRPFRLHDRLLFTRDSVEHVDWKRQKLYP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24271
Sequence Length: ... |
Q6MK45 | MFDINKDPFEHFDRLMKEAVAKQIPEANAMSVATVDEKGVPSVRIVYLKEVSQGGFVFYGNYNSHKGKDIETNPIVCLNFHWPAIWQQIRITGKAEKISAAESDAYFATRARLSQIGAWASHQSETIPALDWLSRRVQEYEKQFDGQVVPRPPHWGGWRVIPTEIEFWFGLGGRLHERHIYQRTEDGGWKTFLRSP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 22590
Sequence Length: ... |
Q2KVR0 | MSVSDLRQSYERGVLLEQQAAATPIDQFALWFDEAQAAQVPEPNAMTLATVDASGQPSARIVLIKAFDARGFTFFTNYTSRKGEDLLANPRAALLFFWQALERQVRIEGVVERVSADESDAYFHSRPVGSRIGAWASEQSQPITREALEARERDFKARFGDTPPRPPHWGGYRLVPTYFEFWQGRPSRLHDRLRYRPDGKQGWVMDRLSP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 23962
Sequence Length: ... |
Q3IDP4 | MKLEDIRREYLQNALSEDNLLDDPFKQFETWLEHAVASNLPDPTAMVVATVDDTGQPSQRIVLLKHLDNDGFVFFTNTGSRKAQELKGNNKISLHFPWHPMERQVIVYGEAKPLPTSAVAKYFLSRPKESQLAAWASAQSRPVSSRKVLMETFANMKNKFAKGEIPLPDFWGGYCVVPQKIEFWQGGAHRLHDRFMYQRQADNSWQITRLNP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24362
Sequence Length: ... |
Q4FS02 | MNMDFTDQRLSYEKGQLDQQSVPISPFELLKAWMHEAIEEQVQEPYAMSLATCGADDKPSVRIVLLREITDKGIVFYTNYESAKGQDIAENPNAEALFFWHKLERQIRISGSIAKIDADKSAAYFQKRPHDSQVGTWVSQPQSGEVASRDVMEQTFEQLQTDYPDGAAVPTPGFWGGYEITVSEIEFWQGRANRMHDRIVYHKEVDGSFSTKRLLP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24642
Sequence Length: ... |
A1SUY2 | MSFISKIRCAFTLGQGVLIENEALKETNDPILFFNNWLKKAQDTGIILPESMSISTCTPEGRPSSRMVLLKEVDSKGFVFFTNYDSRKAHDLEANPFAALLFHWNILQRQVRIEGRVERISTAQSNAYFQSRGRGSRIGAWASHQSQELNDRQTLVERVKYFEEKFAGKEIPLPEFWGGYRVIPESIEFWQGKADRLHDRFVYQPTEKNWTVKRLNP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 25178
Sequence Length: ... |
A5FJ95 | MTKLSVNINKIATLRNARGGNVPDLLKVAADIQRFGGQGITIHPRPDERHIRYQDARDLKAIVTTEYNIEGNPQHNFIDLVLECKPDQVTLVPDAIGAITSSAGWDTIKNQEYLKEVIQEFQRNGIRTSIFVDPVLEMIEGAKKTGTDRIELYTEAFAHQYDLGNKNGIDPYVKAAELANELGLGINAGHDLSLDNIQFFKQNIPGLLEVSIGHALISEALYLGLDNVVNMYLKKLK | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
B9M5K2 | MARLGVNIDHVATIRQARGGAEPDPVAAAAIAELAGADGITIHLREDRRHIQDRDLRLLRQTIKTRLNLEMAATDEMVSIALSVKPDMCTLVPEKRQELTTEGGLDVRLHLDAIRGAVQKLQDGGLIVSLFIDPDTDQIKAADKSGADYIEIHTGAFAEASDWKAEQEELKKIENAIKLAGKLGLGVNAGHGLNYSNIRKVAALGGIEEYNIGHSIISKAVLVGLDRAVRDMVDLVKYS | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
Q3V8C9 | MAKLGVNIDHVATIRQARGGVEPDPVAAAAIAEFAGADGITVHLREDRRHIQDRDLRLLRQTVKTKLNLEMAATDEMVGIALSVKPDMCTLVPERRQELTTEGGLDVRVGMQALADAIGRLQDGGIVVSLFIDPDADQVKASSKVGADYIEIHTGTFAEAREWKKEQAELERIENAIKLGTKLGLGINAGHGLNYTNVRKVAALGGIEEFNIGHSIISRAVFTGLDRAVRDMVDLVKYA | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
Q5FNS2 | MIRLGVNIDHVATLRNARGGTFPDPVAAAELAIASGADGITAHLREDRRHIRDADMPRLRALSAPLNFEMAATDEMVRIACDLRPHACCLVPEKRQEVTTEGGLDIVGQSEALKPKIARLRDAGIRVSLFIDPEARQIETAAALGAPVVELHTGAYALGGSEELERLRSAAGTVAACGLELHAGHGLTYDNVGAIADLTGLAELNIGHFLIGQAIFDGLGPVVRKMKSLINS | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
O26102 | MRFGLNIDHIVTLREIRKTYEPEILEALFIAKNTHKVDLITIHLREDRRHIQNEDVLKLLEISPLPINIECSINAEITDFLCSLKNKPSKVTIVPENRNEVTTEGGLDCSLKGLGEVIRAYHNKGIEVSLFIDPLKDALHFAREHQVKQVEFHTGVYANLHNALYSNANNQIHAISVLKDKSPKELKEELHNAFLQLRRMSKEAFFMGITACAGHGLNYTNVKELLKIPSLRELNIGHSVVSKAVLVGLEKAILEMAQLIKR | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
Q8D304 | MSKLLLGVNVDHVASLRNVRGGKFPDPVQLAILAEIAGADSITTHLREDNRHINEKDVICIKKSIQSRLNLEISTKKEMINKAINILPYSCCLVPENRQEITTESGIDVIKNKKYLKKVICKLKSLGIKVSLFVDPIKNQILSSSEINADCIEINTGKYSEQDKKENKEEINLIKLCAKYANKLGLEVHAGHGLNYFNVRSIVNIKEIKELNIGHSIISRSLIVGMQNAVKEMKDIIYSEKIKWQ | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
B3CLF3 | MKLGVNIDHVATLRNARGASYPDPLKAAKIAINAGADFLTVHLREDRRHIRDEDVFNLKQNISTELNLEIAATEEMLKIAKEVKPYSICIVPEKREELTTEGGLNIVNMHSKLSGIIEEMHSFDIKVSLFIDPNINQLKYLEKLERKPDIIEIHTGDYCDNPSEEKLKLITNSAEYINNLGIECHAGHGINYKHAKEIKKIPHISALNIGHSLISEAIFHGLHSVTKKMKMTISK | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
A7IM59 | MAVLKPVRLGVNVDHVATVRNARGGALPDPVRAAALAKAAGAHGITAHLREDRRHIRDADMERLKAEIDLPLNFEMAATDEMVAIACRVRPNACCLVPERREERTTEGGLDAAGQRAELAPRIARLKAAGIRVSLFIAADPAQIAAAAELGADIVELHTGAWCDAVTEGRHVEAEAEFVRLKAGARQAAGLGLEVHAGHGLDYATAERIAAFPQIVELNIGHFLIGEAIFVGLDQAIARMRAAIAAGRAAVGDGAAA | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
Q9PH84 | MSQRTRLSVNVNKIAVLRNSRGDGAPDVIRAASACIDAGAHGITVHPRPDARHIRHDDVIGLSALTRARGVEFNIEGNPFAEPRAGYCGLLALCRETRPHQVTLVPDGDQQITSDHGFDFAREGPGLRPLIDEIKQWGCRVSLFVDVNVTGLADAAIWGVDRIELYTGPYAEMHHAGCSDAVLREFATTARLAQDVGLGVNAGHDLSQTNLGVFLGAVPDVLEVSIGHALISEALYEGLVPTVRRYLDILDSVNPAVSMR | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
O59080 | MDKLKIIMEKGTERLKRGFAKMVKGGVIMDVTNAEQARIAEEAGAVAVMALHKVPADIRKAGGVARMAPVEKIQEIMDAVTIPVMAKCRIGHEAEARILEALGVDMIDESEVLTPADPFFHIYKKKFTAPFVCGARNLGEAVRRIWEGAAMIRTKGEAGTGNIIEAVRHVRLVNENIRLIQRMTDEEIYGVAEKFAEPYLRLAFSVKEISGLPKRVLENEPIYEGFTYREIVEDIYKILLEIKKLGRLPVVNFAAGGVATPADAALMMAMGMDGVFVGSGIFKSSNPPKMARAIVEAVNHWDEPDVLAEISREIGEPMRG... | Function: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G... |
Q9UWX3 | MRLYELSFAQIEDFFYKLAEVKDIIKDHGLLEFLPEFKKLDSTVHTGTTRVKHAFPIFQKGGVVMDITNVQQAQIAEEAGAVAVMVLDKLPYDVRKSGGVARMADPKIIEEVMSSITIPVMAKVRIGHYYEAKLLEALGVDMIDESEVLTPADEEHHINKWEFSVPFVNGARNLGEALRRTSEGASMIRTKGEAGTGNVSEAVKHMKIINSEIRSLISMSEEDRVKKAREYQVPYQIVELTAKIKRLPIVNFAAGGIATPADAALMMWLGADGLFVGSGIFKSQDPDERAKAVVLAAACWEYPEIVLEAQKMISEQKSMM... | Function: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G... |
A5UY93 | MTVGILALQGDFREHEEMLRRIGAPTLQVRLPKHLQHVERLIIPGGESTTIGKLLAMYGLIDPLRARIRDGMPVWGTCAGAILLAQRIADGRADQPSLRLMDVTARRNAFGSQLESFEVDLPVLGLGDEPLRMVFIRAPVLEDLGRDVTPLAHLDDGRVVAARQGTMLATCFHPELTPDERMHRYFLAM | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutam... |
Q1AWE7 | MAGRRNGHAGRPRVGVLALQGDFREHAEILERLGAEPVEVRRPEDLRGLDGLIIPGGESTAIGNLMVHSGMLDAIRSFFYQGGAVWGTCAGMVLAASATTGPSQPLLGIMSALVERNGFGRQVHSFEADLEVKGFDRPFRGVFIRAPYFEDVGPGVEVLAEIDGRVVAARAGKVLVTAFHPELTDDTRFHEYFLREVCGSDERS | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutam... |
A4FBA2 | MGGVSTARPVIGVLALQGGVAEHLTALERSGAEARPVRRPEELAQVHGLVLPGGESTAMTRLLDGFELFEPLRERLAAGMPAFGSCAGMVLLAGTVLDDRVEQDTPPVRPFGAIDMAVRRNAFGRQVDSFEADLDFAGVTDGPVHAVFIRAPWVDKVGADVRVLASVAPSGHGSEVTAPAGRIVAVQQGPVLATAFHPELVSGDERVHRYFVQTVRAS | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutam... |
Q9UWX4 | MKIGIIAYQGSFEEHFLQLKRAFDKLSLNGEIISIKIPKDLKGVDGVIIPGGESTTIGLVAKRLGLLDELKEKITSGLPVLGTCAGAIMLAKEVSDAKVGKTSQPLIGTMNISVIRNYYGRQKESFEAIVDLSKIGKDKAHVVFIRAPAIAKVWGKAQSLAELNGVTVFAEENNMLATTFHPELSDTTSIHEYFLHLVKG | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutam... |
Q02CB5 | MKKVGVLSLQGDFAAHGAALERAGAQPVFVREREQLNQIEGLILPGGESTTMLKLLRYEDLFDDVAEFGRTKPVFGTCAGAILMAKGVTNPAQESFGLVDIEVERNAYGRQTDSRIAQVRPFPDFENRTAPGELKAVFIRAPIIRRIEDGVRVLASYQGDPVLIEQGRFLVATFHPELTDDARVHSLFLSKL | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutam... |
Q15121 | MAEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEKSEEITTGSAWFSFLESHNKLDKDNLSYIEHIFEISRRPDLLTMVVDYRTRVLKISEEDELDTKLTRIPSAKKYKDIIRQPSEEEIIKLAPPPKKA | Function: Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm (By similarity). Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content o... |
Q62048 | MAEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEKSEEITTGSAWFSFLESHNKLDKDNLSYIEHIFEISRRPDLLTMVVDYRTRVLKISEEEELDTKLTRIPSAKKYKDIIRQPSEEEIIKLAPPPKKA | Function: Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm. Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose... |
Q9FR44 | MAASYEEERDIQKNYWIEHSADLTVEAMMLDSRASDLDKEERPEVLSLLPPYEGKSVLELGAGIGRFTGELAQKAGELIALDFIDNVIKKNESINGHYKNVKFMCADVTSPDLKITDGSLDLIFSNWLLMYLSDKEVELLAERMVGWIKVGGYIFFRESCFHQSGDSKRKSNPTHYREPRFYSKVFQECQTRDAAGNSFELSMIGCKCIGAYVKNKKNQNQICWIWQKVSSENDRGFQRFLDNVQYKSSGILRYERVFGQGFVSTGGLETTKEFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISF... | Function: Involved in phosphocholine biosynthesis . Catalyzes the N-methylation of phosphoethanolamine, phosphomonomethylethanolamine and phosphodimethylethanolamine, the three methylation steps required to convert phosphoethanolamine to phosphocholine (PC) . Required for root system development and epidermal cell inte... |
A0A1B2CTB4 | MLPRALTLSALLALLLAIYLALAPARLSCRCRSWEQCWPSLEAWSHLNASLNSHLVDLRPIASVCHEPILDQPACDIVRRMSNSGRWRTGQPGALINSFWESGFGSNETCSLSSGQENLCHQGRIPLYAAVVESTQEVQTAVKFAREHNLRLVIRNTGHDGAGSSSGPDSFQIFTHRLSDILYHENFRITGSNTSVGPAVSIGAGVLFGDLYVHGGQKGFIVTGGDSATVGAAGGFTQGGGVPGFLGHTWGLAADNVLEFEIVTATGNLVIANAGQHPDLFWALRGGGGGTFGVAVRVTMRTYPDHPAVKSTISITGDGQ... | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group . The first stage is catalyzed by the nonribosomal pepdide synthetase penN that condenses anthranilic acid and O-methyl-L-... |
P01212 | MGLEARHCCMFLLVFASLSVEIRADCSKDCASCALHLGQQREINSLACTLECEGKLPSAKAWGTCKELLLLTKVDNVQDGEKYQDNNDSHYAAKKYGGFMKRYGGFMKKMDELYHAEPEEDDAGGEILAKNYGGFMKKEYDSDRDAADLLRELLATSGDPESSIYHDNNSETPGEINKRYGGFMRGYRRSTDLEDETSGIQKRYGGFMRRVGRPEWWEDYQKRYGGFMTRFTDSFLPSDEDGESYSKENPDMEKRYGGFMRF | Function: Enkephalin neuropeptides compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress.
PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing.
Sequen... |
P01211 | MARFLGLCTWLLALGPGLLATVRAECSQDCATCSYRLARPTDLNPLACTLECEGKLPSLKTWETCKELLQLTKLELPPDATSALSKQEESHLLAKKYGGFMKRYGGFMKKMDELYPLEVEEEANGGEVLGKRYGGFMKKDAEEDDGLGNSSNLLKELLGAGDQREGSLHQEGSDAEDVSKRYGGFMRGLKRSPHLEDETKELQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFAEPLPSEEEGESYSKEVPEMEKRYGGFMRF | Function: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress.
PTM: Proenkephalin-A is cleaved by CTSL to generate Met-enkephalin.
Sequence Mass (Da): 29788
Sequence Length: 263
Subcellular Locati... |
Q28409 | WETCKEFLKLSQLEIPQDGTSALRESSPEESHALRKKYGGFMKRYGGFMKKMDELYPQEPEEEAPAEILAKRYGGFMKKDAEEEEDALASSSDLLKELLGPGETETAAAPRGRDDEDVSKSHGGFMRALKGSPQLAQEAKMLQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFADSLPSDEEGESYS | Function: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress.
PTM: Processed and degraded by ACE.
Sequence Mass (Da): 21267
Sequence Length: 187
Subcellular Location: Cytoplasmic vesicle
|
P01210 | MARFLTLCTWLLLLGPGLLATVRAECSQDCATCSYRLVRPADINFLACVMECEGKLPSLKIWETCKELLQLSKPELPQDGTSTLRENSKPEESHLLAKRYGGFMKRYGGFMKKMDELYPMEPEEEANGSEILAKRYGGFMKKDAEEDDSLANSSDLLKELLETGDNRERSHHQDGSDNEEEVSKRYGGFMRGLKRSPQLEDEAKELQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFAEALPSDEEGESYSKEVPEMEKRYGGFMRF | Function: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress.
PTM: Proenkephalin-A is cleaved by CTSL to generate Met-enkephalin.
Sequence Mass (Da): 30787
Sequence Length: 267
Subcellular Locati... |
A0A1B2CTC1 | MGSIDDSFSLPAPSDEHGFEALGTQLVEAMSTYAKCLKAENLPPPSLYPMFSASTSVACPEGIEAKRKIVELSQLICAATMDPELNLLISSLQFHFCSSLKVAIDLRIYEYIPVDGTVSLSQLAELAGRIMRVLTNKHVFMQIQPGHYAHTRMSSLLLKTKAKDLLSHRLDDVFRSASREADALAQAGYREPDRRAAKGFNLAFNTDKNFWEYIATDDPKRGARFARAMHAVNINSLDVIPRLYPFDSLATDGSLIVDVGGGQGQVAKRILEYYPNSGLRCIVQDGYVTNGSTAGPAAVEMHRHDFFEAQPIKGAAAYFF... | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group . The first stage is catalyzed by the nonribosomal pepdide synthetase penN that condenses anthranilic acid and O-methyl-L-tyrosi... |
P04094 | MAQFLRLCIWLLALGSCLLATVQADCSQDCAKCSYRLVRPGDINFLACTLECEGQLPSFKIWETCKDLLQVSKPEFPWDNIDMYKDSSKQDESHLLAKKYGGFMKRYGGFMKKMDELYPVEPEEEANGGEILAKRYGGFMKKDADEGDTLANSSDLLKELLGTGDNRAKDSHQQESTNNDEDSTSKRYGGFMRGLKRSPQLEDEAKELQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFAESLPSDEEGESYSKEVPEMEKRYGGFMRF | Function: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress.
PTM: Proenkephalin-A is cleaved by CTSL to generate Met-enkephalin.
Sequence Mass (Da): 30932
Sequence Length: 269
Subcellular Locati... |
Q9GMY3 | MKWMVVVLLCLQLLEAKVVKVPLKKLKSLRETMKEKGLLEEFLKNHKYDPAQKYRYTDFSVAYEPMAYMDAAYFGEISIGTPPQNFLVLFDTGSSNLWVPSVYCQTQACTGHTRFNPSQSSTYSTNGQTFSLQYGSGSLTGFFGYDTLTVQSIQVPNQEFGLSENEPGTNFVYAQFDGIMGMAYPSLAMGGATTALQGMLQEGALTSPVFSFYLSNQQGSQNGGAVIFGGVDNSLYQGQIYWAPVTQELYWQIGIEEFLIGGQASGWCSQGCQAIVDTGTSLLTVPQQYMSALLQATGAQEDQYGQFFVNCNYIQNLPTF... | Function: Hydrolyzes a variety of proteins.
Catalytic Activity: More restricted specificity than pepsin A, but shows preferential cleavage at Tyr-|-Xaa bonds. High activity on hemoglobin.
Sequence Mass (Da): 42921
Sequence Length: 389
Subcellular Location: Secreted
EC: 3.4.23.3
|
Q48558 | MKQTECTTILVGKKASIDGSTMIARSEDGGRVIIPEGFKVVNPEDQPKHYTSVISKQKIDDEDLAETPLRYTSAPDVSGKNGIWGAAGINADNVAMTATETITTNSRIQGVDPILDPSEGGLGEEDFVTLTLPYLHSAFDGVKRVGYLVEKYGTYEMNGMAFSDKDNIWYLETIGGHHWIARRIPDDAYVIAPNRLNIDTFDFDDSENFATASDLKDLIDEYHLNPDREGYNMRHIFGSSTIKDAHYNNPRAWYIHNYFDPDFGGTPADQDQPFICRANRLISIEDIKWAESSHYQDTPYDAYGDQGTPEQKKTFRPIGI... | Function: Hydrolyzes a wide range of dipeptides but unable to hydrolyze dipeptides containing proline. Highest activity against Met-Ala.
Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
Sequence Mass (Da): 53513
Sequence Length: 474
EC: 3.4.13.19
|
Q8G6Z9 | MACTTILVGKDASYDGSTIIARNEDSANGEFNPKRFIVVKPEEQPREYKSVISHLTITLPDDPLQYTAVPNADLKEGIWGEAGVNEANVAMSATETLTTNERVLGADPFVEYTPAKGDEPEVPGGIGEEDFLTIVLPYVKTAREGVQRLGALLEEFGTYEMNGVAFSDSNEIWWLETVGGHHWIAKRVPDEAYVTMPNQLGIDEFDLEDALGDQEAHMCSEDLAEFIETNHLDLAVENTTPFNPRDAFGSHSDSDHVYNTPRAWYMQRFLNPYDEVWDGPDADHKPTSDDIPWARQPERKVTIEDIKYVLSSHYQGTPFD... | Function: Hydrolyzes a wide range of dipeptides. Highest activity against Ala-Gln.
Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
Sequence Mass (Da): 59751
Sequence Length: 533
EC: 3.4.13.19
|
B8F8H3 | MQQLFSQHIARIQQIVQHALELARLDGLWIYAGQAKYHFLDDQTSPFKINPHFNYIFPDPTVEQSWLFLDGKNKPKLYFYAPQDYWHCTPNPPTSAFFADEFEWQMLTDSQQIQQYIINPTHCAFIGEQTELAKSLGFEHINPQKVLNVLHFERSIKSEFEIECIYQAQLTALAGHHAAKEAFFASKSEFEINLAYLQATKQSDNNVPYGNIVAINQHSAILHYTKLDFTPPCERHSFLLDAGTSYLGYASDLTRTYAFEPQSEFAAMIAQMEQFKLDTIADMQVGMNYLSYHTQMHRWISQMLHQFEFVKLPADQIFEE... | Cofactor: Binds 2 manganese ions per subunit.
Function: Splits dipeptides with a prolyl residue in the C-terminal position.
Catalytic Activity: H2O + Xaa-L-Pro dipeptide = an L-alpha-amino acid + L-proline
Sequence Mass (Da): 50882
Sequence Length: 440
EC: 3.4.13.9
|
Q2S6U2 | MSDSAYQNHLSILRKRFDQALLETDFDGVILASGRLTYYFGDDHSHPFHPYAMAQQWAPFDLMPDVFIHIQRGETPRLLWPAKQDFWHVVYPIPEGGWCDQWRVEPVSSLQEWLPQISGKTAWIGPEYNEAPGLNPNLSVNPEALLHRLNYQRAYKTEFEIDCLWRANQAGAAGHKAAQAAFLTGKSECDVYRDFLAASGQLSNQEPYPGIVALNENAAVLHYEKKNPLKPDAMRTLLIDAGAAYGGYASDITRTYTAGSGLFAELIERVNTLQLSIAAQAVHGKAFSELHQATLAGVANILHETRICSLSVEAQLDKRI... | Cofactor: Binds 2 manganese ions per subunit.
Function: Splits dipeptides with a prolyl residue in the C-terminal position.
Catalytic Activity: H2O + Xaa-L-Pro dipeptide = an L-alpha-amino acid + L-proline
Sequence Mass (Da): 48837
Sequence Length: 438
EC: 3.4.13.9
|
B9EAD7 | MKEKLIDRLTSYVVIDTQSDASSTTTPSTDKQWNLLNQLKQEIEQLGLETDIDEYGYLFATLPSNTNKDVPVIGLLAHVDTATDFTGTNVNPQIIQSYDGNDITLKSGLKIETAKFPELSLYKGHTLITTDGTTLLGADNKAGIAEIMTAIEYLIAHPEIKHGKIRFGFTPDEEIGRGPHKFDVERFACDFAYTIDGGRRGELQYESFNAAGVNVTFNGVNVHPGSAKDKMVNALNLAVRFQSSLPANEVPEHTEGYEGFFHLMELNGNVERAQLSYIIRDHSREQFEARKVKMHEIITSIQNEYGEQAAHIEINDQYYN... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Cleaves the N-terminal amino acid of tripeptides.
Catalytic Activity: Release of the N-terminal residue from a tripeptide.
Sequence Mass (Da): 45438
Sequence Length: 407
Subcellular Location: Cytoplasm
EC: 3.4.11.4
|
Q6D4E3 | MDKLLDRFLNYVSFDTQSKSGVRQVPSTDGQLKLARALQQELLELGFEQIVLSKQGCLTAALPSNVAWSVPAIGFISHMDTSPDFSGKNVNPQILENYRGGDIALGVGDEVLSPVMFPVLHQLLGHTLITTDGKTLLGADDKAGIAEIITALVRLKKSQLPHGDIRIAFTPDEEIGKGAQFFDVKAFNAQWAYTVDGGGVGELEYENFNAASVQVKIVGNNVHPGSAKGVMVNALTLASRYHQHVPESESPEQTEGYQGFYHLHSMKGSVERADLHYIVRDFDRNGFEQRKQTMLDIAEKVGAGLHPDCYIEVTITDTYY... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Cleaves the N-terminal amino acid of tripeptides.
Catalytic Activity: Release of the N-terminal residue from a tripeptide.
Sequence Mass (Da): 45106
Sequence Length: 410
Subcellular Location: Cytoplasm
EC: 3.4.11.4
|
P84516 | MSRAPTLAAAAAVAAVVLICSSSTATAADGNARQPPLAPGLSFDFYKRSCPKAESIVRSFVQDAVRRDVGLAAGLLRLHFHDCFVQGCDASVLLDGSATGPGEQQAPPNLTLRPTAFKAINDIHDRLHKECGGTVVSCSDVLALAARDSVVVSGGPSYKVPLGRRDSASFATQQDVLSGLPPPTAAVPALLAVLSKINLDATDLVALSGGHTIGLGHCTSFEDRLFPRPDPTLNATFAGQLRRTCPAKGTDRRTPLDVRTPNAFDNKYYVNLVNREGLFTSDQDLFSNARTRALVDKFARSQRDFFDQFAFSVVKMGQIK... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might ... |
P86103 | DNTAKEKDSPANLSLRTCAAGDNAEQPLDPSRNTFDNAYYIALQRQAGVLFSDQSLFTSAR | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
P86014 | VSCADILTMATRQFDNVYYKNLQQGK | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might ... |
P25625 | MRLAVVVTLLVHCFLVTCSPGDNLDEFIDCTYACEYNRRCPNSQINYIDPETNMFHDIEFFDTPPLYSKLLFWDCISDCDYQCQHIITRWRIDEEEEIYQFHGKWPFLRVLGTQEFFSTIFSIGNFIPHYKGFVKFSRIIREEGDRRRKNSRSILIWNYLYVTVAGMLAWTASSVFHCRDLIITEKLDYFFAGLTVLTGFHAIFARMTSMFLYPKIAQAFTASVAAIFALHILRLYVDWSYTYNMRFNIFFGVLQYILLIMLSCQNYHALQKQKLMGEFKKTAYSSFKRQIFKLCVIPILLVIVTTMAMSLELFDFFSYE... | Function: Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchors proteins. Required for phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodelin... |
Q42580 | MANAKPFCLLGFFCLLLQLFSIFHIGNGELEMNYYKESCPKAEEIIRQQVETLYYKHGNTAVSWLRNLFHDCVVKSCDASLLLETARGVESEQKSKRSFGMRNFKYVKIIKDALEKECPSTVSCADIVALSARDGIVMLKGPKIEMIKTGRRDSRGSYLGDVETLIPNHNDSLSSVISTFNSIGIDVEATVALLGAHSVGRVHCVNLVHRLYPTIDPTLDPSYALYLKKRCPSPTPDPNAVLYSRNDRETPMVVDNMYYKNIMAHKGLLVIDDELATDPRTAPFVAKMAADNNYFHEQFSRGVRLLSETNPLTGDQGEIR... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might ... |
Q7F1U0 | MASATNSSLSLMLLVAAAMASVASAQLSATFYDTSCPNALSTIKSVITAAVNSEARMGASLLRLHFHDCFVQGCDASVLLSGQEQNAGPNVGSLRGFSVIDNAKARVEAICNQTVSCADILAVAARDSVVALGGPSWTVLLGRRDSTTASEALANTDLPAPSSSLAELIGNFSRKGLDATDMVALSGAHTIGQAQCQNFRDRIYNETNIDSAFATQRQANCPRPTGSGDSNLAPLDTTTPNAFDNAYYSNLLSNKGLLHSDQVLFNGGSADNTVRNFASNAAAFSSAFTTAMVKMGNISPLTGTQGQIRLSCSKVNS | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might ... |
Q9ZV04 | MANKSLEIRFLFPLVLFLVVKLLCVDGKGFNNNGHKIRKGRWEGKLKMNFYHNSCPGAEDIVRQIVWKKVEANRSLAPKLLRVHYHDCFVRGCDASLLLDSVAGKAVSEKEARPNLSLSGFEIIDEIKYILEKRCPNTVSCADILTLAARDAVSYEFERPLWNVFTGRVDGRVSLATEAARDLPSAGANFTTLQKLFAESDLDVVDLVALSGAHTIGIAHCGVFGRRLLNFTGKGDTDPSLNPSYASFLKSECSDKSLRLNPSAVVGMDPTGPLAFDSGYFVSLLKNKGLFTSDAALLTDPSAAHIASVFQNSGAFLAQF... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might ... |
O80822 | MGVYLGKYCYIMIIMLVLVLGKEVRSQLLKNGYYSTSCPKAESIVRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKSAEQAALPNLGLRGLEVIDDAKARLEAVCPGVVSCADILALAARDSVDLSDGPSWRVPTGRKDGRISLATEASNLPSPLDSVAVQKQKFQDKGLDTHDLVTLLGAHTIGQTDCLFFRYRLYNFTVTGNSDPTISPSFLTQLKTLCPPNGDGSKRVALDIGSPSKFDESFFKNLRDGNAILESDQRLWSDAETNAVVKKYASRLRGLLGFRFDYEFGKAMIKMSSIDVKTDVDGEV... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might ... |
O22862 | MVMIHIFLTVMVVGGVSLFPETAEAIVMGPSMQKLTWHYYKVYNTCENAENFVRHQVEIFYKNDKSIAPKLLRLLYSDCFVSGCDASVLLEGPNSEKMAPQNRGLGGFVLIDKIKIVLEQRCPGVVSCADILNLATRDAVHLAGAPSYPVFTGRRDGLTSDKQTVDLPSPSISWDQAMSYFKSRGLNVLDMATLLGSHSMGRTHCSYVVDRLYNYNKTGKPSPTMNKYFLSEMAKQCPPRTRKGQTDPLVYLNPDSGSNHSFTSSFYSRILSNKSVLEVDQQLLYNDDTKQISKEFSEGFEDFRKSFALSMSKMGAINVL... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress (Probable). The enzyme ... |
Q43735 | MAASKRLVVSCLFLVLLFAQANSQGLKVGFYSKTCPQLEGIVKKVVFDAMNKAPTLGAPLLRMFFHDCFVRGCDGSVLLDKPNNQGEKSAVPNLSLRGFGIIDDSKAALEKVCPGIVSCSDILALVARDAMVALEGPSWEVETGRRDGRVSNINEVNLPSPFDNITKLISDFRSKGLNEKDLVILSGGHTIGMGHCPLLTNRLYNFTGKGDSDPSLDSEYAAKLRKKCKPTDTTTALEMDPGSFKTFDLSYFTLVAKRRGLFQSDAALLDNSKTRAYVLQQIRTHGSMFFNDFGVSMVKMGRTGVLTGKAGEIRKTCRSA... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might ... |
Q9SS67 | MKIATFSVLLLLLFIFPVALAQLKFKFYSESCPNAETIVENLVRQQFARDPSITAALTRMHFHDCFVQGCDASLLIDPTTSQLSEKNAGPNFSVRGFELIDEIKTALEAQCPSTVSCSDIVTLATRDAVFLGGGPSYVVPTGRRDGFVSNPEDANEILPPPFISVEGMLSFFGNKGMNVFDSVALLGAHTVGIASCGNFVDRVTNFQGTGLPDPSMDPTLAGRLRNTCAVPGGFAALDQSMPVTPVSFDNLFFGQIRERKGILLIDQLIASDPATSGVVLQYASNNELFKRQFAIAMVKMGAVDVLTGSAGEIRTNCRAF... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might ... |
Q9LSP0 | MKPKSKVAESTAASCFLVMSLLCSCIIGDQMETNNEGLSYSYYEKTCPKVEEIVRSSLSSMFILDPTSPAALLRLMFHDCQVQGCDASILLEPIRDQQFTELDSAKNFGIRKRDLVGSIKTSLELECPKQVSCSDVIILAARDAVALTGGPLISVPLGRKDSLSTPSKHVADSELPPSTADVDTTLSLFANKGMTIEESVAIMGAHTIGVTHCNNVLSRFDNANATSENMDPRFQTFLRVACPEFSPTSQAAEATFVPNDQTSVIFDTAYYDDAIAGRGNLRIDSEIGADPRTRPFVEAFAADQDRFFNAFSSAFVKLSS... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might ... |
Q9LV48 | MSTAPSPGTTPSPSPPSPPTNSTTTTPPPAASSPPPTTTPSSPPPSPSTNSTSPPPSSPLPPSLPPPSPPGSLTPPLPQPSPSAPITPSPPSPTTPSNPRSPPSPNQGPPNTPSGSTPRTPSNTKPSPPSDSSDGLSTGVVVGIAIGGVAILVILTLICLLCKKKRRRRHDDEAAYYVPPPPPSGPKAGGPYGGQQQYWQQQNASRPSDNHVVTSLPPPKPPSPPRKPPPPPPPPAFMSSSGGSDYSDLPVLPPPSPGLVLGFSKSTFTYEELSRATNGFSEANLLGQGGFGYVHKGILPSGKEVAVKQLKAGSGQGERE... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 69272
Sequence Length: 652
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9LK03 | MSSAPPPGGTPSPPPQPLPIPPPPQPLPVTPPPPPTALPPALPPPPPPTALPPALPPPPPPTTVPPIPPSTPSPPPPLTPSPLPPSPTTPSPPLTPSPTTPSPPLTPSPPPAITPSPPLTPSPLPPSPTTPSPPPPSPSIPSPPLTPSPPPSSPLRPSSPPPPSPATPSTPPRSPPPPSTPTPPPRVGSLSPPPPASPSGGRSPSTPSTTPGSSPPAQSSKELSKGAMVGIAIGGGFVLLVALALIFFLCKKKRRRDNEAPPAPIDGVPYGGQQQQNASRRSDHVVMSVPPPKSPSSAPPRPPHFMSSGSSGDYDSNYSD... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75380
Sequence Length: 717
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q1PEM5 | MARSNRCVPQNSSIVQIPIEEVFKTQLKSRWQQITMSSASSPPPPQVFVPEPLFSEPPPPPKAPVNVSLSPPPPPRSPSTSTPPRLGNRNPPPPASPSGQEPTTPTMTPGFSLSPPSPSRLSTGAVVGISIGGGVFVLTLIFFLCKKKRPRDDKALPAPIGLVLGIHQSTFTYGELARATNKFSEANLLGEGGFGFVYKGILNNGNEVAVKQLKVGSAQGEKEFQAEVNIISQIHHRNLVSLVGYCIAGAQRLLVYEFVPNNTLEFHLHGKGRPTMEWSLRLKIAVSSSKGLSYLHENCNPKIIHRDIKAANILIDFKFE... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56081
Sequence Length: 513
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9ZNQ8 | MASSPESAPPTNSTSSPSPPSNTNSTTSSPPAPSPPSPTPPQGDSSSSPPPDSTSPPAPQAPNPPNSSNNSPSPPSQGGGGERGNGGNNGGNDTPPSRGSPPSPPSRSNGDNGGSRSSPPGDTGGSRSDNPPSSGGSSGGGGGGRSNTNTAIIVGVLVGAGLLMIVLIIVCLRRKKKRKDSFYPEPMKGNQYQYYGNNNNNNASQNYPNWHLNSQGQNQQSTGGWGGGGPSPPPPPRMPTSGEDSSMYSGPSRPVLPPPSPALALGFNKSTFTYQELAAATGGFTDANLLGQGGFGYVHKGVLPSGKEVAVKSLKAGSGQ... | Function: Required during abscisic acid (ABA)-mediated activation of Ca(2+) channels. Regulates ABA signaling pathways. Modulates the expression of genes related to cell elongation and ABA signaling during root growth.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topol... |
Q8GX23 | MADSPVDSSPAPETSNGTPPSNGTSPSNESSPPTPPSSPPPSSISAPPPDISASFSPPPAPPTQETSPPTSPSSSPPVVANPSPQTPENPSPPAPEGSTPVTPPAPPQTPSNQSPERPTPPSPGANDDRNRTNGGNNNRDGSTPSPPSSGNRTSGDGGSPSPPRSISPPQNSGDSDSSSGNHPQANIGLIIGVLVGAGLLLLLAVCICICCNRKKKKKSPQVNHMHYYNNNPYGGAPSGNGGYYKGTPQDHVVNMAGQGGGNWGPQQPVSGPHSDASNLTGRTAIPSPQAATLGHNQSTFTYDELSIATEGFAQSNLLGQ... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 70902
Sequence Length: 670
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9LS95 | MAEGQSPENSPPSPTPPSPSSSDNQQQSSPPPSDSSSPSPPAPPPPDDSSNGSPQPPSSDSQSPPSPQGNNNNDGNNGNNNNDNNNNNNGNNNNDNNNGNNKDNNNNGNNNNGNNNNGNDNNGNNNNGNNNDNNNQNNGGGSNNRSPPPPSRNSDRNSPSPPRALAPPRSSGGGSNSSGNNEPNTAAIVGIVAGAGLLFLVMILFCVCCCRKKKKKHQMPYYAGNGYATGKGDQYQQQQYNNQSDHVMNLSQQYPGSNGNNNWMNSPPPPPPGSWQPSPPPPPPPVSGGMNGNSSDFSSNYSGPHGPSVPPPHPSVALGF... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 74687
Sequence Length: 700
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9XI96 | MAEGQSPENSPPAPPPPSPPSPPSSNDQQTTSPPPSDNQETTSPPPPSSPDIAPPPQQQQESPPPPLPENSSDGSSSSSPPPPSDSSSQSQSPPPPSTSPPQQSDNNGNKGNNNENNKGNDGSSGDGGNKNMSHTPPPPSKTSDHSSHSQPRSLAPPTSNSGSNSSSNDGLNIGAVIGLVAAAGILFIVMILLCVCCFRKKKKKSKLDQMPYYGSNAYPAGKTGGDQYYNQNAATQQQQHYNQNDHIVNLPPPPGSMGTNWVSSPPPPPPGNWQPMPSPPAPVSGGANVIQSGEMSSNFSSGPYAPSLPPPHPSVALGFN... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 74329
Sequence Length: 699
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9FFW5 | MSLVPPLPILSPPSSNSSTTAPPPLQTQPTTPSAPPPVTPPPSPPQSPPPVVSSSPPPPVVSSPPPSSSPPPSPPVITSPPPTVASSPPPPVVIASPPPSTPATTPPAPPQTVSPPPPPDASPSPPAPTTTNPPPKPSPSPPGETPSPPGETPSPPKPSPSTPTPTTTTSPPPPPATSASPPSSNPTDPSTLAPPPTPLPVVPREKPIAKPTGPASNNGNNTLPSSSPGKSEVGTGGIVAIGVIVGLVFLSLFVMGVWFTRKRKRKDPGTFVGYTMPPSAYSSPQGSDVVLFNSRSSAPPKMRSHSGSDYMYASSDSGMV... | Function: Could be involved in the negative regulation of root growth.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 72390
Sequence Length: 681
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9SX31 | MATTPVQPPVSNSPPVTSPPPPLNNATSPATPPPVTSPLPPSAPPPNRAPPPPPPVTTSPPPVANGAPPPPLPKPPESSSPPPQPVIPSPPPSTSPPPQPVIPSPPPSASPPPALVPPLPSSPPPPASVPPPRPSPSPPILVRSPPPSVRPIQSPPPPPSDRPTQSPPPPSPPSPPSERPTQSPPSPPSERPTQSPPPPSPPSPPSDRPSQSPPPPPEDTKPQPPRRSPNSPPPTFSSPPRSPPEILVPGSNNPSQNNPTLRPPLDAPNSTNNSGIGTGAVVGISVAVALVVFTLFGIFVWCLRKREKRLSAVSGGDVTP... | Function: Could be involved in the negative regulation of root growth.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75128
Sequence Length: 708
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
A0A452E9Y6 | MLVCLHLQVFLASVALFEVAASDTIAQAASTTTISDAVSKVKTQVNKAFLDSRTRLKTALSSEAPTTRQLSEYFKHAKGRTRTAIRNGQVWEESLKRLRRDTTLTNVTDPSLDLTALSWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLAVPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSSEHSKVQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPFFRAGFVCPTPPYQSLARDQINAVTSFLDASLVYGSEPSLASRL... | Cofactor: Binds 1 Ca(2+) ion per heterodimer.
Function: Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (By similarity). Also involved in the conversion of iodide (I(-)) into hypoiod... |
P22079 | MRVLLHLPALLASLILLQAAASTTRAQTTRTSAISDTVSQAKVQVNKAFLDSRTRLKTAMSSETPTSRQLSEYLKHAKGRTRTAIRNGQVWEESLKRLRQKASLTNVTDPSLDLTSLSLEVGCGAPAPVVRCDPCSPYRTITGDCNNRRKPALGAANRALARWLPAEYEDGLSLPFGWTPGKTRNGFPLPLAREVSNKIVGYLNEEGVLDQNRSLLFMQWGQIVDHDLDFAPDTELGSSEYSKAQCDEYCIQGDNCFPIMFPPNDPKAGTQGKCMPFFRAGFVCPTPPYKSLAREQINALTSFLDASFVYSSEPSLASRL... | Cofactor: Binds 1 Ca(2+) ion per heterodimer.
Function: Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (By similarity). Also involved in the conversion of iodide (I(-)) into hypoiod... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.