UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 2 35.2k | Functional Description stringlengths 5 30.7k |
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P43180 | MGVFNYESETTSVIPAARLFKAFILEGDNLIPKVAPQAISSVENIEGNGGPGTIKKINFPEGFPFKYVKDRVDEVDHTNFKYNYSVIEGGPVGDTLEKISNEIKIVATPDGGCVLKISNKYHTKGNHEVKAEQVKASKEMGETLLRAVESYLLAHSDAYN | May be a general steroid carrier protein. Causes an allergic reaction in human. Is a cause of type I allergic reactions in Europe, North America and USSR. Belongs to the BetVI family. |
P43183 | MGVFNYETEATSVIPAARLFKAFILDGDNLFPKVAPQAISSVENIEGNGGPGTIKKISFPEGFPFKYVKDRVDEVDHTNFKYSYSVIEGGPVGDTLEKISNEIKIVATPNGGSILKINNKYHTKGDHEVKAEQIKASKEMGETLLRAVESYLLAHSDAYN | May be a general steroid carrier protein. Pollen. Causes an allergic reaction in human. Is a cause of type I allergic reactions in Europe, North America and USSR. Belongs to the BetVI family. |
P43184 | MGVFNYESETTSVIPAARLFKAFILEGDTLIPKVAPQAISSVENIEGNGGPGTIKKITFPEGSPFKYVKERVDEVDHANFKYSYSMIEGGALGDTLEKICNEIKIVATPDGGSILKISNKYHTKGDHEMKAEHMKAIKEKGEALLRAVESYLLAHSDAYN | May be a general steroid carrier protein. Causes an allergic reaction in human. Is a cause of type I allergic reactions in Europe, North America and USSR. Belongs to the BetVI family. |
P43185 | MGVFNYETEATSVIPAARMFKAFILDGDKLVPKVAPQAISSVENIEGNGGPGTIKKINFPEGFPFKYVKDRVDEVDHTNFKYNYSVIEGGPVGDTLEKISNEIKIVATPDGGCVLKISNKYHTKGNHEVKAEQVKASKEMGETLLRAVESYLLAHSDAYN | May be a general steroid carrier protein. Interacts with brassinosteroids such as brassinolide and 24-epicastasterone. Causes an allergic reaction in human. Is a cause of type I allergic reactions in Europe, North America and USSR. Belongs to the BetVI family. |
P43186 | MGVFNYESETTSVIPAARLFKAFILDGDNLIPKVAPQAISSVENIEGNGGPGTIKKITFPEGSPFKYVKERVDEVDHANFKYSYSMIEGGALGDTLEKICNEIKIVATPDGGSILKISNKYHTKGDHEMKAEHMKAIKEKGEALLRAVESYLLAHSDAYN | May be a general steroid carrier protein. Causes an allergic reaction in human. Is a cause of type I allergic reactions in Europe, North America and USSR. Belongs to the BetVI family. |
Q9NZ33 | MESKEKRAVNSLSMENANQENEEKEQVANKGEPLALPLDAGEYCVPRGNRRRFRVRQPILQYRWDMMHRLGEPQARMREENMERIGEEVRQLMEKLREKQLSHSLRAVSTDPPHHDHHDEFCLMP | Signaling adapter molecule involved in p75NTR/NGFR signaling. Plays a role in cell cycle progression and neuronal differentiation. Inhibits neuronal differentiation in response to nerve growth factor (NGF). May act as a link between the cell cycle and neurotrophic factor signaling, possibly by functioning as an upstream modulator of receptor signaling, coordinating biological responses to external signals with internal cellular states (By similarity). Interacts with neurotrophin receptor p75NTR/NGFR. Interacts with OMP (By similarity). Shuttles between the cytoplasm and the nucleus. Expressed in central nervous system, with high level in pituitary, cerebellum and temporal lobe. Expressed in lung, skeletal muscle, peripheral blood leukocyte, stomach, lymph node, trachea and bone marrow. Highly expressed in acute myeloid leukemia. Phosphorylated. Phosphorylation of Ser-102 protects it from the proteasome (By similarity). Ubiquitinated. Degraded by the proteasome (By similarity). Belongs to the BEX family. Was named BEX2 by some authors. |
Q2PG52 | MESKEKRAVNNLSMENTNQENEEKEEKEQVANKGEPLALPLDAGEYCVPRGNRRRFRVRQPILQYRWDMMHRLGEPQARMREENMERIGEEVRQLMEKLREKQLSHSLRAVSTDPPHHDHHDEFCLMP | Signaling adapter molecule involved in p75NTR/NGFR signaling. Plays a role in cell cycle progression and neuronal differentiation. Inhibits neuronal differentiation in response to nerve growth factor (NGF). May act as a link between the cell cycle and neurotrophic factor signaling, possibly by functioning as an upstream modulator of receptor signaling, coordinating biological responses to external signals with internal cellular states (By similarity). Interacts with neurotrophin receptor p75NTR/NGFR. Interacts with OMP (By similarity). Shuttles between the cytoplasm and the nucleus. Phosphorylated. Phosphorylation of Ser-105 protects it from the proteasome (By similarity). Ubiquitinated. Degraded by the proteasome (By similarity). Belongs to the BEX family. |
Q9R1J2 | MESKDQGVKNLNMENDHQKKEEKEEKPQDTIRREPAVALTSEAGKNCAPRGGRRRFRVRQPIAHYRWDLMQRVGEPQGRMREENVQRFGGDVRQLMEKLRERQLSHSLRAVSTDPPHHDHHDEFCLMP | Signaling adapter molecule involved in p75NTR/NGFR signaling. Plays a role in cell cycle progression and neuronal differentiation. Inhibits neuronal differentiation in response to nerve growth factor (NGF). May act as a link between the cell cycle and neurotrophic factor signaling, possibly by functioning as an upstream modulator of receptor signaling, coordinating biological responses to external signals with internal cellular states (By similarity). Interacts with neurotrophin receptor p75NTR/NGFR (By similarity). Interacts with OMP. Shuttles between the cytoplasm and the nucleus. Primarily localized to neuronal cells within several regions of the brain, including the olfactory epithelium, bulb, peri/paraventricular nuclei, suprachiasmatic nucleus, arcuate nucleus, median eminence, lateral hypothalamic area, thalamus, hippocampus and cerebellum (at protein level). Expressed in brain, mid term embryos and to a lesser extent in ovary. In testis, it is expressed in the pachytene spermatocytes and spermatids but not in spermatogonia. Down-regulated following RA treatment. Up-regulated in parthenogenetic embryos. Phosphorylated. Phosphorylation of Ser-105 protects it from the proteasome (By similarity). Ubiquitinated. Degraded by the proteasome (By similarity). Belongs to the BEX family. Truncated N-terminus. |
Q6XUZ8 | MESKDQGAKNLNMENDHQKKEEKEEKPQDTIKREPVVAPTFEAGKNCAPRGGRRRFRVRQPIAHYRWDLMHRVGEPQGRMREENVQRFGEDMRQLMEKLRERQLSHSLRAVSTDPPHHDHHDEFCLMP | Signaling adapter molecule involved in p75NTR/NGFR signaling. Plays a role in cell cycle progression and neuronal differentiation. Inhibits neuronal differentiation in response to nerve growth factor (NGF). May act as a link between the cell cycle and neurotrophic factor signaling, possibly by functioning as an upstream modulator of receptor signaling, coordinating biological responses to external signals with internal cellular states. Interacts with OMP (By similarity). Interacts with neurotrophin receptor p75NTR/NGFR. Shuttles between the cytoplasm and the nucleus. Predominantly nuclear. Expressed in the central nervous system. Expressed in Schwann cells from newborn sciatic nerve. Oscillates during the cell cycle, being lowest at G1 and highest at S phase (at protein level). Phosphorylated. Phosphorylation of Ser-105 protects it from the proteasome. Ubiquitinated (Probable). Degraded by the proteasome (By similarity). Belongs to the BEX family. |
Q2TBV0 | MMPKEEQVLKNLTMENANEENEKKDEKEQDANKGEPLALSLGAGEYCVPRGNRRRFRVRQPILHYRWDMTQRLGKPQARMREENIERIGEEMRQLMEKLREKQLSHSLRAVSTDPPHHEHNDEFCLMP | Regulator of mitochondrial apoptosis and G1 cell cycle. Regulates the level of PP2A regulatory subunit B and PP2A phosphatase activity (By similarity). Interacts with OMP. Interacts with LMO2, possibly leading to regulate the transcriptional activity of a DNA-binding complex containing LMO2 (By similarity). Belongs to the BEX family. |
Q5JVV9 | MESKEERALNNLIVENVNQENDEKDEKEQVANKGEPLALPLNVSEYCVPRGNRRRFRVRQPILQYRWDIMHRLGEPQARMREENMERIGEEVRQLMEKLREKQLSHSLRAVSTDPPHHDHHDEFCLMP | Regulator of mitochondrial apoptosis and G1 cell cycle in breast cancer. Protects the breast cancer cells against mitochondrial apoptosis and this effect is mediated through the modulation of BCL2 protein family, which involves the positive regulation of anti-apoptotic member BCL2 and the negative regulation of pro-apoptotic members BAD, BAK1 and PUMA. Required for the normal cell cycle progression during G1 in breast cancer cells through the regulation of CCND1 and CDKN1A. Regulates the level of PP2A regulatory subunit B and PP2A phosphatase activity. Interacts with OMP (By similarity). Interacts with LMO2, possibly leading to regulate the transcriptional activity of a DNA-binding complex containing LMO2. Expressed in central nervous system, with high level in pituitary, cerebellum and temporal lobe. Widely expressed in breast cancer cell lines. Belongs to the BEX family. Was named BEX1 by some authors. |
Q9WTZ8 | MESKVEQGVKNLNMENDHQEKEEKEEKPQDASKRDPIVALPFEAGDYYVPRGGRRRFRVRQPIVHYRWDLMHRVGEPQGRMREENVQRFGDDVRQLMEKLRERQLSHSLRAVSTDPPHHDHHDEFCLMP | Regulator of mitochondrial apoptosis and G1 cell cycle. Regulates the level of PP2A regulatory subunit B and PP2A phosphatase activity (By similarity). Interacts with LMO2, possibly leading to regulate the transcriptional activity of a DNA-binding complex containing LMO2 (By similarity). Interacts with OMP. Primarily localized to neuronal cells within several regions of the brain, including the olfactory epithelium, bulb, peri/paraventricular nuclei, suprachiasmatic nucleus, arcuate nucleus, median eminence, lateral hypothalamic area, thalamus, hippocampus and cerebellum (at protein level). Belongs to the BEX family. |
Q3MKQ1 | MESKVEQGVKNLNMENDHQEKEEKEEKPQDANKREPVVALPFEAGEYYVPRGSRRRFRVRQPIAHYRWDLMHRVGEPQGRMREENVQRFGEDMRQLMEKLRERQLSHSLRAVSTDPPHHDHHDEFCLMP | Regulator of mitochondrial apoptosis and G1 cell cycle. Regulates the level of PP2A regulatory subunit B and PP2A phosphatase activity (By similarity). Interacts with LMO2, possibly leading to regulate the transcriptional activity of a DNA-binding complex containing LMO2. Interacts with OMP (By similarity). Belongs to the BEX family. |
Q3ZBJ6 | MANIHQENEEMEQPVQNGEEDRPLGGGEGHQPERNHRRGQARRLAPNFRWVIPNRQVNDGMGGEGDDMEIFMEEMREIRRKLRELQLRNCLRILMGELSNHHDHHDEFCLMP | May be a signaling adapter molecule involved in p75NTR-mediated apoptosis induced by NGF. Plays a role in zinc-triggered neuronal death (By similarity). Self-associates. Binds to the DEATH domain of p75NTR/NGFR. Interacts with 14-3-3 epsilon YWHAE. Interacts with DIABLO/SMAC. Shuttles between the cytoplasm and the nucleus. Associates with replicating mitochondria (By similarity). The nuclear export signal is required for export from the nucleus and the interactions with itself and p75NTR/NGFR. Ubiquitinated. Degraded by the proteasome (By similarity). Binds transition metals. Belongs to the BEX family. |
Q5JQT5 | MANIHQENEEMEQPMQNGEEDRPLGGGEGHQPAGNRRGQARRLAPNFRWAIPNRQINDGMGGDGDDMEIFMEEMREIRRKLRELQLRNCLRILMGELSNHHDHHDEFCLMP | May be a signaling adapter molecule involved in p75NTR-mediated apoptosis induced by NGF. Plays a role in zinc-triggered neuronal death (By similarity). May play an important role in the pathogenesis of neurogenetic diseases. Self-associates. Binds to the DEATH domain of p75NTR/NGFR. Interacts with 14-3-3 epsilon (YWHAE). Interacts with DIABLO/SMAC. Shuttles between the cytoplasm and the nucleus. Associates with replicating mitochondria (By similarity). Found in ovarian granulosa cells, testis, prostate and seminal vesicle tissue. High levels also detected in liver. The nuclear export signal is required for export from the nucleus and the interactions with itself and p75NTR/NGFR. Ubiquitinated. Degraded by the proteasome (By similarity). Binds transition metals. Belongs to the BEX family. |
Q9D1N5 | MANVHQENEEMEQPLQNGQEDRPVGGGEGHQPAANNNNNNHNHNHNHHRRGQARRLAPNFRWAIPNRQMNDGLGGDGDDMEMFMEEMREIRRKLRELQLRNCLRILMGELSNHHDHHDEFCLMP | May be a signaling adapter molecule involved in p75NTR-mediated apoptosis induced by NGF. Plays a role in zinc-triggered neuronal death. Self-associates (PubMed:11830582). Binds to the DEATH domain of p75NTR/NGFR (PubMed:11830582). Interacts with 14-3-3 epsilon (YWHAE) (PubMed:11278287). Interacts with DIABLO/SMAC (PubMed:15178455). Shuttles between the cytoplasm and the nucleus. Associates with replicating mitochondria. Widely expressed. The nuclear export signal is required for export from the nucleus and the interactions with itself and p75NTR/NGFR. Ubiquitinated (Probable). Degraded by the proteasome. Binds transition metals. Belongs to the BEX family. Extended C-terminus. |
Q9JIT2 | MANIHQENEEMEQPLQNGQEDRPVGGGEGHQPAANNNNHNHNHNHNHNHNHNHHRRGQARRLAPNFRWAIPNRQMNDGLGGDGDDMEMFMEEMREIRRKLRELQLRNCLRILMGELSNHHDHHDEFCLMP | May be a signaling adapter molecule involved in p75NTR-mediated apoptosis induced by NGF. Plays a role in zinc-triggered neuronal death. Self-associates. Binds to the DEATH domain of p75NTR/NGFR. Interacts with 14-3-3 epsilon (YWHAE). Interacts with DIABLO/SMAC. Shuttles between the cytoplasm and the nucleus. Associates with replicating mitochondria (By similarity). In cochlea, it is expressed in pillar cells from postnatal day 2 to adulthood. In neurons degenerating after kainate-induced seizures, likely in a zinc-dependent manner. The nuclear export signal is required for export from the nucleus and the interactions with itself and p75NTR/NGFR. Ubiquitinated (Probable). Degraded by the proteasome. Binds transition metals. Belongs to the BEX family. |
B9LW38 | MRLGVCYFPEHWPSEEWERDVAAMADAGLEYVRMAEFSWGVLEPERGTFDFEWLDEAIELIGDHGMQAVLCTPTATPPKWLVDERPSIRQEDPDGTVREHGSRRHYCFNSDAYREETARIVERVTERYADSPHVAGWQTDNEFGCHETVRCYCDDCADAFRTWLADRYGDIDRLNEAWGNAFWSQQYGSFDEIDPPGPTPAEHHPSRLLAYARFSSDSVVEYNRLHADLIREADPDWFVTHNFMGRFPTLNAYDVSEDLDRVAWDSYPTGFVQDRYDGEASPDQLRAGDPDQVGMDHDIYRSALDRPFWVMEQQPGDVNWPPHCPQPGEGAMRLWAHHAAAHGADAVLYFRWRRCLEGQEQYHAGLRKADGSPDRGYADAAHTSEEFATLDGASHVDAPVAVVFDYDSLWALNAQPHAPDFDYWALQEAFYGAVRGRGVQVDVVPPSADLSGYAAVVAPALHLVTEDLADRLTDYIAGGGEVLFGPRTGVKDAENKLRPMSQPGPLTDLVGATVDQHESLPRRLETTVRRVGDPTDDSEEIAAPPVSFRTWAEWLDPDAAEPQYAYDVDGPADGRPAVVTNTVGDGQVTYCGVWPESDLADALASDLLDRAGVRYAERLPDGVRIGYRGGRTWVTNFTSDRLRLPEIDPESLAVDDTDRDGFDPMADDDKDSSADGIVVGPYGVAVIEGDCVDGLRIAQT | Cleaves o-nitrophenyl-beta-D-galactopyranoside (ONPG) in vitro. Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Requires 4 M NaCl or KCl for maximal activity. Optimum pH is 6.5 with ONPG as substrate. Measured at 37 degrees Celsius and in 4 M KCl. Optimum temperature is around 50-55 degrees Celsius in 4 M KCl and at pH 6.5. Partial activity (10-13% of maximum) at temperatures from 4-10 degrees Celsius. Belongs to the glycosyl hydrolase 42 family. |
P83252 | TGVTYDHRALVIDGXXXVLVSGSIHYPRAASSWYAVET | Involved in cell wall degradation. Degrades polysaccharides containing beta-(1-->4)-linked galactans, acting as an exo-(1-->4)-beta-D-galactanase (By similarity). Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Heterodimer of a large and a small subunit. The small subunit is N-glycosylated. There are three forms of the large subunit which have the same sequence but differ in charge. There are four forms of the small subunit which have the same sequence but differ in charge. Belongs to the glycosyl hydrolase 35 family. |
P16279 | MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKVPEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQHYGFVLYRTTLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENMGRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVRSHLGGWGHRDSGHHDEAWAHNSSNYTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVDRPVIGSSVTYDHPSKPVEKRLMPPPPQKNKDSWLDHV | Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. Has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers. Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Optimum pH is 4.5-5.5. Homodimer (PubMed:22128166). May form higher multimers (Probable). Localized to the perinuclear area of the cytoplasm but not to lysosomes. Detected in placenta (at protein level) (PubMed:8383699). Detected in fibroblasts and testis (PubMed:2511208). The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Belongs to the glycosyl hydrolase 35 family. Beta-galactosidase entry |
B5XQY2 | MQISDTGHSHMPDFHAVLAREDWQNQTITHLNRLPAHPAFASWRDELAARDNHLSTRRRQLDGEWQFVYARSPFAVDAQWLTQDLPDSRGTPVPSNWQMEGYDAPIYTNVRYPIDTTPPRVPEDNPTGCYSLHFTVEDTWRENGQTQIIFDGVNSAFHLWCNGVWVGYSQDSRLPAAFDLSPFLRPGDNRLCVMVMRWSAGSWLEDQDMWRMSGIFRSVWLLNKPQQRLCDVQLTPALDALYRDGTLQVQATVEATEAALAGLSVGVSLWRGEEQVAAGRQPLGTPAVDERGHYAERVDFALAVTAPAHWSAETPNCYRAVVTLWRGDELLEAEAWDIGFRRIEIADGLLRLNGKPLLIRGVNRHEHHYLRGQVVTEADMVQDILLMKQNNFNAVRCSHYPNAPRWYELCNRYGLYVVDEANIETHGMVPMNRLSDDPAWLPAFSARVTRMVQSNRNHPCIIIWSLGNESGGGGNHEALYHWLKRNDPSRPVQYEGGGADTTATDIICPMYARVERDQPIPAVPKWGIKKWISLPGEQRPLILCEYAHAMGNSLGNFADYWQAFREYPRLQGGFIWDWADQAIRKIFDDGSVGWAYGGDFGDKPNDRQFCMNGLVFPDRTPHPSLVEAKHAQQYFQFTLLSTSPLRVRITSEYLFRPTDNEVVRWQVQSAGETLYHGNLTLALPPEGSDEITLLDSLILPEGARAVWLTLEVTQPRATDWSEADHRVAWQQFPLPAPLALPAPTVPAGAPDLIVSDEVWQIRAGSQCWTIDRRTGLLSRWSVGGQEQLLTPLRDQFIRAPLDNDIGVSEVERIDPNAWVERWKSAGLYDLEAHCVQCDAQRLANETLVDCRWHYLRGEEVVIVSHWRMHFTADGTLRLAVDGERAETLPPLPRVGLHFQVADQQAPVSWLGLGPHENYPDRRSSACFARWEQPLAAMTTPYIFPTENGLRCDTQALDWGRWHVSGHFHFSVQPWSTRQLMETDHWHKMQAEDGVWITLDGLHMGVGGDDSWTPSVLPQWLLSQTRWQYEFFLRCL | Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Binds 2 magnesium ions per monomer. Binds 1 sodium ion per monomer. Homotetramer. Belongs to the glycosyl hydrolase 2 family. |
P00723 | MSCLIPENLRNPKKVHENRLPTRAYYYDQDIFESLNGPWAFALFDAPLDAPDAKNLDWETAKKWSTISVPSHWELQEDWKYGKPIYTNVQYPIPIDIPNPPTVNPTGVYARTFELDSKSIESFEHRLRFEGVDNCYELYVNGQYVGFNKGSRNGAEFDIQKYVSEGENLVVVKVFKWSDSTYIEDQDQWWLSGIYRDVSLLKLPKKAHIEDVRVTTTFVDSQYQDAELSVKVDVQGSSYDHINFTLYEPEDGSKVYDASSLLNEENGNTTFSTKEFISFSTKKNEETAFKINVKAPEHWTAENPTLYKYQLDLIGSDGSVIQSIKHHVGFRQVELKDGNITVNGKDILFRGVNRHDHHPRFGRAVPLDFVVRDLILMKKFNINAVRNSHYPNHPKVYDLFDKLGFWVIDEADLETHGVQEPFNRHTNLEAEYPDTKNKLYDVNAHYLSDNPEYEVAYLDRASQLVLRDVNHPSIIIWSLGNEACYGRNHKAMYKLIKQLDPTRLVHYEGDLNALSADIFSFMYPTFEIMERWRKNHTDENGKFEKPLILCEYGHAMGNGPGSLKEYQELFYKEKFYQGGFIWEWANHGIEFEDVSTADGKLHKAYAYGGDFKEEVHDGVFIMDGLCNSEHNPTPGLVEYKKVIEPVHIKIAHGSVTITNKHDFITTDHLLFIDKDTGKTIDVPSLKPEESVTIPSDTTYVVAVLKDDAGVLKAGHEIAWGQAELPLKVPDFVTETAEKAAKINDGKRYVSVESSGLHFILDKLLGKIESLKVKGKEISSKFEGSSITFWRPPTNNDEPRDFKNWKKYNIDLMKQNIHGVSVEKGSNGSLAVVTVNSRISPVVFYYGFETVQKYTIFANKINLNTSMKLTGEYQPPDFPRVGYEFWLGDSYESFEWLGRGPGESYPDKKESQRFGLYDSKDVEEFVYDYPQENGNHTDTHFLNIKFEGAGKLSIFQKEKPFNFKISDEYGVDEAAHACDVKRYGRHYLRLDHAIHGVGSEACGPAVLDQYRLKAQDFNFEFDLAFE | Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Belongs to the glycosyl hydrolase 2 family. |
Q5FJ37 | MQANIKWLDDPEIFRVNQLPAHSDHPFFKNYREWQNNHSSFKQSLNGMWQFKFSKDPQSRPVDFYKKDFNTSSFTTIPVPSEIELNNFAQNQYINTLYPWEGKIFRRPAYALNKSDAEEGSFSEGKDNTVGSYIKHFDLNPELRDHDIHIVFEGAERAMYVWLNGHFIGYAEDSFTPSEFDLTKYIKEKDNILAVEVFKHSTASWLEDQDMFRFSGLFRSVELLAFPETHLVDLDLKPTVCDNYQDGIFNAELKFTGSLNGHVHLSVEDVNGSAILEQDVPLDSEVEFTSSTLENIHLWDNHHPYLYQLLIEVHDENGHLVELIPYQFGFRRIEINQDKVILLNGKCLIINGVNRHEWNAKTGRSITLNDMEKDIDTFKENNINAVRTCHYPNQIPWYYLCDQNGIYMMAENNLESHGTWQKMGQVEPSDNVPGSVPEWREAVIDRARNNYETFKNHTSILFWSLGNESYAGSNIVAMNEFYKEHDSSRLVHYEGVVHRPELKDQISDIESHMYLPPKEVAEYLRNNPQKPFMECEYMHDMGNSDGGMGSYIKLIDEYPQYVGGFIWDFIDQALLVYDPISKQNVLRYGGDFDDRHSDYEFSGDGLMFADRTPKPAMQEVRYYYGLHK | Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Heterodimer of a large and a small subunit. Belongs to the glycosyl hydrolase 2 family. |
P20043 | MSNKLVKEKRVDQADLAWLTDPEVYEVNTIPPHSDHESFQSQEELEEGKSSLVQSLDGDWLIDYAENGQGPVNFYAEDFDDSNFKSVKVPGNLELQGFGQPQYVNVQYPWDGSEEIFPPQIPSKNPLASYVRYFDLDEAFWDKEVSLKFDGAATAIYVWLNGHFVGYGEDSFTPSEFMVTKFLKKENNRLAVALYKYSSASWLEDQDFWRMSGLFRSVTLQAKPRLHLEDLKLTASLTDNYQKGKLEVEANIAYRLPNASFKLEVRDSEGDLVAEKLGPIRSEQLEFTLADLPVAAWSAEKPNLYQVRLYLYQAGSLLEVSRQEVGFRNFELKDGIMYLNGQRIVFKGANRHEFDSKLGRAITEEDMIWDIKTMKRSNINAVRCSHYPNQSLFYRLCDKYGLYVIDEANLESHGTWEKVGGHEDPSFNVPGDDQHWLGASLSRVKNMMARDKNHASILIWSLGNESYAGTVFAQMADYVRKADPTRVQHYEGVTHNRKFDDATQIESRMYAPAKVIEEYLTNKPAKPFISVEYAHAMGNSVGDLAAYTALEKYPHYQGGFIWDWIDQGLEKDGHLLYGGDFDDRPTDYEFCGNGLVFADRTESPKLANVKALYANLKLEVKDGQLFLKNDNLFTNSSSYYFLTSLLVDGKLTYQSRPLTFGLEPGESGTFALPWPEVADEKGEVVYRVTAHLKEDLPWADEGFTVAEAEEVAQKLPEFKPEGRPDLVDSDYNLGLKGNNFQILFSKVKGWPVSLKYAGREYLKRLPEFTFWRALTDNDRGAGYGYDLARWENAGKYARLKDISCEVKEDSVLVKTAFTLPVALKGDLTVTYEVDGRGKIAVTADFPGAEEAGLLPAFGLNLALPKELTDYRYYGLGPNESYPDRLEGNYLGIYQGAVKKNFSPYRPQETGNRSKVRWYQLFDEKGGLEFTANGADLNLSALPYSAAQIEAADHAFELTNNYTWVRALSAQMGVGGDDSWGQKVHPEFCLDAQKARQLRLVIQPLLLK | Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Monomer. Belongs to the glycosyl hydrolase 2 family. |
Q7WTB4 | MQANINWLDNPEVFRVNQLPAHSDHPFFRDYREWQKQHSSYQQSLNGKWKFHFSANPMDRPQDFYQRDFDSSNFDSIPVPSEIELSNYTQNQYINVLFPWEGKIFRRPAYALDPNDHEEGSFSKGADNTVGSYLKRFDLSSALIGKDVHIKFEGVEQAMYVWLNGHFVGYAEDSFTPSEFDLTPYIQDKDNLLAVEVFKHSTASWLEDQDMFRFSGIFRSVELLGIPATHLMDMDLKPRVADNYQDGIFNLKLHFIGKKAGSFHLLVKDIKGHTLLEKNEDIKENVQINNEKFENVHLWNNHDPYLYQLLIEVYDEQQNLLELIPFQFGFRRIEISPEKVVLLNGKRLIINGVNRHEWDAKRGRSITMSDMTTDINTFKENNINAVRTCHYPNQIPWYYLCDQNGIYVMAENNLESHGTWQKMGEIEPSDNVPGSIPQWKEAVIDRARINYETFKNHTSILFWSLGNESYAGDNIIAMNEFYKSHDDTRLVHYEGVVHRPELKDKISDVESCMYLPPKKVEEYLQNDPPKPFMECEYMHDMGNSDGGMGSYIKLLDKYPQYFGGFIWDFIDQALLVHDEISGHDVLRYGGDFDDRHSDYEFSGDGLMFADRTPKPAMQEVRYYYGLHK | Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Heterodimer of a large and a small subunit. By lactose. Belongs to the glycosyl hydrolase 2 family. |
Q9CE65 | MAMMTMIDVLERKDWENPVVSNWNRLPMHTPMDLLEKQSLNGLWNFDHFSRISDVPKNWLELTESKTEIIVPSNWQIEFKDKSDVPIYTNVTYPIPIQPPYVPEANPVGAYSRYFDITKEWLESGHVHLTFEGVGSAFHFWLNGEYGGYSEDSRLPAEFDISNLAKEGQNCLKVLVFRWSKVTYFEDQDMWRMSGIFRSVNLQWLPDNYLLDFSIKTDLDEDLDFANVKLQAYAKNIDDACLEFKLYDDEQLIGECHGFDAEIGVVNPKLWSDEIPYLYRLELTLMDRSGAVFHKETKKIGIRKIAIEKGQLKINGKALLVRGVNKHEFTPEHGYVVSEEVMIKDIKLMKEHNFNAVRCSHYPNDSRWYELCDEYGLYVMDEANIETHGMTPMNRLTNDPTYLPLMSERVTRMVMRDRNHPSIIIWSLGNESGYGSNHQALYDWCKSFDSSRPVHYEGGDDASRGATDATDIICPMYARVDSPSINAPYSLKTWMGVAGENRPLILCEYAHDMGNSLGGFGKYWQAFREIDRLQGGFIWDWVDQGLLKDGNYAYGGDFGDKPNDRQFSLNGLVFPNRQAKPALREAKYWQQYYQFELEKTPLGQVFAFTVTNEYLFRSTDNEKLCYQLINGLEVLWENELILNMPAGGSMRIDLSELPIDGTDNLFLNIQVKTIEKCNLLESDFEVAHQQFVLQEKINFTDRIDSNEEITLFEDEELLTVRSAKQKFIFNKSNGNLSRWLDEKGNEKLLHELSEQFTRAPLDNDIGVSEVEHIDPNAWLERWKGIGFYELKTLLKTMIIQATENEVIISVQTDYEAKGKIAFSTIREYHIFRNGELLLKVDFKRNIEFPEPARIGLSLQLAEKAENVTYFGLGPDENYPDRRGASLFGQWNLRITDMTTPYIFPSENGLRMETRELNYDRLKVRAMGQSFAFNLSPYSQNQLAKKGHWHLLEEEAGTWLNIDGFHMGVGGDDSWSPSVAQEYLLTKGNYHYEVSFKLT | Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Belongs to the glycosyl hydrolase 2 family. |
Q48846 | MQPNIQWLDTPAVFRVGQLPAHSDHRYYATLAEMAQQQSSFEQSLNGTWQFHYSVNAASRPKSFYELAFDAQDFEPITVPQHIELAGYEQLHYINTMYPWEGHYYRRPAFSTSDDKQHLGMFSEADYNPVGSYLHHFDLTPALRNQRVIIRFEGVEQAMYVWLNGQFIGYAEDSFTPSEFDLTPYLKETDNCLAVEVHKRSSAAFIEDQDFFRFFGIFRDVKLLAKPRTHLEDLWVIPEYDVVQQTGQVKLRLQFSGDENRVHLRIRDQHQIILTADLTSGAQVNDLYKMPELVQAWSNQTPNLYTLELEVVDQAGETIEISQQPFGFRKIEIKDKVMLLNGKRLVINGVNRHEWHPETGRTITAEDEAWDIACMQRNHINAVRTSHYPDRLSFYNGCDQAGIYMMAETNLESHGSWQKMGAVEPSWNVPGSYDEWEAATLDRARTNFETFKNHVSILFWSLGNESYAGSVLEKMNAYYKQQDPTRLVHYEGVFRAPEYKATISDVESRMYATPAEIKAYLDNAPQKPFILCEYMHDMGNSLGGMQSYIDLLSQYDMYQGGFIWDFIDQALLVTDPVTGQRELRYGGDFDDRPSDYEFSGDGLVFATRDEKPAMQEVRYYYGEHK | Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Heterodimer of a large and a small subunit. Belongs to the glycosyl hydrolase 2 family. |
Q02603 | MQANLQWLDDPEVFRVNQLPAHSDHHYYHDTAEFKTGSRFIKSLNGAWRFNFAKTPAERPVDFYQPDFDATDFDTIQVPGHIELAGYGQIQYINTLYPWEGKIYRRPPYTLNQDQLTPGLFSDAADNTVGSYLKTFDLDDVFKGQRIIIQFQGVEEALYVWLNGHFIGYSEDSFTPSEFDLTPYIQDQGNVLAVRVYKHSTAAFIEDQDMFRFSGIFRDVNILAEPASHITDLDIRPVPNANLKSGELNITTKVTGEPATLALTVKDHDGRVLTSQTQTGSGSVTFDTMLFDQLHLWSPQTPYLYQLTIEVYDADHQLLEVVPYQFGFRTVELRDDKVIYVNNKRLVINGVNRHEWNAHTGRVISMADMRADIQTMLANNINADRTCHYPDQLPWYQLCDEAGIYLMAETNLESHGSWQKMGAIEPSYNVPGDNPHWPAAVIDRARSNYEWFKNHPSIIFWSLGNESYAGEDIAAMQAFYKEHDDSRLVHYEGVFYTPELKDRISDVESRMYEKPQNIVAYLEDNPTKPFLNCEYMHDMGNSLGGMQSYNDLIDKYPMYQGGFIWDFIDQALFVHDPITDQDVLRYGGDFDERHSDYAFSGNGLMFADRTPKPAMQEVKYYYGLHK | Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Heterodimer of a large and a small subunit. Belongs to the glycosyl hydrolase 2 family. |
Q03WL0 | MTSIKQILARHDWENPVVTNWNRLPLHTSMSYANERNKREIKQPRKSLNGPWQFSYFENLSDIDEEWRKKDLPTSKIIHVPSNWQLQGDYDVPVYTNVTYPFPVNPPYVPTENPVGAYSKKVFLDNKWLADNTESHVVFNGVGSAFYLWVNGEWVGYSEDSRLPAEFDITEELRAGENRIAVLVLKWSKGSYFEDQDMWRMSGIFRDVDLIRVPKTRFQDLAIETKLDEDLDDATVEVRAQLVGNSADNLSVTAELFYHGMSLFKATEQFGNRVIDERGTNDGQVSLELPVKNPALWSAEVPNLYDIKVSLHDGEENYQIENKKVGIRKVQIKDGLLTLNNQPLLIRGVNKHEFNSKTGYYVDEKTMIDDIRMMKEHNFNAVRLSHYPNASRWYELCDQYGLYLVDEANIETHGVKPMNYLTNDPKYLPLMMERVTRMVQRDYNHPSIIIWSLGNESGYGHNHDAMYQWIKNTDPSRPIQYEGGGADTPATDIIAPMYARVDQDQVEEVNSKWAIKKWIGLSKENRPLILCEYAHSMGNSLGGFNKYWEAFEKYPRLQGGFIWDWVDQGLLTKNNEGQSYYAYGGDFGDYPNDRQFSLDGLLFPDRTPKPALLEAKYCQQYFAFQLEKDPTGKVNYMTVSNKHLFKTVNDATLIYQILSNDQVIETKKIKLNLAPQTEERVSLNFSDNSNEDVYMNCQIVQDSTDGLIRSGTLLAYKQFILRNKPIMISDVRSSDDYEDFLINDATDSLSISLDDAIWQFNKRTGWLSNWIKNGQEKVLTPLKDQFSRAALDNDIGVSEVTNIDPNAWFERWQATGFNHLNEKLVQFNWTALKDEVRITTQHQFLSPIDQHIMFISSKEYRINHVGDLKVYVDVWRQVADPQPARIGLSVQINATTDAVTYSGLGPMENYPDRRSAAIRGKWDASLKELYTPYVFPSENGLRTEVAYLKFDHHVIRALEQRFSFNLSQFSQAQLSAVTHQHLLKPEEGVWLNIDGYHMGVGGDDSWSPSVSPEFLLSNDHYHYSFSWSNAEGEANV | Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Binds 2 magnesium ions per monomer. Binds 1 sodium ion per monomer. Homotetramer. Belongs to the glycosyl hydrolase 2 family. |
Q4R564 | MPGFLVRILPLLLPLLLLGPTRGLRNATRRVFEIAYSQDRFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNTIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKEAILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPIITVQVENEYGSYFACDFDYLRFLQKRFHHHLGDDVVLFTTDGAHETFLQCGALQGLYTTVDFGPGSNITDAFQIQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEVVASSLYDILARGASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNVIQKFEKVPEGPIPPSTPKFAYGKVSLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQYYGFVLYRTTLPQDCSNSTPLSSPFNGVHDRAYVAVDGIPQGVLERNRVITLNITGKTGATLDLLVENMGRVNYGAYINDFKGLVSNLTLDSNILTGWTIFPLDTEDAVRSHLGGWEHRDSGRHDEAWAHSSSNYTLPAFYVGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELERAPCSSDGPELCAVEFVDRPVIGSSQIYDHLSKPVEQRLMAPPPKKTKIRGWSMYDDESL | Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Homodimer. May form higher multimers. Belongs to the glycosyl hydrolase 35 family. |
P48981 | MGVGIQTMWSILLLFSCIFSAASASVSYDHKAIIINGQKRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEERYDLVKFIKLVQQEGLFVNLRIGPYVCAEWNFGGFPVWLKYVPGIAFRTDNEPFKAAMQKFTEKIVSMMKAEKLFQTQGGPIILSQIENEFGPVEWEIGAPGKAYTKWAAQMAVGLDTGVPWIMCKQEDAPDPVIDTCNGFYCENFKPNKDYKPKMWTEVWTGWYTEFGGAVPTRPAEDVAFSVARFIQSGGSFLNYYMYHGGTNFGRTAGGPFMATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKSCESALVSVDPSVTKLGSNQEAHVFKSESDCAAFLANYDAKYSVKVSFGGGQYDLPPWSISILPDCKTEVYNTAKVGSQSSQVQMTPVHSGFPWQSFIEETTSSDETDTTTLDGLYEQINITRDTTDYLWYMTDITIGSDEAFLKNGKSPLLTIFSAGHALNVFINGQLSGTVYGSLENPKLSFSQNVNLRSGINKLALLSISVGLPNVGTHFETWNAGVLGPITLKGLNSGTWDMSGWKWTYKTGLKGEALGLHTVTGSSSVEWVEGPSMAEKQPLTWYKATFNAPPGDAPLALDMGSMGKGQIWINGQSVGRHWPGYIARGSCGDCSYAGTYDDKKCRTHCGEPSQRWYHIPRSWLTPTGNLLVVFEEWGGDPSRISLVERGTALDAKKL | Involved in cell wall degradation. Degrades polysaccharides containing beta-(1-->4)-linked galactans, acting as an exo-(1-->4)-beta-D-galactanase. Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Belongs to the glycosyl hydrolase 35 family. |
P23780 | MLRVPLCTPLPLLALLQLLGAAHGIYNVTQRTFKLDYSRDRFLKDGQPFRYISGSIHYFRIPRFYWEDRLLKMKMAGLNAIQMYVPWNFHEPQPGQYEFSGDRDVEHFIQLAHELGLLVILRPGPYICAEWDMGGLPAWLLEKQSIVLRSSDPDYLVAVDKWLAVLLPKMKPLLYQNGGPIITVQVENEYGSYFACDYDYLRFLVHRFRYHLGNDVILFTTDGASEKMLKCGTLQDLYATVDFGTGNNITQAFLVQRKFEPKGPLINSEFYTGWLDHWGKPHSTVKTKTLATSLYNLLARGANVNLYMFIGGTNFAYWNGANTPYEPQPTSYDYDAPLSEAGDLTKKYFALREVIQMFKEVPEGPIPPSTPKFAYGKVALRKFKTVAEALGILCPNGPVKSLYPLTFTQVKQYFGYVLYRTTLPQDCSNPKPIFSSPFNGVRDRAYVSVDGVPQGILDRNLMTALNIRGKAGATLDILVENMGRVNYGRFINDFKGLISNMTINSTVLTNWTVFPLNTEAMVRNHLWGREASDEGHLDGRSTSNSSDLILPTFYVGNFSIPSGIPDLPQDTFIQFPGWSKGQVWINGFNLGRYWPTMGPQKTLFVPRNILTTSAPNNITVLELEFAPCSEGTPELCTVEFVDTPVIS | Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Homodimer. May form higher multimers. Belongs to the glycosyl hydrolase 35 family. |
Q04F24 | MTNKISFRDIINRKDWENPVITNWHRLPIHTEMNYSKSLNEDKQKTIQSLNGNWCFSYFSKVTDVPENWADRDLTKSNIMPVPSNWQLHGYDQPIYSNVAYPFPANPPYLPEENPTACYSRIFQLNDDWLQSGQNHVIFNGVGSAFHLWLNGQWIGYSEDSRLPAEFDLTKYLKSGKNRISVMVLRWSKGSYFEDQDMWRMSGIFRDVEVKHLPATYLQDYQLQTDLDDDLDQAKITIKAQVAGKNFSQNKLRTRLYFANEKVADQSSRLSTRAVDERGPLDNQFIAELNLKDPYLWSAELPYLYQLVIELLTDDGDILQVEKVNIGVRKVEIKNGLLKLNGKPLLIRGTNKHEFDSKKGYAVDEETMIQDIKAMKRNNFNAVRCSHYPNNRRWYELCDQYGLYVVDEANIETHGMVPMNRLTNDPVYLPLMSDRVTRMVTRDRNHPSIIIWSLGNESGYGRNHAALYNWIKQSDLSRPVQYEGGGANTAVTDIIVPMYARVEQDQIESVNSKWSLKKWIGLPGETRPLILCEYAHDMGNSLGGFGKYWQAFHKYPRLQGGFIWDWVDQGLLKKDVNGNDFYAYGGDFKDQPNDRQFCLDGLLFPDRTPKPAMHEVKYWQQYYLFNLQRNPLGQAESFTVTNDYSFKKSSNERLHYQIKSENEIVIDKYIDLVLNPGESLLIKLPKGRSSTSSLLDIDISLIKGNSWAPSGFKIASEQYVLAKKFGPTNAVTAATNKISLIENKDTNTFEIKLDDQKWQFAKNSGLLVSWSKSGNENLLDALRDQFTRAPLDNDIGVSKVDHIDPNAWYERWKSAGMYNLKTNLVSIDAEQLERAVLIRTEHSYSNHFQILFKSSKIYRIDANGTMTVTVDVSLAQGIPFPARIGLTCHLADQITDVSYTGLGPFENYPDRQSAAQYGHWQMELDDLYTPYIFPSENGSRGQVSQLEFGKQKISAYHEQNFSFNLSRFSKQQLARISHRNLLQAENGVWLSIDGYRMGVGGDDSWSPSVAPEYLLSNNYYHYAFQWCRKDI | Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Binds 2 magnesium ions per monomer. Binds 1 sodium ion per monomer. Homotetramer. Belongs to the glycosyl hydrolase 2 family. |
Q6D736 | MSDSVLSNPTRQHATLREILARRDWENPACTNYQRLPAHPPFNSWRNVAAAHQDEPSQRLRRLNGEWKFSYFTRPEAVPESWLQQDLPDSATIPVPSNWQLQGYDTPIYTNVKYPIPVNPPYVPEDNPTGCYSLTFKVNHDWLSCGQTRVIFDGVNSAFYLWCNGHWVGYSQDSRLPAEFDISRYLTTGENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDVTLLHKPTVHLGDIQLTTPLSADFRHGTLDIQVKATLSESEAKNYRVHAQLWRGNNLIGETRQAFGSDIVDERGTYHDRASLRLDVTRPDLWSAELPHLYRAVIALETAEGELLEAEAYDVGFRKVEISNGLLLLNGKPLLIRGVNRHEHHPQNGQVMDEETMRRDIMLMKQHNFNAVRCSHYPNHPLWYRLCDRYGLYVVDEANIETHGMQPMNRLSDDPMWLPAYSERVSRMVQRDRNHPCIIIWSLGNESGYGANHDALYQWIKRHDPTRPVHYEGGGANSRATDIVCPMYARVDEDQPFPNVPKWSISKWISMPNEHRPLILCEYAHAMGNSLGGFARYWKAFRQYPRLQGGFIWDWVDQALIRHDEQGNAYWAYGGDFGDMPNDRQFCLDGLLFPDRTPHPSLYEAQRAQQHIQFVWQAESPCELRVTSEYLFRHTDNEQLNWHITLDDKTLVEGSLPLKLAPQATQTLTLLESLPTVDRAGEIWLNVEVVQPKETAWSKANHRCAWDQWQLPIPLHLPEASCSKQKIPPVLRASDIYFDVVQGEQHWRFNRQSGLLEQWWTADTPALLTPLQDQFVRAPLDNDIGISEVDRIDPHAWAERWKSAGLYQLQTQCVAIQADQLADAVHIVTEHVFRHAGQILLRSKKRWQIDAYGVMTVDVDVDVATVLPSLARVGLSCQLADVAPQVSWIGLGPHENYPDRQLAAQHGHWNLPLDDLHTPYIFPSENGLRCNTRALTYGKWAITGNFHFGLSRYGLTQLMTCTHHHLLEKEKGVWLNLDGFHMGIGGDDSWSPSVHCDDLLTATHYHYRVAIQRH | Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Binds 2 magnesium ions per monomer. Binds 1 sodium ion per monomer. Homotetramer. Belongs to the glycosyl hydrolase 2 family. |
P85412 | EIQNAGLYAILR | Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Causes an allergic reaction in human. Binds to IgE. On the 2D-gel the determined pI of this protein is: 6.23, its MW is: 90 kDa. Belongs to the glycosyl hydrolase 35 family. |
Q6LL68 | MALSDIIQRRDWENPQSVNIHCLKAHSPLASYRDINHARDGIHAQRQSLNGQWKFKLFDAPEQVEGEFIDVQFNDSAWGDITVPSNWQLQGYDKPIYANVKYPFEVNPPYVPADNPTGCYRTRLTLTEADLESTQRIIFDGVNSAFHLWCNGDWVGYSQDSRLPAEFDLSQYLTAGENTLAVMVIRWSDGSYLEDQDMWWLSGIFRDVTLLSKPKQCIEDVFITPDLDACYRDGSLSIVTHISAPETSQVHVQLFDGSQAVTEPSIARPHNRRIDERGSYDDVVFQTLHVREPQQWTAETPNLYRVVVSLLDAEGNHLESEAYQVGFRKVEVKDGQLQLNGKPLLIRGVNRHEHHPELGHVMTEEDMVRDICLMKQYNFNAVRTAHYPNHPRWYELCDQYGLYVCDEANIETHGMIPMNRLSADPQWAHAYMSRYTQMVMRDKNHPSIIIWSLGNESGHGSSHNAMYAWSKQFDPSRPVQYEGGGANTTATDIICPMYARVNTTVEDEAVPKWPIKQWISLPNEQRPLILCEYAHAMGNSLGNFNEYWDAFREFPRLQGGFIWDWVDQGLSQWDNDGKHFWAYGGDFGDTINDRQFCINGLIFPDRTPHPTLEEVKFCQRMITVALTQQDKQQCHLTVTNEYVFRSTDNEQLHWSVLENGVEVQSGQCTLAIDAGSQQTVDIALDFQPKADAKYHLNTDICLISATPWAQAGHVSATEQFTLSNTSSLTLPKISILSAPQLSEQGRDILVSNLDKKHQWQWNVESGLLTSWMVDGQSQLLHAPEDNFFRAPLDNDIGVSEIDNIDPNAWVCRWDAAGIGRWERECVSCTSESLSQAVKVTSTFAYHHNGGVQAITVWTYTLDNQGEMHIDVDVTLADHLPPMPRIGLELALPLPSDNTTVTWQGLGPFENYPDRLAAARFGQHTQSLDAMHTPYIFPTDSGLRSGTQWLNVGNLECTGDFLFSVSRFSQQQLTEAKHTNELTLEDKIYLRIDHQHMGVGGDDSWSPSVHEEFQLTDNTYRFSIMLKPRHN | Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Binds 2 magnesium ions per monomer. Binds 1 sodium ion per monomer. Homotetramer. Belongs to the glycosyl hydrolase 2 family. |
C8VPG3 | MRVDSTVLALVALATDCLGLAIKSNEPELLRRDALPIYKNASYCVDERVRDLLSRMTLEEKAGQLFHKQLSEGPLDDDSSGNSTETMIGKKHMTHFNLASDITNATQTAEFINLIQKRALQTRLGIPITISTDPRHSFTENVGTGFQAGVFSQWPESLGLAALRDPQLVREFAEVAREEYLAVGIRAALHPQVDLSTEPRWARISGTWGENSTLTSELIVEYIKGFQGEGKLGPKSVKTVTKHFPGGGPMENGEDSHFYYGKNQTYPGNNIDEHLIPFKAALAAGATEIMPYYSRPIGTNWEAVGFSFNKEIVTDLLRGELGFDGIVLTDWGLITDTYIGNQYMPARAWGVEYLSELQRAARILDAGCDQFGGEERPELIVQLVREGTISEDRIDVSVARLLKEKFLLGLFDNPFVNASAANNIVGNEHFVNLGRDAQRRSYTLLTNNQTILPLAKPGEGTRFYIEGFDSAFMSARNYTVVNTTEEADFALLRYNAPYEPRNGTFEANFHAGSLAFNATEKARQAKIYSSLPTIVDIILDRPAVIPEVVEQAQAVLASYGSDSEAFLDVVFGVSKPEGKLPFDLPRSMDAVEAQAEDLPFDTENPVFRYGHGLEYEDN | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose. Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Optimum pH is 6.0. Optimum temperature is 52 degrees Celsius. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
V5RMD5 | MDIQSNVLTITSGSTPTDTSSNGQAAKSTKERIKRSDFPSDFVFGAATASYQVEGAWNEGGKGMSNWDYFTQSQPGGISDFSNGTIAIDHYNMFKDDVVVMKKLGLKAYRFSLSWPRILPGGRLCHGVSKEGVQFYNDLIDALLAADIEPYITIFHWDIPQCLQLEYGGFLHERVVKDFIEYSEICFWEFGDRVKYWITLNEPWSFTVQGYVAGAFPPNRGVTPKDTEETQKHARLHRGGGKLLAAFKYGNPGTEPYKVAHNLILCHAHAVDIYRTKYQESQGGKIGITNCISWNEPLTDSQEDKDAATRGNDFMLGWFVEPVVTGEYPESMIKYVGDRLPKFSEKEEKLVKGSYDFLGINYYTSTYTSDDPTKPTTDSYFTDSHTKTSHERNKVPIGAQAGSDWLYIVPWGIYRVMVDMKKRYNDPVIYITENGVDEVNDKSKTSTEALKDDIRIHYHQEHLYYLKLAMDQGVNVKGYFIWSLFDNFEWAAGFSVRFGVMYVDYANGRYTRLPKRSAVWWRNFLTKPTAVPLKNEPEKSEDRRKRLRGST | Major beta-glucosidase activating oleuropein into a potent protein cross-linking agent (PubMed:25697790, PubMed:28483880). No activity with rutin, luteolin or p-nitrophenyl-beta-glucopyranoside as substrates (PubMed:25697790). H2O + oleuropein = D-glucose + oleuropein aglycone Optimum pH is 5.5. Optimum temperature is 37 degrees Celsius. Homomultimer. Native form of the enzyme requires at least an octamer conformation. Distinctive compartmentalization of the oleuropein/OeGLU dual partner is a requisite to ensure a correct defense system response and to prevent the autotoxicity. Expressed in expanding leaves and in young drupes, mostly in the developing seed coat tissues, the perisperm and the mesocarp. Also detected in shoot and root meristems, flower buds, developing ovaries and tapetal cells of the anther. Not detected in embryos or endosperm, or in leaf trichomes. Expressed in the developing mesocarp from 13 weeks after flowering until veraison, when the color of drupes turned from green to black. Belongs to the glycosyl hydrolase 1 family. |
B8NJF4 | MRFVSLAVGAALLGAAGASSISSNVGLLKANGVALGNWEAAYEKASAFVSGLTTDQKLALITGSNVESTNGNFTPLYFLDGDMGLQDFYYVSAFSLSSALAMTWDRDAIYEQAKAVGSEFYNKGVQVVAGPTSQPLGRTPWGGRGVEGFGPDPYLNGLATGLTTKGYVDAGVIPGGKHFLLYEQETNRTSSFGSSGEGSPYSSNADDKTIHETYLWPFYDAVKNGAGAVMCAMTKVNGTMACENSDLLMKMLKTELGFPGMVWPDMNGQNSAKGSALGGEDYGSSSIWSTSTMESFLSNGTLSEARLNDMAIRNLIGYYYVNLDNGRQPTRQTTDVYVDVRANHSKLIRENGAKSMALLKNEGVLPLSKPRVMSIFGAHAGPIMGGPNSNVDVMGSGPTYQGHLATGSGSGMASMPYLITPYGALTNKAAQDGTVLRWVLNDTYSSGGGSSLVPSSTSSTAVEPSFENFATGSDICLVFINALAGEGADRTELYNADQDAMVNTVADNCNNTVAVVNTVGPRLLDQWIEHDNVTAVLYGSLLGQESGNSIVDLLYGDVNPSGRLVHTIAKNESDYNVGLCYTAQCNFTEGVYLDYRYFDAHNITPRYPFGHGLSYTTFHYSSLAIKAPSSITKAPKGNLTVGGPSDLWDVVGTVSARIANNGTLSGAEVPQLYLGFPDSADQPVRQLRGFDRVELSAGQEAVVTFNLRRRDISYWNVKTQQWMVAGGKYTVFVGGSSRDLRLNGTFFLWVGS | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
A2QPK4 | MKVLSFIVAAALLGLTGASSNSSPGLLKSDGVVLGDWESAYQKASSFVAGLTTDQKLALITGSSVNSTNGSFSGLTFLDGDMGLQNFFYVSAFSLSSALAMTWDRDAIYAQAKAVGSEFYNKGIQVVAGPTSQPLGRTPWGGRIVEGFGPDPYLNGLASGLTAKGYIDAGVIPGAKHFLLYEQETNRTGGGGGGGGDSGSAPYSSNADDKTLHETYLWPFYDAVKHGLGAVMCAMTKVNGTLSCQNSDLLMKHLKTELGFPGLVWPDTNGQSSALESAVNGEDYGSSSIWSTSTMETLLSNGSLSEARLDDMAVRNLMGYYYVNLDNGLQPEEQSEDAYVDVRGNHSKLIRENGAKSMALLKNKNALPLRKPRVMSVFGAHAGPVLGGPNTAMDIEGSGPTYQGHLATGTGSAQASLPYLVPPYVALTNRIIEDGTMMRWVLNDTYSSSSTSGLITEGTDSTAVDPSFADYATNSDACLVFLNALSGEGADRTELYNDDQDTMVNTVADNCNNTIVIINTVGPRLMDQWIEHDNVTAVLYGSLLGQESGNSIVDILYGDVNPSGRLIHTIAKNESDYNVKICYTAQCNFTEGVYLDYRYFDAHNVTPRYPFGHGLSYTTFSYSDLNIEKPSTLSKYPTGEKAVGGNSDLWDIVGNVSVKVANTGSLDGAEVPQLYLGFPTAAQQPVRQLRGFERVEIASGKQSQVTFQLRRRDISYWDVPAQQWLVASGDYKVYVGASSRDLKLNGTFTVQTSS | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
Q2UNR0 | MRFVSLAVGAALLGAAGASSISSNVGLLKANGVALGNWEAAYEKASAFVSGLTTDQKLALITGSNVESANGNFTPLYFLDGDMGLQDFYYVSAFSLSSALAMTWDRDAIYEQAKAVGSEFYNKGVQVVAGPTSQPLGRTPWGGRGVEGFGPDPYLNGLATGLTTKGYVDAGVIPGGKHFLLYEQETNRTSSFGSSGEGSPYSSNADDKTIHETYLWPFYDAVKNGAGAVMCAMTKVNGTMACENSDLLMKMLKTELGFPGMVWPDMNGQNSAKGSALGGEDYGSSSIWSTSTMESFLSNGTLSEARLNDMAIRNLIGYYYVNLDNGRQPTRQTTDVYVDVRANHSKLIRENGAKSMALLKNEGVLPLSKPHVMSIFGAHAGPIMGGPNSNVDVMGSGPTYQGHLATGSGSGMASMPYLITPYDALTNKAAQDGTVLRWVLNDTYSSGGGSSLVPSSTSSTAVEPSFENFATGSDICLVFINALAGEGADRTELYNADQDAMVNTVADNCNNTVAVVNTVGPRLLDQWIEHDNVTAVLYGSLLGQESGNSIVDLLYGDVNPSGRLVHTIAKNESDYNVGLCYTAQCNFTEGVYLDYRYFDAHNITPRYPFGHGLSYTTFHYSSLAIKAPSSITKAPKGNLTVGGPSDLWDVVGTVSARIANNGTLSGAEVPQLYLGFPDSADQPVRQLRGFDRVELSAGQEAVVTFNLRRRDISYWNLKTQQWMVAGGKYTVFVGGSSRDLRLNGTFFLWVGS | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
C8V4V5 | MRVPSLSVLSFLLGTALAAASNFEAGLLSSGKVSLGDWKSAHEKASQFVAKLNTTEKIKLITGSSVTTTNGETFTALDILDGDMGAQAYYYVSAFSLSSALAMTWDKEAMYEQGRAIAAEFYGKGIQMVAGPTSQPLGRTPWGGRLVESFGPDPYLNGIATGLETRAYADVGVIAGAKHFILNEQETNRTGGMGGGGGAPGGGGMGRGAEFSSSVPGGMSPTSSAGAIPSSTSTPGGSGMGGGMAGSSAFSSSSSSGAPYSSNADDKTLHETYLWSFYDAVHSGLGGVMCAMTKVNGTLSCQSSSLLLDILKTELGFPGMVWPDTNGQQDALASAANGLDYGSSSLWSESTIEGYLESNNITEARLNDMAIRNLMGYYYVNLDNGTQPSTAAQDDYVDVRANHAKLIRSHGSKSMVLLKNKNNTLPLYKPHKMAIFGSHARAAVAGPNMQFSVEGSGPTYDGHIATDSGSGQASLPYLITPENALNIKASQDGTMLRWIANDTYSSSTGSALVMQGSSSTSVTPSVSAYSENMDVCLVFINALAGEGADRTELRNTDQDNLINEVADNCDNTVVVINTVGARILDSWIEHENVTAVLYGSLLGQESGNSIVDVLYGDVNPSGRLTYTIAKTESDYNVDICYTAQCNFTEGNYIDYRYFDAYNVTPRYEFGYGLSYTDFAYSNLHIQGPSALSTYPTGQLAVGGYEDLWDTVAKVTVTIRNAGSLDGAEVPQLYISYPDVAKQPVRQLRGFHNVYIKKGQSTKVTFELRRRDISYWDVQHQKWAVAPGTYEAWVGASSRDLRTHGSFVVKTKA | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
A1CMH6 | MPPPDSNPGSFRDHLKHDNKNNNSSTTSKGKQRYTPLHDSIPEEIASPRSASASSSFDLDPDLENQSRNDYKLRPLARSSSTNGGHNYSTAYIPVIRDEGDDVETYLDSITEAEQELLSLSKQYDFADDSDDFDSDDDAALRRKVQKQEQRRRRERLKAKVWTPVKYARIWRRTLVVVIVALALLVWGFLRFTAAQRQGPKVWPMLPSDSWFPSPKGGTLKHWEESYRKAQSLVRNMTLIEKVNITTGTGWQMGMCVGNTGPAELVKFPSLCLQDGPQGLRYADHVTAFPAGITTGSTWNRTLMRERGIAMGREARLKGVNVLLGPSIGPIGMMPAGGRNWEGFGSDPVLQGVAAAETIRGIQSNGVMATAKHFLMNEQEHFRQPFEWGISTALSSNVGDRALHEVFAWPFAESIRADVASVMCSYQMVNNSHACENSKLLNGILKDELGFQGFVQSDWLAQRSGINSALGGLDMSMPGDGLHWTDGKSLWGRELTRAVLNTSIPMERLNDMVTRIVAAWYQFEQDEWERPPPEGNGGPNFSSWTGGDVGWLHAGSNDGLYAVVNQYIDAQGTGPEAHSIIARKVAAEGTVLLKNVDHTLPLSRNASGPSGVMRVGIYGDDAGPAQGPNACPDRGCNQGTLATGWGSGTVDFPYLVSPLEALETAWKTEVEMTAFLRNAVMPADVADKDLCLVFANADSGEGFISAGGIHGDRNDLFLQKGGDTLIRTVASHCGEGQGKTVVVIHAVGPVVMESWIDLPGVHAVLLANLPGQESGNALMDVLFGDVDASGRLPYTIGKSLEEYGTEAQVLYEPNAPVPQVDLLDALFIDYRHFDQYNITPRFEFGFGLSYTTFKLKDLHVRSLQSKSRSPAARPAAAVSPPEYNTTLPDPALALFPPGFQPVYKYIYPYLPSLDGTAPANYSYYPKDYNQTQGPSPAGGGAGGNPALFQEMASVSVQVQNTGDRKGQEVVQVYVSFPSDEKVKIDFPERVLRNFTKVELEPGERREVQMTLSRKDLSYWSVREQNWVMPDGDFQIWVGRSSRDLPLQAKY | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
B0YD91 | MAPPDSTHGGSFRDHLKTNDRSSTSKGKQRYSPLQEAIPEEISSFRSPSEYADTDSDSDLERSGSYKLRPVDRYGSHHSSAFIPVIREENGVETYLDSITEAEQELLSASKQYDLVDDDDSSDFDSDEEATLRYRLKDRLKRRRARLQAWQPVKYARIWWRTLLAVVVTLVVVVWGFLSFAVSHREEPTVWPMVPSDSWFPSPKGGTLKHWEESYKKAQSLVRNMTLVEKVNITTGIGWQMGLCVGNTGPADIVKFPSLCLQDGPQGLRFADHVSAFPAGITTGSTWNRELMRERGVAMGREARLKGVNVLLGPSMGPLGMMPAGGRNWEGFGSDPVLQAVAAAETIRGIQSNGVMATAKHFVMNEQEHFRQPFEWGIPTALSSNVGDRALHEVFAWPFAESIRADVASVMCSYQMVNNSHACENSKLLNGILKDELGFQGFVQSDWLAQRSGINSALGGLDMSMPGDGLHWVDGKSLWGSELTRAVLNTSVPVERLNDMVTRIVAAWYHLGQDTWERPPPEGNGGPNFSSWTNDEVGWLHTGSNDGSYARVNHYVDAQGTGPEAHSIIARKVAAEGTVLLKNVDRTLPLSRNASSPSGGILRVGIYGDDAGPALGPNACPDRGCNQGTLATGWGSGTVEFPYLVSPIEALESAWSTEIESTAYLRNAVMPADAVDKDLCLVFVNADSGEGYISAGGIHGDRNDLFLQKGGDTLVRTVSSNCGGGQGKTVVVIHAVGPVVMESWIDLPGVHAVLLANLPGQESGNALVDVLFGEVDASGRLPYTIGKSLEDYGPGAQVLYEPNAPVPQVDFLDALYIDYRHFDRHNITPRFEFGFGLSYTTFELLDLSISPLQQKSRSVPPRPADAVAPPVYDISLPDPASALFPAGFQPVFKYIYPYLSNLDGTAPHNYSFYPKGYNETQRPSPAGGGAGGHPALYEEMVSVKLQVSNTGDRKGQEVVQVYVSFPPDFPERVLRNFTKIELEPSERREVQMTLSRKDLSYWSTREQNWVMPEGKFQIWVGRSSRDLPLMGEY | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
Q4WD56 | MAPPDSTHGGSFRDHLKTNDRSSTSKGKQRYSPLQEAIPEEISSFRSPSEYADTDSDSDLERSGSYKLRPVDRYGSHHSSAFIPVIREENGVETYLDSITEAEQELLSASKQYDLVDDDDSSDFDSDEEATLRYRLKDRLKRRRARLQAWQPVKYARIWWRTLLAVVVTLVVVVWGFLSFAVSHREEPTVWPMVPSDSWFPSPKGGTLKHWEESYKKAQSLVRNMTLVEKVNITTGIGWQMGLCVGNTGPADIVKFPSLCLQDGPQGLRFADHVSAFPAGITTGSTWNRELMRERGVAMGREARLKGVNVLLGPSMGPLGMMPAGGRNWEGFGSDPVLQAVAAAETIRGIQSNGVMATAKHFVMNEQEHFRQPFEWGIPTALSSNVGDRALHEVFAWPFAESIRADVASVMCSYQMVNNSHACENSKLLNGILKDELGFQGFVQSDWLAQRSGINSALGGLDMSMPGDGLHWVDGKSLWGSELTRAVLNTSVPVERLNDMVTRIVAAWYHLGQDTWERPPPEGNGGPNFSSWTNDEVGWLHTGSNDGSYARVNHYVDAQGTGPEAHSIIARKVAAEGTVLLKNVDRTLPLSRNASSPSGGILRVGIYGDDAGPALGPNACPDRGCNQGTLATGWGSGTVEFPYLVSPIEALESAWSTEIESTAYLRNAVMPADAVDKDLCLVFVNADSGEGYISAGGIHGDRNDLFLQKGGDTLVRTVSSNCGGGQGKTVVVIHAVGPVVMESWIDLPGVHAVLLANLPGQESGNALVDVLFGEVDASGRLPYTIGKSLEDYGPGAQVLYEPNAPVPQVDFLDALYIDYRHFDRHNITPRFEFGFGLSYTTFELLDLSISPLQQKSRSVPPRPADAVAPPVYDISLPDPASALFPAGFQPVFKYIYPYLSNLDGTAPHNYSFYPKGYNETQRPSPAGGGAGGHPALYEEMVSVKLQVSNTGDRKGQEVVQVYVSFPPDFPERVLRNFTKIELEPSERREVQMTLSRKDLSYWSTREQNWVMPEGKFQIWVGRSSRDLPLMGEY | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
Q2UTX5 | MPPPPFRDAPSSAKSSQRYTPLHESIPEELNDKQYSSDADSLPLSDPSDGEDDSEIRLRRVDRNGTRSNQATAYVPVVRKSGDVEAYFDSIAEAELELLSASRQYDGVDDDDDDSDGYGVGVKRGQRQGLLKRTHDGRTGWRTVYYSKYWWRALIGVVVVLVLLVLVFLGLARSKQVGDELDYSMIPAESWFPSPRGGALKEWAADYQKAALLVGNMTLIEKVNITTGTGWQMGLCVGNTGPAESVHFPSLCLQDGPMGIRYADHISAFPPGLTTGATWNRDLIRERGIAMGLEARLKGVNVLLGPSMGPLGMMPAGGRNWEAFGSDPVLQGVAAAETIKGIQSNGVMATAKHFVMNEQEHFRQPFEWGIPTALSSNVGDRALHEVFAWPFAESIRADVASVMCAYQMVNNSHACENSKLLNGILKDELGFQGFVQSDWLAQRSGINSALGGLDMSMPGDGLHWADGKSLWGSELTRAVLNTSIPMERLNDMVTRIVAAWYHLGQDQWERPPPDGEGGPNFSSWTDDQTGWWQQASVEAGDQDGGWGIVNKYVDAGAGHGDIARKVAAEGIVLVKNNNNTLPLSRSPPSPYRIGIYGDDAGPALGPNACPDRGCSQGTLASGWGSGTVEFPFLVSPLEALQGAWETEVEITPYLQNMVMPVSVQDKDLCLVFANANSGEGYIHAGGIHGDRNDLFLQKGGDTLIQAVANNCAGPTVVVVHAVGPVVVESWIDLPGVDAVLFAHLPGQESGNALVDVLFGDVDASGRLPYTVGKSLEDYGPGAQVLYENNAPVPQVDFLDALYIDYRYFDKFNITPRYEFGFGLSYTSFELSKLYIKSMQWKSRLPKSRPQDQVSPPEYDTRPPVNENVLFPEGFHALSKYVYSYLPSLDGTAAANYTEYPDGYDLPRQPSEAGGDLGGNPSLYEEMAKVQVQVANTGARAGQTVVQAYVSFPSDVVEEGDLVEVPVDEKGETVTFVPSKEQVEFPDRVLRNFTKIALEPGEKKTVEMTLSRKDLSYWSARQQNWVMPDGDFQIWVGQSSRDLPLHGKY | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
C8V1D9 | MPKSYTPVHDSIPEEDHFSSDDESNFRLHRIDRSASRSQSPKENEGEPSILAPLVRKSTDFETYLDSLTEDEQQLLSASKDHDIEDLDRFGDGTAAARRRFSESKKRRKLLAKRGGWRAVYYSKTWWRTLVVVIIALGLLVWGFLKYASTRGDIWEEYDMPGPDSYFPTPKGGTLKHWAESYEKASKLVERMTLIEKVNITTGTGWQMGINSKLTISGPAALVGFPSLCLQDGPLGIRFADHITAFPAGITTGATWNRDLMRQRGAAIGLEARLKGVNVILGPSMGPLGMMPAGGRNWEGFGSDPVLQAVAAVETIHGIQSNGVMATAKHYIMNEQEHFRQPNEWGIPYALSSNIDDRALHEVFLWPFAESIRADVASVMCSYNQVNNSHACENSKLLNGILKDELGFQGFVQSDWLAQRSGVNSALGGLDMSMPGDGLHWADGRSLWGSELTRAALNTSVPMERLNDMVTRIVAAWYQLGQDSWESPAPDGDGGPNFSSWTDDEFGFRYPGSPGDTSAARVNRFIDAQGRGEEGHWNIARKVAAEGIVLVKNVGGVLPLSRSPRANAERPYRVGVYGDDGGPAAGPNICTDRGCNSGTLAMGWGSGTVEFPYLISPIDALQGAWQSDVQMTPYLRNAVMPADTSDKDLCLVFVNADSGEGYISAGGIHGDRNNLFLQKGGDTLVHTVATNCGGPTVVVVHAVGPVIVEPWIDLPGVQAVLFAHLPGEESGNALLDVLFGDVDASGRLPYTVGKSLEDYGPGAQVLYEPNAPVPQVDFSDALYIDHRYFDRNNINPRYEFGFGLSYTKWELTNMKITRLQRNPSRLPAARPPDAVAPPSYDANPPLANESVLFPPGFRILSKYIYPYLPTLEATTPPPPNPEASGSATDQKPHRTKPSDAGGGAGGNPSLYEEVARIDLTVQNTGTRSGQQVIQLYVSFPHTVTESSGQKSHENIDFPDRVLRNFTKISLAPGQKMDVNMTLTRKDLSYWSVREQNWVLPKDEFYFWVGYSSRNLPLGKPFDP | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
A1DLJ5 | MAPPDSTHGGSFRDHLKTNDRSSTSKGKQRYAPLHEAIPEEISSFRSPSEYADADTDSDSDHENSGSYQLRPVDRYGSHHSSAFIPVIRDDGGVETYLDSITEAEQELLSASKQYDLFDDDDSDDLDSDEEATLRYKLKDRLKRRRARLQAWPPVKYARIWWRTLLAVIVTLAVVVWGFLSFAVSHREEPKVWPMVPSDSWFPSPKGGTLKHWEESYKKAQSLVRNMTLVEKVNITTGIGWQMGLCVGNTGLRFADHVSAFPAGITTGSTWNRELMRERGVAMGREARLKGVNVLLGPSMGPLGMMPAGGRNWEGFGSDPVLQAVAAAETIRGIQSNGVMATAKHFVMNEQEHFRQPFEWGIPTALSSNVGDRALHEVFAWPFAESIRADVASVMCSYQMVNNSHACENSKLLNGILKDELGFQGFVQSDWLAQRSGINSVLGGLDMSMPGDGLHWVDGKSLWGSELTRAVLNTSVPVERLNDMVTRIVAAWYHLGQDTWERPPPEGNGGPNFSSWTNDKVGWLHTGSNDGSYAVVNHYVDAQGTGPEAHSIIARKVAAEGTVLLKNVDRTLPLSRNASSPSGGILRVGIYGDDAGPASGPNACPDRGCNQGTLATGWGSGTVEFPYLVSPIEALESAWSTEIESTAYLRNAVMPADAVDKDLCLVFVNADSGEGYISAGGIHGDRNDLFLQKGGDTLVRTVASNCGGGQGKTVIVIHAVGPVVMESWIDLPGVHAVLLSNLPGQESGNALMDVLFGEVDASGRLPYTIGKSLEDYGPGAQVLYEPNAPVPQADFLDALYIDYRHFDRYNITPRFEFGFGLSYTTFELSDLSISPLQRKSRSPPPRPADAVAPPVYDTSLPDPASALFPTGFQPIFKYIYPYLSNLDGTAPRNYSFYPKGYNETQSPSPAGGGAGGHPALYEEMVSVKLQVSNTGDRKGQEVVQLYVSFPPDVTEEGDWVEVDSDADKTGEKQRERMKIEFPERVLRNFTKIELEPSERREVQMTLSRKDLSYWSTREQNWVMPEGKFQIWVGRSSRDLPLMGEY | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
O08487 | MTMIFPKGFMFGTATAAYQIEGAVAEGGRTPSIWDTFSHTGHTLNGDTGDVADDFYHRWEDDLKLLRDLGVNAYRFSIGIPRVIPTPDGKPNQEGLDFYSRIVDRLLEYGIAPIVTLYHWDLPQYMASGDGREGGWLERETAYRIADYAGIVAKCLGDRVHTYTTLNEPWCSAHLSYGGTEHAPGLGAGPLAFRAAHHLNLAHGLMCEAVRAEAGAKPGLSVTLNLQICRGDADAVHRVDLIGNRVFLDPMLRGRYPDELFSITKGICDWGFVCDGDLDLIHQPIDVLGLNYYSTNLVKMSDRPQFPQSTEASTAPGASDVDWLPTAGPHTEMGWNIDPDALYETLVRLNDNYPGMPLVVTENGMACPDKVEVGTDGVKMVHDNDRIDYLRRHLEAVYRAIEEGTDVRGYFAWSLMDNFEWAFGYSKRFGLTYVDYESQERVKKDSFDWYRRFIADHSAR | Bifunctional beta-D-glucosidase/beta-D-fucosidase. Activity towards pNP-beta-D-fucoside is about 80-85% of the activity towards pNP-beta-D-glucoside. Also has slight activity (less than 10%) towards pNP-beta-D-galactoside, and very low activity (less than 1%) towards pNP-beta-D-xyloside. Hydrolyzes laminaribiose, sophorose, cellobiose and gentobiose. Not active against maltose, pNP-alpha-D-glucoside or pNP-beta-L-fucoside. Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Hydrolysis of terminal non-reducing beta-D-fucose residues in beta-D-fucosides. Inhibited by Cu(2+), Ag(+) and Hg(+), but not by other cations such as Mg(2+), Ca(2+), Mn(2+) and Co(2+). Inhibited by 1-amino-1-deoxy-D-glucose and p-chloromercuribenzoic acid, but not by EDTA or dithiothreitol. Inhibited by the disaccharides sucrose, lactose and cellobiose. The monosaccharides D-fructose, D-mannose, D-xylose and D-glucose increase the beta-D-fucosidase activity, but not the beta-D-glucosidase activity. D-glucose inhibits the beta-D-glucosidase activity, but promotes the beta-D-fucosidase activity. D-fucose inhibits the beta-D-glucosidase activity and does not significantly affect the beta-D-fucosidase activity. Optimum pH is 5.5 with pNP-beta-D-glucoside as a substrate. Retains more than 90% of its activity between pH 5.0 and 7.0. Retains 70% of its activity at pH 4.5 and 8.5. Optimum temperature is 45 degrees Celsius with pNP-beta-D-glucoside as a substrate. Retains 60% of its activity after 10 minutes incubation at 50 degrees Celsius. Monomer. Belongs to the glycosyl hydrolase 1 family. |
B0Y7Q8 | MRVLSAIALVASLASSALSAPASESRVSTQLRSRDAEGYSSPPYYPAPNGGWLSSWADAYEKAQRVVRDMTLAEKVNLTTGTGIFMGPCVGQTGSALRFGIPNLCLQDSPLGVRNSDHNTAFPAGITVGATFDKDLMYARGVELGKEFRGKGINVLLGPSVGPIGRKPRGGRNWEGFGADPSLQAIGGAQTIKGIQSQGVIATIKHYIGNEQEMYRMSNVGQRAYSSNIDDRTLHEVYLWPFAEGIRAGVGAVMTAYNEVNSSACSQNSKLLNEILKDELGFQGFVMTDWLGQYGGVSSALAGLDMAMPGDGAIPLLGTAYWGSELSRSILNGSVPVSRLNDMVTRIVAAWYKMGQDGDFPLPNFSSNTQDATGPLYPGALFSPSGVVNQYVNVQADHNITARAIARDAITLLKNDDNILPLKKDDALKVFGTDAGPNPDGLNSCADMGCNKGVLTMGWGSGTSRLPYLVTPQEAIANISSNAAFFITDKFPSNVAVSSGDVAVVFISADSGENYITVEGNPGDRTSAGLNAWHNGDKLVKDAAAKFSKVVVVVHTVGPILMEEWIDLPSVKAVLVAHLPGQEAGWSLTDVLFGDYSPSGHLPYTIPRAESDYPSSVGLLSQPIVQIQDTYTEGLYIDYRHFLKANITPRYPFGHGLSYTTFSFSQPTLSVRTALDSTYPPTRPPKGPTPTYPTAIPDPSEVAWPKNFDRIWRYLYPYLDDPASAAKNSSKTYPYPAGYTTVPKPAPRAGGAEGGNPALFDVAFAVSVTVTNTGSRPGRAVAQLYVELPDSLGETPSRQLRQFAKTKTLAPGTSETLTMEITRKDISVWDVVVQDWKAPVRGEGVKIWLGESVLDMRAVCEVGGACRVI | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
B8NP65 | MAAFPAYLALLSYLVPGALSHPEAKTLTSRASTEAYSPPYYPAPNGGWISEWASAYEKAHRVVSNMTLAEKVNLTSGTGIYMGPCAGQTGSVPRFGIPNLCLHDSPLGVRNSDHNTAFPAGITVGATFDKDLMYERGVGLGEEARGKGINVLLGPSVGPIGRKPRGGRNWEGFGADPSLQAFGGSLTIKGMQSTGAIASLKHLIGNEQEQHRMSSVITQGYSSNIDDRTLHELYLWPFAESVRAGAGSVMIAYNDVNRSACSQNSKLINGILKDELGFQGFVVTDWLAHIGGVSSALAGLDMSMPGDGAIPLLGTSYWSWELSRSVLNGSVPVERLNDMVTRIVATWYKMGQDKDYPLPNFSSNTEDETGPLYPGALFSPSGIVNQYVNVQGNHNVTARAIARDAITLLKNNDNVLPLKRNNTLKIFGTDAGTNSDGINSCTDKGCNKGVLTMGWGSGTSRLPYLITPQEAIANISSNAGFHITDTFPSGVTAGPDDIAIVFINSDSGENYITVDGNPGDRTLAGLHAWHNGDNLVKAAAEKFSNVVVVVHTVGPILMEEWIDLDSVKAVLVAHLPGQEAGWSLTDILFGDYSPSGHLPYTIPHSESDYPESVGLIAQPFGQIQDDYTEGLYIDYRHFLKANITPRYPFGHGLSYTTFNFTEPNLSIIKALDTAYPAARPPKGSTPTYPTAKPDASEVAWPKNFNRIWRYLYPYLDNPEGAAANSSKTYPYPDGYTTEPKPAPRAGGAEGGNPALWDVTFSVQVKVTNTGSRDGRAVAQLYVELPSSLGLDTPSRQLRQFEKTKILAAGESEVLTLDVTRKDLSVWDVVVQDWKAPVNGEGVKIWVGESVADLRVGCVVGEGCSTL | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
Q4WMU3 | MRVLSAIALVASLASSALSAPASESRVSTQLRSRDAEGYSSPPYYPAPNGGWLSSWADAYEKAQRVVRDMTLAEKVNLTTGTGIFMGPCVGQTGSALRFGIPNLCLQDSPLGVRNSDHNTAFPAGITVGATFDKDLMYARGVELGKEFRGKGINVLLGPSVGPIGRKPRGGRNWEGFGADPSLQAIGGAQTIKGIQSQGVIATIKHYIGNEQEMYRMSNVGQRAYSSNIDDRTLHEVYLWPFAEGIRAGVGAVMTAYNEVNSSACSQNSKLLNEILKDELGFQGFVMTDWLGQYGGVSSALAGLDMAMPGDGAIPLLGTAYWGSELSRSILNGSVPVSRLNDMVTRIVAAWYKMGQDGEFPLPNFSSNTQDATGPLYPGALFSPSGVVNQYVNVQADHNITARAIARDAITLLKNDDNILPLKKDDALKVFGTDAGPNPDGLNSCADMGCNKGVLTMGWGSGTSRLPYLVTPQEAIANISSNAAFFITDNFPSNVAVSSGDVAVVFISADSGENYITVEGNPGDRTSAGLNAWHNGDKLVKDAAAKFSKVVVVVHTVGPILMEEWIDLPSVKAVLVAHLPGQEAGWSLTDVLFGDYSPSGHLPYTIPRAESDYPSSVGLLSQPIVQIQDTYTEGLYIDYRLFLKANITPRYPFGHGLSYTTFSFSQPTLSVRTALDSTYPPTRPPKGPTPTYPTAIPDPSEVAWPKNFGRIWRYLYPYLDDPASAAKNSSKTYPYPAGYTTVPKPAPRAGGAEGGNPALFDVAFAVSVTVTNTGSRPGRAVAQLYVELPDSLGETPSRQLRQFAKTKTLAPGTSETLTMEITRKDISVWDVVVQDWKAPVRGEGVKIWLGESVLDMRAVCEVGGACRVI | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
Q2UN12 | MAAFPAYLALLSYLVPGALSHPEAKTLTSRASTEAYSPPYYPAPNGGWISEWASAYEKAHRVVSNMTLAEKVNLTSGTGIYMGPCAGQTGSVPRFGIPNLCLHDSPLGVRNSDHNTAFPAGITVGATFDKDLMYERGVGLGEEARGKGINVLLGPSVGPIGRKPRGGRNWEGFGADPSLQAFGGSLTIKGMQSTGAIASLKHLIGNEQEQHRMSSVITQGYSSNIDDRTLHELYLWPFAESVRAGAGSVMIAYNDVNRSACSQNSKLINGILKDELGFQGFVVTDWLAHIGGVSSALAGLDMSMPGDGAIPLLGTSYWSWELSRSVLNGSVPVERLNDMVTRIVATWYKMGQDKDYPLPNFSSNTEDETGPLYPGALFSPSGIVNQYVNVQGNHNVTARAIARDAITLLKNNENVLPLKRNDTLKIFGTDAGTNSDGINSCTDKGCNKGVLTMGWGSGTSRLPYLITPQEAIANISSNAEFHITDTFPLGVTAGPDDIAIVFINSDSGENYITVDGNPGDRTLAGLHAWHNGDNLVKAAAEKFSNVVVVVHTVGPILMEEWIDLDSVKAVLVAHLPGQEAGWSLTDILFGDYSPSGHLPYTIPHSESDYPESVGLIAQPFGQIQDDYTEGLYIDYRHFLKANITPRYPFGHGLSYTTFNFTEPNLSIIKALDTAYPAARPPKGSTPTYPTAKPDASEVAWPKNFNRIWRYLYPYLDNPEGAAANSSKTYPYPDGYTTEPKPAPRAGGAEGGNPALWDVTFSVQVKVTNTGSRDGRAVAQLYVELPSSLGLDTPSRQLRQFEKTKILAAGESEVLTLDVTRKDLSVWDVVVQDWKAPVNGEGVKIWVGESVADLRVGCVVGEGCSTL | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
Q0CI67 | MAPSSLKWTLLCALPWTLASPASYNVHHARDSDAQAFSPPYYPTPHGGWIADWAEAYEKASQLVRNMTLAEKVNLTTGTGMYMGPCAGQTGSVPRFGIPNLCMHDGPLGVRNTDHNTAFPPGITVGATFDKDLMRSRGVALGEEGRGKGVNVLLGPSVGPIGRKPRGGRNWEGFGADPSLQAIAGSLTIEGMQSTGLIACIKHFIANEQEMHRMSSVVTQGYSSNVDDRTLHELYLWPFAEGVRAGVGSLMAAYNDVNNSASSQNSKMLNDILKDELGFQGFVMSDWFGNYGGVSAALAGLDVSMPGDGAIPLLGDSYWGSELSRSILNGTVPVDRLNDMATRILASWYKMGQDQDYPLPNFSANTEDAEGPLYPGAVFSPKGVVNKFVNVQGDHNVTARAIARDAITLLKNNNNILPLHRNDSLKIFGTDAGTNPDGINSCSDKGCNKGVLTMGWGSGSSKLPYLVTPQEAIANISSHAEFHITDSFPSDVSAGPNDIAIVFINSDSGENYITVEGNPGDRTSAGLNAWHNGDDLVKAAAEKFRQVVVVYHTVGPVLMEEWIDLEPVKAVLVAHLPGQEAGWSLTDVLFGDYSPSGHLPYTIPRSESDYPDSVSLIQQPFGRIQDDYTEGLYIDYRHFAKAGITPRFPFGYGLSYTNFNFSRASISAQSSLDTAYPAPRSPKGSTPEYSTAIPPAAEAAWPKNFNRIWRYLYPYLDNPEGARANSSRKYPYPDGYSTVQKPGPRAGGGEGGNPALFDVAFSVQVQVTNTGARKGRAVAQLYVELPDSLGVDTPSRQLRQFEKTKILAPGESQVLTMEITRKDLSVWDVVAQDWKAPVNGEGVKMWIGESVADMRVLCTVGEGCSTL | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
C8V6A2 | MAHRWLILALVAAAAPRALASPGPSLNERQSDDEPFSPPYYPAPNGGWVSTWAEAYEKAHSIVSNLTLAEKVNLTTGTGIFMGPCAGQTGSVPRLGIPNLCLHDSPLGVRNTDHNTAFPPGITVGATFDKSLMYERGVGLGEEARGKGVNVLLGPSVGPLGRKPRGGRNWEGFGFDPVLQGIGGAETIKGMQSTGLIACIKHFVGNEQEMHRMSSVVTQGYSSNIDDRTLHELYIWPFAEGVRAEVGSVMIAYNDVNKSSCSQNSKLINGVLKDELGFQGFVVTDWLAHYGGVSSALAGLDMDMPGDGAVPLFGNSYWGPELSRSILNGTVPVERLNDMVTRILATWYKMGQDQDYPLPNFSSNTEDEKGLLYPGAVISPIGVVNQYVNVQGNHNITARAIARDAITLLKNEGDLLPLRRNDSLKVFGTDAGPDPQGLNSCADKGCNRGVLTMGWGSGTSKLPYLITPQEAIANITPTAEFFITDSFPSSVDANDEDIAIVFINSDSGENYITVDGNPGDRKTSGLHAWHNGDELVKAAAERFSQVVVVIHTVGPIILEEWIDLDSVKAVLIAHLPGQEAGYSLTDVLFGDYSPSGHLPYTIPYQESNYPSSVGLLQQPFGQIQDYYTEGLYIDYRHFLKEDITPRYAFGHGLSYTTFEFSEPALSVVTPLDSAYPPSRPAKGPTPTYPNTIPPASEAAWPAKFNRIWRYIYPYLNNPQADAAVANSSKTYPYPDGYSTDPQPPPRAGGAEGGNPALWDVAFSVQVTVTNTGQHSGRAVAQLYVELPDSLGLDTPSRQLRQFEKTKVLETGQSETLTLEVTRKDVSVWDVEVQDWKTVVGGEGVKIHIGESVLDIRTECEVGGRCVTL | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
A1DMR8 | MRVLSAIALVASLVPSALSAPASESRVSTQLQSRDAAGYSSPPYYPAPNGGWLSSWADAYEKAQRVVRNMTLAEKVNLTTGTGIFMGPCVGQTGSALRFGIPNLCLQDSPLGVRNSDHNTAFPAGITVGATFDKDLMYARGVELGEEFRGKGINVFLGPSVGPIGRKPRGGRNWEGFGADPSLQAIGGAQTIKGIQSRGVIATIKHYIGNEQEMYRMSNIGQRAYSSNIDDRTLHELYLWPFAEGIRAGVGAVMTAYNEVNSSACSQNSKLLNEILKDELGFQGFVMTDWLGQYGGVSSALAGLDMAMPGDGAIPLLGNAYWGSELSHSILNGSVPVSRLNDMVTRIVATWYKMGQDGDFPLPNFSSNTQDATGPLYPGALFSPSGVVNQYVNVQADHNITARAIARDAITLLKNDDNILPLKRNDSLKVFGTDAGPNPDGLNSCADMGCNKGVLTMGWGSGTSRLPYLVTPQEAIANISSNAAFFITDNFPSNVAVSSGDVAVVFISADSGENYITVEGNPGDRTSAGLNAWHNGDKLVKDAAAKFSKVVVVVHTVGPILMEEWIDLPSVKAVLVAHLPGQEAGWSLTDVLFGDYSPSGHLPYTIPRAESDYPSSVGLLSQPIVQIQDTHTEGLYIDYRHFLKSSITPRYPFGHGLSYTTFSFSQPTLSVRTALDSAYPPTRPPKGPTPTYPTTIPNPSEVAWPKNFDRIWRYLYPYLDDPAGAAKNSSKTYPYPAGYTTVPKPAPRAGGAEGGNPALFDVAFAVSVTVTNTGTRPGRAVAQLYVELPDSLGETPSRQLRQFAKTKTLAPGASETLTMEFTRKDISVWDVVVQDWKAPVRGEGVKIWLGESVLDMRAVCEVGGACRVI | Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Glycan metabolism; cellulose degradation. Belongs to the glycosyl hydrolase 3 family. |
Q8S3F5 | MNIGRLVWNEDDKAIVASLLGKRALDYLLSNSVSNANLLMTLGSDENLQNKLSDLVERPNASNFSWNYAIFWQISRSKAGDLVLCWGDGYCREPKEGEKSEIVRILSMGREEETHQTMRKRVLQKLHDLFGGSEEENCALGLDRVTDTEMFLLSSMYFSFPRGEGGPGKCFASAKPVWLSDVVNSGSDYCVRSFLAKSAGIQTVVLVPTDLGVVELGSTSCLPESEDSILSIRSLFTSSLPPVRAVALPVTVAEKIDDNRTKIFGKDLHNSGFLQHHQHHQQQQQQPPQQQQHRQFREKLTVRKMDDRAPKRLDAYPNNGNRFMFSNPGTNNNTLLSPTWVQPENYTRPINVKEVPSTDEFKFLPLQQSSQRLLPPAQMQIDFSAASSRASENNSDGEGGGEWADAVGADESGNNRPRKRGRRPANGRAEALNHVEAERQRREKLNQRFYALRSVVPNISKMDKASLLGDAVSYINELHAKLKVMEAERERLGYSSNPPISLDSDINVQTSGEDVTVRINCPLESHPASRIFHAFEESKVEVINSNLEVSQDTVLHTFVVKSEELTKEKLISALSREQTNSVQSRTSSGR | Homodimer. By UV treatment. |
O23090 | MYNLTFSPSLSSSLLSFTQQTPAAIVSSSPPDLVLQQKLRFVVETSPDRWAYVIFWQKMFDDQSDRSYLVWVDGHFCGNKNNNSQENYTTNSIECELMMDGGDDLELFYAASFYGEDRSPRKEVSDESLVWLTGPDELRFSNYERAKEAGFHGVHTLVSIPINNGIIELGSSESIIQNRNFINRVKSIFGSGKTTKHTNQTGSYPKPAVSDHSKSGNQQFGSERKRRRKLETTRVAAATKEKHHPAVLSHVEAEKQRREKLNHRFYALRAIVPKVSRMDKASLLSDAVSYIESLKSKIDDLETEIKKMKMTETDKLDNSSSNTSPSSVEYQVNQKPSKSNRGSDLEVQVKIVGEEAIIRVQTENVNHPTSALMSALMEMDCRVQHANASRLSQVMVQDVVVLVPEGLRSEDRLRTTLVRTLSL | Homodimer. |
Q8S3F3 | MNSLVGDVPQSLSSLDDTTTCYNLDASCNKSLVEERPSKILKTTHISPNLHPFSSSNPPPPKHQPSSRILSFEKTGLHVMNHNSPNLIFSPKDEEIGLPEHKKAELIIRGTKRAQSLTRSQSNAQDHILAERKRREKLTQRFVALSALIPGLKKMDKASVLGDAIKHIKYLQESVKEYEEQKKEKTMESVVLVKKSSLVLDENHQPSSSSSSDGNRNSSSSNLPEIEVRVSGKDVLIKILCEKQKGNVIKIMGEIEKLGLSITNSNVLPFGPTFDISIIAQKNNNFDMKIEDVVKNLSFGLSKLT | Homodimer. Expressed in roots. By cold treatment. Extended C-terminus. |
Q8S3F2 | MDEDFFLPDFSLVDIDFDFNIYEENNLSPDESLSNSRRADQSSKFDHQMHFECLREKPKAAVKPMMKINNKQQLISFDFSSNVISSPAAEEIIMDKLVGRGTKRKTCSHGTRSPVLAKEHVLAERKRREKLSEKFIALSALLPGLKKADKVTILDDAISRMKQLQEQLRTLKEEKEATRQMESMILVKKSKVFFDEEPNLSCSPSVHIEFDQALPEIEAKISQNDILIRILCEKSKGCMINILNTIENFQLRIENSIVLPFGDSTLDITVLAQMDKDFSMSILKDLVRNLRLAMV | Homodimer. Expressed in roots and leaves. By cold treatment. Extended C-terminus. |
Q67Z70 | MDDSSFMDLMIDTDEYLIDDWESDFPICGETNTNPGSESGSGTGFELLAERPTKQMKTNNNMNSTSSSPSSSSSSGSRTSQVISFGSPDTKTNPVETSLNFSNQVSMDQKVGSKRKDCVNNGGRREPHLLKEHVLAERKRRQKLNERLIALSALLPGLKKTDKATVLEDAIKHLKQLQERVKKLEEERVVTKKMDQSIILVKRSQVYLDDDSSSYSSTCSAASPLSSSSDEVSIFKQTMPMIEARVSDRDLLIRVHCEKNKGCMIKILSSLEKFRLEVVNSFTLPFGNSTLVITILTKMDNKFSRPVEEVVKNIRVALAE | Transcription activator that regulates the expression of at least NAI2, PYK10 and PBP1. Required for and mediates the formation of endoplasmic reticulum bodies (ER bodies). Involved in the symbiotic interactions with the endophytes of the Sebacinaceae fungus family, such as Piriformospora indica and Sebacina. Homodimer. Expressed constitutively in roots, leaves, stems, and flowers. |
Q5XEY8 | MTWKPKMLILSHDLISPEKYIMGEDDIVELLGKSSQVVTSSQTQTPSCDPPLILRGSGSGDGEGNGPLPQPPPPLYHQQSLFIQEDEMASWLHQPNRQDYLYSQLLYSGVASTHPQSLASLEPPPPPRAQYILAADRPTGHILAERRAENFMNISRQRGNIFLGGVEAVPSNSTLLSSATESIPATHGTESRATVTGGVSRTFAVPGLGPRGKAVAIETAGTQSWGLCKAETEPVQRQPATETDITDERKRKTREETNVENQGTEEARDSTSSKRSRAAIMHKLSERRRRQKINEMMKALQELLPRCTKTDRSSMLDDVIEYVKSLQSQIQMFSMGHVMIPPMMYAGNIQQQYMPHMAMGMNRPPAFIPFPRQAHMAEGVGPVDLFRENEETEQETMSLLLREDKRTKQKMFS | Homodimer. Expressed constitutively in leaves, stems, and flowers. |
Q8S3F0 | MSILSTRWFSEQEIEENSIIQQFHMNSIVGEVQEAQYIFPHSFTTNNDPSYDDLIEMKPPKILETTYISPSSHLPPNSKPHHIHRHSSSRILSFEDYGSNDMEHEYSPTYLNSIFSPKLEAQVQPHQKSDEFNRKGTKRAQPFSRNQSNAQDHIIAERKRREKLTQRFVALSALVPGLKKMDKASVLGDALKHIKYLQERVGELEEQKKERRLESMVLVKKSKLILDDNNQSFSSSCEDGFSDLDLPEIEVRFSDEDVLIKILCEKQKGHLAKIMAEIEKLHILITNSSVLNFGPTLDITIIAKKESDFDMTLMDVVKSLRSALSNFI | Homodimer. Expressed in flowers. By ethylene (ACC) and jasmonic acid (JA) treatments. |
Q8GYC3 | MEDLDHEYKNYWETTMFFQNQELEFDSWPMEEAFSGSGESSSPDGAATSPASSKNVVSERNRRQKLNQRLFALRSVVPNISKLDKASVIKDSIDYMQELIDQEKTLEAEIRELESRSTLLENPVRDYDCNFAETHLQDFSDNNDMRSKKFKQMDYSTRVQHYPIEVLEMKVTWMGEKTVVVCITCSKKRETMVQLCKVLESLNLNILTTNFSSFTSRLSTTLFLQVTLSLSPSLISLFGNVITSTNYKILNASREYCTCLVLV | Homodimer. Expressed constitutively in roots, leaves, stems, and flowers. |
Q9LUK7 | MINTDDNLLMIEALLTSDPSPPLLPANLSLETTLPKRLHAVLNGTHEPWSYAIFWKPSYDDFSGEAVLKWGDGVYTGGNEEKTRGRLRRKKTILSSPEEKERRSNVIRELNLMISGEAFPVVEDDVSDDDDVEVTDMEWFFLVSMTWSFGNGSGLAGKAFASYNPVLVTGSDLIYGSGCDRAKQGGDVGLQTILCIPSHNGVLELASTEEIRPNSDLFNRIRFLFGGSKYFSGAPNSNSELFPFQLESSCSSTVTGNPNPSPVYLQNRYNLNFSTSSSTLARAPCGDVLSFGENVKQSFENRNPNTYSDQIQNVVPHATVMLEKKKGKKRGRKPAHGRDKPLNHVEAERMRREKLNHRFYALRAVVPNVSKMDKTSLLEDAVCYINELKSKAENVELEKHAIEIQFNELKEIAGQRNAIPSVCKYEEKASEMMKIEVKIMESDDAMVRVESRKDHHPGARLMNALMDLELEVNHASISVMNDLMIQQANVKMGLRIYKQEELRDLLMSKIS | Homodimer. By UV treatment. |
Q9S7Y1 | MCAKKEEEEEEEEDSSEAMNNIQNYQNDLFFHQLISHHHHHHHDPSQSETLGASGNVGSGFTIFSQDSVSPIWSLPPPTSIQPPFDQFPPPSSSPASFYGSFFNRSRAHHQGLQFGYEGFGGATSAAHHHHEQLRILSEALGPVVQAGSGPFGLQAELGKMTAQEIMDAKALAASKSHSEAERRRRERINNHLAKLRSILPNTTKTDKASLLAEVIQHVKELKRETSVISETNLVPTESDELTVAFTEEEETGDGRFVIKASLCCEDRSDLLPDMIKTLKAMRLKTLKAEITTVGGRVKNVLFVTGEESSGEEVEEEYCIGTIEEALKAVMEKSNVEESSSSGNAKRQRMSSHNTITIVEQQQQYNQR | Homodimer (Probable). Interacts with LHW. |
Q9LS08 | MYAMKEEDCLQTFHNLQDYQDQFHLHHHPQILPWSSTSLPSFDPLHFPSNPTRYSDPVHYFNRRASSSSSSFDYNDGFVSPPPSMDHPQNHLRILSEALGPIMRRGSSFGFDGEIMGKLSAQEVMDAKALAASKSHSEAERRRRERINTHLAKLRSILPNTTKTDKASLLAEVIQHMKELKRQTSQITDTYQVPTECDDLTVDSSYNDEEGNLVIRASFCCQDRTDLMHDVINALKSLRLRTLKAEIATVGGRVKNILFLSREYDDEEDHDSYRRNFDGDDVEDYDEERMMNNRVSSIEEALKAVIEKCVHNNDESNDNNNLEKSSSGGIKRQRTSKMVNRCYN | Transcription factor required for MONOPTEROS-dependent root initiation in embryo. Transcriptionally controlled by MONOPTEROS. Homodimer (Probable). Interacts with LHW. At the globular stage, expressed in cells adjacent to the hypophysis and at later embryonic stages, specific for vascular tissues. No visible phenotype, probably due to redundancy with BHLH30. |
Q8S3E8 | MYPSIEDDDDLLAALCFDQSNGVEDPYGYMQTNEDNIFQDFGSCGVNLMQPQQEQFDSFNGNLEQVCSSFRGGNNGVVYSSSIGSAQLDLAASFSGVLQQETHQVCGFRGQNDDSAVPHLQQQQGQVFSGVVEINSSSSVGAVKEEFEEECSGKRRRTGSCSKPGTKACREKLRREKLNDKFMDLSSVLEPGRTPKTDKSAILDDAIRVVNQLRGEAHELQETNQKLLEEIKSLKADKNELREEKLVLKAEKEKMEQQLKSMVVPSPGFMPSQHPAAFHSHKMAVAYPYGYYPPNMPMWSPLPPADRDTSRDLKNLPPVA | Homodimer. Expressed constitutively in roots, leaves, stems, and flowers. |
Q9LU71 | MEDIVDQELSNYWEPSSFLQNEDFEYDRSWPLEEAISGSYDSSSPDGAASSPASKNIVSERNRRQKLNQRLFALRSVVPNITKMDKASIIKDAISYIEGLQYEEKKLEAEIRELESTPKSSLSFSKDFDRDLLVPVTSKKMKQLDSGSSTSLIEVLELKVTFMGERTMVVSVTCNKRTDTMVKLCEVFESLNLKILTSNLTSFSGMIFHTVFIEADEEEQEVLRLKIETGIGAYNETQSPTLSIDSLY | Homodimer. Expressed constitutively in roots, leaves, stems, and flowers. |
Q9FLI1 | MEKMMHRETERQRRQEMASLYASLRSLLPLHFIKGKRSTSDQVNEAVNYIKYLQRKIKELSVRRDDLMVLSRGSLLGSSNGDFKEDVEMISGKNHVVVRQCLVGVEIMLSSRCCGGQPRFSSVLQVLSEYGLCLLNSISSIVDDRLVYTIQAEVNDMALMIDLAELEKRLIRMK | Homodimer. Expressed constitutively in roots, leaves, stems, and flowers. |
Q9LTS4 | MMHLILSCSYLISMDGYYNEASEEPSSSSSSGSLARSLFHEYRQSVIPLQNGHVPSMAFMNNLPYVEIRPQESQRLAFNDTQRLFYQMKIEASLREWFPEDFNRKSSPANSDYLRPPHYPSSSSSSLSPNNISEYSSLLFPLIPKPSTTTEAVNVPVLPPLAPINMIHPQHQEPLFRNRQREEEAMTQAILAVLTGPSSPPSTSSSPQRKGRATAFKRYYSMISDRGRAPLPSVRKQSMMTRAMSFYNRLNINQRERFTRENATTHGEGSGGSGGGGRYTSGPSATQLQHMISERKRREKLNESFQALRSLLPPGTKKDKASVLSIAREQLSSLQGEISKLLERNREVEAKLAGEREIENDLRPEERFNVRIRHIPESTSRERTLDLRVVLRGDIIRVDDLMIRLLEFLKQINNVSLVSIEARTLARAEGDTSIVLVISLRLKIEGEWDESAFQEAVRRVVADLAH | Homodimer. |
Q9SN74 | MVSKTPSTSSDEANATADERCRKGKVPKRINKAVRERLKREHLNELFIELADTLELNQQNSGKASILCEATRFLKDVFGQIESLRKEHASLLSESSYVTTEKNELKEETSVLETEISKLQNEIEARANQSKPDLNTSPAPEYHHHHYQQQHPERVSQFPGLPIFQGPGFQQSATTLHPPATVLVLPIQPDPQTQDISEMTQAQQPLMFNSSNVSKPCPRYASAADSWSSRLLGERLKASE | Homodimer (Probable). Forms heterodimer with PYEL proteins bHLH115, bHLH104 and ILR3 (PubMed:25452667). Expressed constitutively in roots, leaves, stems, and flowers. |
Q9SLC9 | MDLTQGFRARSGVVGPVAGLESLNFSDEFRHLVTTMPPETTGGSFTALLEMPVTQAMELLHFPDSSSSQARTVTSGDISPTTLHPFGALTFPSNSLLLDRAARFSVIATEQNGNFSGETANSLPSNPGANLDRVKAEPAETDSMVENQNQSYSSGKRKEREKKVKSSTKKNKSSVESDKLPYVHVRARRGQATDNHSLAERARREKINARMKLLQELVPGCDKIQGTALVLDEIINHVQTLQRQVEMLSMRLAAVNPRIDFNLDSILASENGSLMDGSFNAESYHQLQQWPFDGYHQPEWGREEDHHQANFSMGSATLHPNQVKMEL | Homodimer. A number of isoforms are produced. According to EST sequences. Expressed in leaves, stems, and flowers. No experimental confirmation available. |
Q8S3E7 | MDLSAKDEFSAEKRNPDNYDSVNNPSGDWRVDSYPSENLISAGPASCSPSQMMDSFGQTLWYDPTSVQAVGYAGFNGGNASSSSFRGSIDRSLEMGWNLPNLLPPKGNGLFLPNASSFLPPSMAQFPADSGFIERAARFSLFSGGNFSDMVNQPLGNSEAIGLFLQGGGTMQGQCQSNELNVGEPHNDVSVAVKESTVRSSEQAKPNVPGSGNVSEDTQSSGGNGQKGRETSSNTKKRKRNGQKNSEAAQSHRSQQSEEEPDNNGDEKRNDEQSPNSPGKKSNSGKQQGKQSSDPPKDGYIHVRARRGQATNSHSLAERVRREKISERMKFLQDLVPGCNKVTGKAVMLDEIINYVQSLQRQVEFLSMKLATVNPQMDFNLEGLLAKDALQLRAGSSSTTPFPPNMSMAYPPLPHGFMQQTLSSIGRTITSPLSPMNGGFKRQETNGWEGDLQNVIHINYGAGDVTPDPQAAATASLPAANMKVEP | Transcriptional activator involved in cell elongation. Regulates the expression of a subset of genes involved in cell expansion by binding to the G-box motif. Homodimer (Probable). Interacts with IBH1. Expressed constitutively in roots, stems, and flowers. Plants over-expressing BHLH49 show increased hypocotyl and cotyledon lengths and increased flower size. May be due to a competing acceptor splice site. |
Q9XEF0 | MENSYDSSKWSDSTTPYMVSWSLQSESSDSDWNRFNLGFSSSSFGGNFPADDCVGGIEKAESLSRSHRLAEKRRRDRINSHLTALRKLVPNSDKLDKAALLATVIEQVKELKQKAAESPIFQDLPTEADEVTVQPETISDFESNTNTIIFKASFCCEDQPEAISEIIRVLTKLQLETIQAEIISVGGRMRINFILKDSNCNETTNIAASAKALKQSLCSALNRITSSSTTTSSVCRIRSKRQRWFLSSHYSHNE | Homodimer. Expressed constitutively in roots, stems, and flowers. Repressed by salicylic acid (SA) treatment. |
Q8S3E6 | MIIPETDSFFFQEQPQHQPLYPDEALSPSLFGFDHYDHFYESFLPSQEIFLPSPKTRVFNESQELDSFHTPKHQKLIDSSFHFNSHDPFSPSPESNYLLDSYITEASNISKFQAPDFSSTFKVGWTEQGDTKKRELSAQSIAARKRRRRITEKTQELGKLIPGSQKHNTAEMFNAAAKYVKFLQAQIEILQLKQTKMQTLDSSKVGREMQFLLGSQEIQEKLSTEEVCVVPREMVQVLKAEECILTNPKISRDINKLLSTNLMN | Homodimer. Expressed constitutively in roots, leaves, stems, and flowers. |
Q80TH0 | MEEILRKLQRDASGSKYKAIKESCTWALETLGGLDTVVKIPPHLLREKCLLPLQLALESKNVKLAQHALAGMQKLLSEERFVSMETDSDEKQLLNQILNAVKVTPSLNEDLQVEVMKVLLCITYTPTFDMNGSAVLKIAEVCIETYTCSCHQRSINTAVRATLSQMLGDLTLQLRQRQENTIIENPDAPQEFRSQGLTVEALCDDVISVLAVLCEKLQASINDSQQLQLLYLECILSVLSSSSSSMHLHRGFTDLIWKSLCPALVVILGNPIHDKTITSAHSTSTSTSMESDSASLGVSDHGRGSGCSCTAPTLSGPVARTIYYLAAELVRLVGSVDSMKPVLQSLYHRVLLYPPPQHRVEAIKIMKEILGSPQRLYDLAGPSSIESEPRKRSISKRKSHLDLLKLIMDGMTEACIKGGIEACYAAVSCVCTLLGALDELSQGKGLNDTQVQQLLLRLEELRDGAESSRDSMEINEADFRWQRRVLSSEHTPWESGNERSPDISISVTTDTGQTTLEGELGQTTPEDHKNGLKSPAIQEGKGTMGKVSEPEAIDQPDVVQRSHTVPYPDITNFLSVDCRTRSYGSRYSESNFSVDDQDLSRTEFDSCDQYSMAAEKDSGRSDVSDIGSDNCSLADEEQTPRDYIGHRSLRTAALSLKLLKNQEADQHSARLFIQSLEGLLPRLLALSSVEEVDSALQNFASTFCSGMMHSPGFDGGSSLSFQMLMNADSLYTAAHCALLLNLKLSHGDYYRKRPTVAPGMMKEFMKQVQTSGVLMVFSQAWLEELYHQVLDRNMLGEAGYWGSPEDNSLPLITMLTDIDGLESSAIGGQLMASASVESPFTQSRRLDDSTVAGVAFARYILVGCWKNLIDTLSTPLTGRMAGSSKGLAFILGAEGIKEQNQKERDAICMSLDGLRKAARLSCALGVAANCASALAQMAAASCVQEEKEERQSQEPSDALAQVKLKVEQKLEQMGKVQGVWLHTAHVLCMDAILSVGLEMGSHNPDCWPHVFRVCEYVGTLEHTHFSDGISQPPLTIHQPQKTSGSSGLLGEIEFKSSSQEQSLEQGPSLNTAPVVQPHSIQELVRECSRGRTSDFRGGSLSGNSAAKVVLSLSTQADRLFDDATDKLNLTALGGFLYQLKKASQSQLFHSVTDTVDYSLTMPGEVKSTQDQKSALHLFRLGDAMLRIVRSKARPLLHVMRCWSLVAPHLVEAACHKERHVSQKAVSFIHDILTEVLTDWSEPPHFHFNEALFRPFERIMQLELCDEDVQDQVVTSIGELVEVCSAQIQSGWRPLFSALETVRSGNKSEVKEYLVGDYSMGKGQAPVFDVFEAFLNTDNIQVFANAATSYIMCLMKFVKGLGEVDCKEIGDCVPGAGATSTDLCLPALDYLRRCSQLLAKIYKMPLKPIFLSGRLASLPRRLQEQSASSEDGIESVLSDFDDDTGLIEVWIILLEQLTAAVSNCPRQHQPPTLDLLFELLRDVTKTPGPGFGIYAVVHLLLPVMSLWLLRSHKDHSYWDVASANFKHAIGLSCELVVEHIQSFLHSDIRYESMINTMLKDLFELLVVCVAKPTETISRVGCSCIRYVLVTAGPVFTEEMWRLACCALQDAFSATLKPVKDLLGCFHGGTEGFSGEGCQVRVAAPSSSPSAEAEYWRIRAMAQQVFMLDTQCSPKTPNNFDHAQSCQLIIELPHDEKPNGHAKKSVSFREIVVSLLSHQVLLQNLYDILLEEFVKGPSPGEEKTVQVPDTKLAGFLRYISMQNLAVIFDLLLDSYRTAREFDTSPGLKCLLKKVSGIGGAANLYRQSAMSFNIYFHALVCAVLTNQETITAEQVKKVLFEEEERSSDSSQQCSSEDEDIFEETAQVSPPRGKEKRQWRARLPSLSVQPVSNADWVWLVKRLHKLCMELCNHYIQMHLDLESSLEEPLTFKSDPFFILPSFQSESSTPSTGGFSGKNTPSEDDRREHLSEPQSLRVGSGDMLMLPPSPKTEKKDPGRKKEWWESAGNKICTMAADKTISKLMTEYKKRRQPHNLPPFPKEVKVDKKGEPLGPRGPDSPLLQRPQHLIDQGQMRHSFSAGPELLRQEKRPRSGSTGSSLSVSVRDAEAQIQAWTNMVLTVLNQIQILPDQTFTALQPAVFPCISQLTCHVTDIRVRQAVREWLGRVGRVYDIIT | Participates in the regulation of systemic glucose homeostasis, where it negatively regulates insulin granule biogenesis in pancreatic islet beta cells (PubMed:24711543). Also regulates glucagon granule production in pancreatic alpha cells (PubMed:25737957). Inhibits nuclear translocation of the transcriptional coregulator PHB2 and may enhance estrogen receptor alpha (ESR1) transcriptional activity in breast cancer cells (By similarity). Interacts with PHB2 (By similarity). Expressed in pancreatic islet (insulin granules of islet alpha and beta cells) and brain (at protein level). Viable and fertile with normal body weight gain. Mice exhibit postprandial hyperinsulinemia and hyperglycemia, and impaired glucose tolerance. Three month old animals show severe insulin resistance in liver and muscle tissue, probably due to chronic insulin exposure. |
O65490 | MSTSQTLGGATRCGRIIGPSLDKIIKNAAWRKHTYLVSSCKSVLDKLESLPDDFHDPSSVVSGLAASDADSVLQPFLLSLETAYSKVVEPSLDCAFKLFSLSILRGEIQSSKQDSILFKLVNAVSKVGAIAEEPIQLAVLRVLLAAVRSPCILIRGDCLLHVVKTCYNIYLGGLSGTTQICAKSVLAQMMLVIFTRSEEDSLDVSVKTIYVNELLTFTDKSVNEGSSVYFCQGFVNEVMAAGQGSPLPPPDVIQILLQNPETETVMTPDSPSFRGYVANGEGDSETGDMSKVRQDAFLLFKNLCKLSMRFSSKENNDDQIMVRGKTLSLELLKVIIDNGGSVWRTNESFINAVKQYLCLSLLKNSAVSIMSIFQLQCAIFMSLLSKLRSVLKAEIGIFFPMIVLRVLENVLQPSYLQKMTVLNLLDKMSQDPQLMVDIFVNYDCDVESSNILERIVNGLLKTALGPPTGSSTTLSPAQDSTFRNDSVKCLVNLAKAMGNWMDQQLKVNETVWPKGSQVYASMDSNASQISELEGTISDCDSQPDTSNPEAYDASMLEQRRAYKIELQKGISLFNRKPSKGVEFLISTKKIGSSPEEVASFLMKTAGLNGTVIGDYLGERDELPLKVMHAYVDSFNFEKKDFVEAIRFFLRGFRLPGEAQKIDRIMEKFAEHYWKCNPGSFTSADTAYVLAYSVIMLNTDAHNNMVKDKMTKADFVRNNRGIDDGKDLPEEYLGSLYDRVVKEEIRMNSDTLAPQNKQVNGLNKLLGLDGILNLVSWMQPDEKPHGANGRLIRDIQEQFQAKPEKSESVYHTVTDISILRFILEVSWGPMLAAFSVTIDQSDDRLATSLCLQGFRYAVHVTAVMGMQTQRDAFVTSMAKFTNLHCAADMKQKNVDAVKAIITIAIEDGNHLHGSWEHILTCLSRIEHLQLLGEVSPSEKRYVPTKKAEVDDKKALGFPNLKKRGSFQNPSVMAVVRGGSYDSTSLVKSVPKLVTPEQIKSFIANLNLLDQIGNFELNHVYANSQRLNSEAIVSFVKALCKVSMSELQSPTDPRVFSLTKLVETAHYNMNRIRLVWSRIWNVLSDFFVSVGLSENLSVAIFVMDSLRQLSMKFLEREELANYHFQHEFLRPFVVVMQKSSSAEIRELIVRCVSQMVLSRVSNVKSGWKNVFTVFTTAALDERKNIVLLAFETIEKIVRDHFHCIIETEITVYADCIRCLITFTNSKFEGDIGFNTIEFLRFCALKLEEGGLVLNEKLKNNTISALKEDFSDTQSFTDLDEQVSYWIPLLTGLCKQVSDPRPAIRKRSIEVLFHILMDHGHLFTRPFWTGIFSSIILPVFNNIRSKTDMLFEESVDSPSSASLDTEETTWDVETSTLALQLLVDLLVKFFRSVRSQLPSVVSIIVGFIKSPFQGSTGSGISVLLHLADGLARSASEDEWREIFLALKEAASLTFAGFMKVLRTMDDIEDVETLSGQSVNIGDLDDDSLHIMSYVVSRTKKHIDVLSQIVEVVSDLYRRNQFSLSASHVDILADIFSCIASHAQQLNTDTVLRRKFKRACSVQNLTEPQLLNFENEAYKSYMMFLQDMVTCNPNVSKELDLESRLVTECAKIVKIYLKCTDPQQQEQQQRKPVLWVLPMESDRVEEATARTSLLVSSLEALCSLEAESLKKHVSSFFPLLVDLVRTEHCSPQVPYVLSNVLKSCIGPILA | Activates the ARF proteins by exchanging bound GDP for free GTP. Plays a role in vesicular protein sorting (By similarity). Inhibited by brefeldin A. Homodimer. Soluble and partially membrane-bound. |
Q9LXK4 | MAAGGFLTRAFDTMLKESGGKKFPDLQKAIQAYQDGSKVVTQAAPSSIVESSQAEGGGEKTGVEADEPQKVTSAEVAQQASQSKSETINVSLANAGHTLGGAEVELVLKPLRLAFETKNLKIFDAALDCLHKLIAYDHLEGDPGLDGGKNSAPFTDILNMVCSCVDNSSPDSTVLQVLKVLLTAVASGKFKVHGEPLLGVIRVCYNIALNSKSPINQATSKAMLTQMISIVFRRMETDIVSASSTVSQEEHVSGDTSSPKNEEITAADENEKEMTLGDALTQAKDTTLASVEELHTLVGGADIKGLEAALDKAVHLEDGKKIKRGIELESMSIGQRDALLVFRTLCKMGMKEDSDEVTTKTRILSLELLQGMLEGVSHSFTKNFHFIDSVKAYLSYALLRASVSQSSVIFQYASGIFSVLLLRFRDSLKGEIGIFFPIIVLRSLDNSECPNDQKMGVLRMLEKVCKDPQMLVDVYVNYDCDLEAPNLFERMVTTLSKIAQGSQSADPNPAMASQTASVKGSSLQCLVNVLKSLVDWEKIRREAENSTRNANEDSASTGEPIETKSREDVPSNFEKAKAHKSTMEAAISEFNRNSVKGVEYLIANKLVERNPASVAQFLRSTSSLSKVMIGDYLGQHEEFPLAVMHAYVDSMKFSEMKFHSAIREFLKGFRLPGEAQKIDRIMEKFAERYCADNPGLFKNADTAYVLAYAVIMLNTDAHNPMVWPKMSKSDFTRMNATNDPEDCAPTELLEEIYDSIVQEEIKLKDDDTMKKLSSQRPGGEERGGLVSILNLGLPKRISAADAKSETEDIVRKTQEIFRKHGVKRGVFHTVEQVDIIRPMVEAVGWPLLAAFSVTMEVGDNKPRILLCMEGFKAGIHIAYVLGMDTMRYAFLTSLVRFTFLHAPKEMRSKNVEALRILLGLCDSEPDTLQDTWNAVLECVSRLEFIISTPGIAATVMHGSNQISRDGVVQSLKELAGRPAEQVFVNSVKLPSESVVEFFTALCGVSAEELKQSPARVFSLQKLVEISYYNIARIRMVWARIWSVLAEHFVSAGSHHDEKIAMYAIDSLRQLGMKYLERAELTNFTFQNDILKPFVIIMRNTQSQTIRSLIVDCIVQMIKSKVGSIKSGWRSVFMIFTAAADDEVESIVEKSFENVEQVILEHFDQVIGDCFMDCVNCLIRFANNKASDRISLKAIALLRICEDRLAEGLIPGGVLKPVDGNEDETFDVTEHYWFPMLAGLSDLTSDYRPEVRNCALEVLFDLLNERGNKFSTPFWESIFHRILFPIFDHVSHAGKESLISSGDVKFRETSIHSLQLLCNLFNTFYKEVCFMLPPLLSLLLDCAKKSDQTVVSISLGALVHLIEVGGHQFSEGDWDMLLKSIRDASYTTQPLELLNALSFDNPKKNLVLAGDIEADASDSPRVDRNPDDIKDNGKVSAQASPRIGTHGTSLESGIPPKADGSEGRPSSSGRAQKDVDDVNLQRSQTFGQRFMDNLFLRNLTSQPKSSVAEVTVPSSPYKHEDPTEPDSREEESPALGAIRGKCITQLLLLGAINSIQQKYWSNLKTPQKIAIMDILFSFIEFASSYNSYSNLRTRMNHIPTERPPLNLLRQELEGTTIYLDVLQKTTSGLADDASNSEDRLEGAAEEKLVSFCEQVLKETSDLQSTLGETTNMDVHRVLELRSPVIVKVLEGMCFMNNTIFRKHMREFYPLLTRLVCCEQMEIRGALANLFKAQLKPLLQQ | Activates the ARF proteins by exchanging bound GDP for free GTP. Plays a role in vesicular protein sorting. Acts as the major regulator of early endosomal vesicle trafficking, particularly at the trans-Golgi-network/early endosome (TGN/EE), but is also involved in the endocytosis process (PubMed:23737757). Together with VPS45/BEN2 required for polar PIN-FORMED (PIN) proteins localization, for their dynamic repolarization, and consequently for auxin activity gradient formation and auxin-related developmental processes (e.g. embryonic patterning, organogenesis and vasculature venation patterning) (PubMed:23737757). Target of hopM1, a conserved Pseudomonas syringae virulence protein that directs the protein to its own proteasome-mediated degradation. Plays a broad role in PAMP-triggered immunity (PTI), effector-triggered immunity (ETI), and salicylic acid (SA)-regulated immunity. Inhibited by brefeldin A. Homodimer (By similarity). Interacts with hopM1 (PubMed:16840699). Interacts with HLB1 (PubMed:26941089). Soluble and partially membrane-bound. A number of isoforms are produced. According to EST sequences. By the pathogen elicitor flagellin 22 and by benzothiadiazole (BTH), a synthetic activator of the salicylic acid (SA)-dependent immunity (at protein level). Ubiquitinated. Inhibited trafficking at the trans-Golgi-network/early endosome (TGN/EE) leading to an increased accumulation of PIN2 in agglomerated intracellular compartments leading to an altered auxin gradient and subsequent growth defects (e.g. disrupted roots architecture and shoot growth) (PubMed:23737757). Increased susceptibility to Pseudomonas syringae infection (PubMed:16840699). Displays growth and polarity defects (PubMed:19230664). |
Q9XCQ3 | MNPMQKKKLISIAIALTLQSYYIPAIAAENNDDEKECPSNISSLPKEKRAKLSPTCLATPENDNHWGWVAGGVAALVAGVAIGVENNGGGDSNHSYTPPKPDNGGDVTPPDDGGNVTPPDDGGNVTPPDDGGDDNVTPPDDSGDDDVAPPDDSGDDDVTPPDDSGDDDVTPPDDSGDGDVTPPDDSGDDDVTPPDDSGDDDVTPPDDSGDDDVTPPDDSGDDDVTPPDDSGDDDVTPPDDSGDDDDTPPDDSVITFSNGVTIDKGKDTLTFDSFKLDNGSVLEGAVWNYSEQDNQWQLTTADGKTLNVTGWDVTDANAAVIEGTQENGLYWKYDSRGYLIIADDNTTVISGDDQAHNSDRGMDISGQDRTGVIISGDRTVNTLTGDSSVTDGATGMVISGDGTTNTISGHSTVDNATGALISGNGTTTNFAGDIAVSGGGTAIIIDGDNATIKNTGTSDISGAGSTGTVIDGNNARVNNDGDMTITDGGTGGHITGDNVVIDNAGSTTVSGADATALYIEGDNALVINEGNQTISGGAVGTRIDGDDAHTTNTGDIAVDGAGSAAVIINGDNGSLTQAGDLLVTDGAMGIITYGTGNEAKNTGNATVRDADSVGFVVAGEKNTFKNKGDIDVSLNGTGALVSGDMSQVTLDGDINVVSVQDSEGVFSSATGVSVSGDSNAVDITGNVNISADYGQDDLAAGAPPLTGVVVGGNGNTVTLNGALNIDDNDLSATGGQYLDVVGLSVTGDDNDVEIDGGINITHSEDPLDGTSADITGISVSGNSTVTLNGHSTIDTNTVVGGHVVLARVNNGGSLILGDDSVVDVNVSYIPTGYYTYNALLMADGEGTSIENKGDITSHGVYSVIRADNGSEVSNSGDILVYATSSNSSEDRAAITRASGEGSAVHNKAGGDITLISDQTPQGSGGIEVYPLKWYTHTFYAMMASDYGDVVNDEGATIHLQGAGVYGVTASRGKALNEGNIYLDGLVPTLDDENNITSTSYWQPSSLYLTSSGMVAGSTDADGDATAINTGNITVNNAGFGMMALNGGTAINQGVITLTADDGVTGQADELVGMAALNGGVVINDTSGVINIDADYGQAFLSDSSSYIINNGSINLNGSPMDDTDSHMGGTPTDKIWIQSLPGSGDSDTRTSDTGFFTAGTLANYGTETLNGDVDVNGGWLYNEAGASLTVNGTVTINGGANALANYGTLDADAISTWHSLFNEADGSITTDLLTLNGDVTFYNNGDFTGSIAGTSYQQEIVNTGDMTVAEDGKSLVSGSFYFYNEEDATLTNSGSAVEGGENTIINLTRANDSLTQVNSGTITATNGYSAITTVNGSNDPKWIWNTATGVINGINPDAPLINLGRGYNFGNQGTINVQGDNAVAISGGTSSYVINLVNSGTINVGTEQGKEDGTNGTGLIGIKGNGNATTINNTADGVINVYADDSYAFGGKTKAIINNGEINLLCDSGCDIYAPGTTGTQNDHNGTADIVIPDATTAPTEGSIPTPPADPNAPQQLSNYIVGTNADGSSGTLKANNLVIGDNVKVDTGFTSGTADTTVVVDNAFTGSNIQGADNITSTSVVWNAQGSQDADGNVDVTMTKNAYADVATDSSVSDVAQALDAGYTNNELYTSLNVGTTAELNSALKQVSGAQATTVFREARVLSNRFTMLADAAPQIKDGLAFNVVAKGDPRAELGNDTQYDMLALRQTLDLTASQNLTLEYGIARLDGDGSKTAGDNGLTGGYSQFFGLKHSMAFDEGLAWNNSLRYDVHNLDSSRSVAYGDVNKIADSDMRQQYLEFRSEGAKTFTMMGDALKVTPYAGVKFRHTMEDGYKERSAGDFNLSMNSGNETAVDSIVGLKLDYAGKDGWSATATLEGGPNLSYSKSQRTASLQGAAGQSFGVDDGQKGGGVNGLATIGVKYSSNDTALHLDAYQWKEDGISDKGFMLNVKKTFR | Truncated N-terminus. |
Q7CSJ3 | MVTETPLEKPLDIGEIPLPAMEKRATEVAILLKTLAHPARLMLACTLAQGEFSVGELEAKLDIRQPTLSQQLGVLREAGIVDTRREAKQIFYRLAEDKAARLIEALYAIFCAPEENL | Represses an operon that comprises at least itself and blh. Binds to a palindromic AT-rich sequence spanning the -10 region of the blh promoter and blocks transcription of the operon. Cells show altered biofilm formation; on glass surfaces and on tobacco root surfaces, it exhibits a greater biofilm mass than the wild-type. |
Q9PFB1 | MVNEMRDDTRPHMTREDMEKRANEVANLLKTLSHPVRLMLVCTLVEGEFSVGELEQQIGIGQPTLSQQLGVLRESGIVETRRNIKQIFYRLTEAKAAQLVNALYTIFCAQEKQA | Represses an operon that comprises itself, XF_0764, XF_0765, XF_0766 and blh. Binds to a palindromic AT-rich sequence spanning the -10 region of the blh promoter and blocks transcription of the operon. |
Q87AD5 | MVNEMRDNTVPHMTREDMEKRANEVANLLKTLSHPVRLMLVCTLVEGEFSVGELEQQIGIGQPTLSQQLGVLRESGIVETRRNIKQIFYRLTEAKAAQLVNALYTIFCTQEKQA | Represses an operon that probably comprises itself, PD_1892, PD_1893, PD_1894 and blh. Binds to a palindromic AT-rich sequence spanning the -10 region of the blh promoter and blocks transcription of the operon (By similarity). |
F4J4S0 | MADDLANLCRFLFDDTAFPSLSSSASSDLFSRRLRSDDSIKRGLRSFYLLLRWGVAPIGGDDADSSGKLRFETWSDSQLQALVSISQAILLLSRSLLGTDLTLNQGLVDQLEPIVLGVIQEVMEFSLSFLEKSSFRQNDLKMEINMEILLEIASFDGSEKQYDILPDFSPAEVAELWPAFSGEHDNMDAQSLVKCTFQGGRCSNEEKPVDRLLITLMSECIESDVQAQSVVKSPFQQDCGDLNPFTRHLAVVHLRCVCRLIMVCKELVQLPNMLDEKTVDQAVLDKLSFCLRILKLLGSLSKDVQSIENDGSLLQAVASFTDAFPKLFRVFFEFTNHTATEGNIESLSLALVEGFLNLVQLIFGKSSVFQNVQACVAASIVSNLDSSVWRYDGSSCNLTPPLAYFPRSVIYTLKLIQDLKRQPYHIHDLRVLESEVTYEDVSSTVDSVYFHLRQEKIPLLKCFTVEDIMRVIFPSSSQWMDNFFHLVYFLHREGVKLRPKVERTYSSLRSNSFAEVESQISHDDEALFGNLFSEGSRSLCSIEPNDQPPVSVSSNLLLQAAKELLNFLRACILCQEWVPSIYEDGCKKLDTGHIDILLNIVGCSIEDKASDGGCMLQDEGRPGHVAFELLLNLLRSRALSDFLESYLFQQILVVENSDFNYNDKTLALLAHTLLCRPGLAGAQLRAKIYDGFVSFVTERARGICAEALSLKELTACLPSAFHIEILLMAFHLSNEAEKAKFSNLIASCLHKVDTPAGICDGPQLSSWAMLISRLLVLLHHMLLHPNTCPTSLMLDLRSKLREVRSCGSNLHVTVGDHLSSWASLVARGITDSWAEDESVSHLMSQMIDFSPHPPTFQNDVSTAKTLNLDYGDLSASLCRVLGLWKGKKAGKVEDLLVERYIFMLSSDIARINCALDSQPSLHVNYQNVDISNSVDLISTSHLLVGDINVVGRNIELRNILIGVLNQLQAAPEQVVEDLGWDYIREGAWLSLLLYFLDGGVWDYCNKNSCSEIDPFWKECTSVDAKYVAAAEGVVSYLMKTGDIAELLRMLSSLVGKYLRVYKKAFLATFSDWNHHGHSSPSLLLLKHTQFGKSLQGEYAKIGDNSLHLQCIFYLSKLDSLGDGRGSGVLWKVFWEFMVHGFPTSLQTSSAILLSCILSIRCIVLTINGLLKLGNSKEKFGVDTSVLHQLLDSIMIIKFDQVFESFHGKCEEIHQNICAVLQLPDLTELFLMKDMEGFVRDISAEQIDRSQVLEGVITKIVDVMDSLSKDSSKSDIFKFYLGVDAVSEHTREFYELQRGDLSVFIDSLDYCSLEPVNIKVLNFLVDLLSVAQSPDLRRRVQQKFIDMDLISLSGWLERRLLGSFVEEIDGKKTAKGNSLPFREAAMNFINCLVSSTNDLQTRELQNHLFEALLISLDTAFLSFDIHMSMSYFHFVLQLAREDNLMKMVLKRTIMLMEKLAAEEKLLPGLKFIFGVIGTLLSNRSPSHGESLCGKSLASYKNTATGPLVPKLSGTTKKSDTLALPVDQEGSSISLECDVTSVDEDEDDGTSDGEVASLDKEDEEDANSERYLASKVCTFTSSGSNFMEQHWYFCYTCDLTVSKGCCSVCAKVCHRGHRVVYSRSSRFFCDCGAGGVRGSSCQCLKPRKYNGNGSAPARGTNNFQSFLPLSEDADQLGESDSDVEEDGFGEENHVVLYIPKETQYKMSLLLEELGIEDRVLELFSSLLPSITSKRDSGLSKEKQVNLGKDKVLSFDTDLLQLKKAYKSGSLDLKIKADYTNSKDLKSLLANGSLVKSLLSVSVRGRLAVGEGDKVAIFDVGQLIGQATIAPINADKANVKPLSRNIVRFEIVHLSFNPVVENYLAVAGLEDCQILTLNHRGEVIDRLAVELALQGAFIRRIDWVPGSQVQLMVVTNKFVKIYDLSQDSISPTQYFTLPNDMIVDATLFVASRGRVFLLVLSEQGNLYRFELSWGGNAGATPLKEIVQIMGKDVTGKGSSVYFSPTYRLLFISYHDGSSFMGRLSSDATSLTDTSGMFEEESDCKQRVAGLHRWKELLAGSGLFICFSSVKSNAVLAVSLRGDGVCAQNLRHPTGSSSPMVGITAYKPLSKDNVHCLVLHDDGSLQIYSHVRSGVDTDSNFTAEKVKKLGSKILNNKTYAGAKPEFPLDFFERAFCITADVRLGSDAIRNGDSEGAKQSLASEDGFIESPSPVGFKISVSNPNPDIVMVGIRMHVGTTSASSIPSEVTIFQRSIKMDEGMRCWYDIPFTVAESLLADEDVVISVGPTTSGTALPRIDSLEVYGRAKDEFGWKEKMDAVLDMEARVLGHGLLLPGSSKKRALAQSASMEEQVIADGLKLLSIYYSVCRPRQEVVLSELKCKQLLETIFESDRETLLQTTACRVLQSVFPRKEIYYQVMFLPNSVKDTMRLLGVVKVTSILSSRLGILGTGGSIVEEFNAQMRAVSKVALTRKSNFSVFLEMNGSEVVDNLMQVLWGILESEPLDTPTMNNVVMSSVELIYSYAECLASQGKDTGVHSVAPAVQLLKALMLFPNESVQTSSRCVLVLAISSRLLQVPFPKQTMLTTDDLVDNVTTPSVPIRTAGGNTHVMIEEDSITSSVQYCCDGCSTVPILRRRWHCTVCPDFDLCEACYEVLDADRLPPPHTRDHPMTAIPIEVESLGADTNEIQFSADEVGISNMLPVVTSSIPQASTPSIHVLEPGESAEFSASLTDPISISASKRAVNSLILSEFLQELSGWMETVSGVQAIPVMQLFYRLSSAIGGAFMDSSKPEEISLDKLIKWLLGEINLSKPFAASTRSSLGEIVILVFMFFTLMLRSWHQPGSDGSSSKLGGSTDVHDRRIVQSSTVVATQSSLHVQERDDFASQLVRACSCLRNQEFVNYLMNILQQLVHVFKSRAANVEARGSSSGSGCGAMLTVRRDLPAGNYSPFFSDSYAKAHRADIFVDYHRLLLENVFRLVYTLVRPEKQEKMGEKEKVYRNASSKDLKLDGFQDVLCSYINNPHTAFVRRYARRLFLHLCGSKTQYYSVRDSWQFSNEVKNLYKHVEKSGGFENNVSYERSVKIVKSLSTIAEVAVARPRNWQKYCLRHGDFLSFLLNGVFHFAEESVIQTLKLLNLAFYQGKDVSSSVQKAEATEVVTGSNRSGSQSVDSKKKKKGEDGHDSGLEKLYVDMEGVVDIFSANCGDLLRQFIDFFLLEWNSSSVRTEAKSVIYGLWHHGRHSFKESLLAALLQKVRYLPAYGQNIVEYTELVSLLLDKAPENNSKQAINELVDRCLNPDVIRCFFETLHSQNELIANHPNSRIYSTLGNLVEFDGYYLESEPCVACSSPDVPYSKMKLESLKSETKFTDNRIIVKCTGSYTIQSVTMNVHDARKSKSVKVLNLYYNNRPVSDLSELKNNWSLWKRAKSCHLSFNQTELKVEFPIPITACNFMIELDSFYENLQALSLEPLQCPRCSRPVTDKHGICSNCHENAYQCRQCRNINYENLDSFLCNECGYSKYGRFEFNFMAKPSFIFDNMENDEDMKKGLAAIESESENAHKRYQQLLGFKKPLLKIVSSIGETEMDSQHKDTVQQMMASLPGPSCKINRKIALLGVLYGEKCKAAFDSVSKSVQTLQGLRRVLMSYLHQKNSNFSSGASRCVVSKTPNNCYGCATTFVTQCLEILQVLSKHPRSRKQLVAAGILSELFENNIHQGPKTARAQARAALSTFSEGDLSAVNELNNLVQKKIMYCLEHHRSMDIALATREEMLLLSEVCSLTDEFWESRLRLVFQLLFSSIKLGAKHPAISEHIILPCLKIISVACTPPKPDTAEKEQTMGKSAPAVQEKDENAAGVIKYSSESEENNLNVSQKTRDIQLVSYLEWEKGASYLDFVRRQYKASQSIRGASQKSRTHRSDFLALKYTLRWKRRSSRTSKGGLQAFELGSWVTELILSACSQSIRSEMCTLISLLAAQSSPRRYRLINLLIGLLPATLAAGESSAEYFELLFKMIETQDALLFLTVRGCLTTICKLISQEVGNIESLERSLQIDISQGFTLHKLLELLGKFLEVPNIRSRFMRDNLLSHVLEALIVIRGLIVQKTKLINDCNRRLKDLLDGLLLESSENKRQFIRACVSGLQTHAEENKGRTCLFILEQLCNLICPSKPEAVYMLILNKSHTQEEFIRGSMTKNPYSSAEIGPLMRDVKNKICQQLDLLGLLEDDYGMELLVAGNIISLDLSIAQVYELVWKKSNQSSTSLTNSALLASNAAPSRDCPPMTVTYRLQGLDGEATEPMIKELEEDREESQDPEIEFAIAGAVREYGGLEILLDMIKSLQDDFKSNQEEMVAVLDLLNHCCKIRENRRALLRLGALSLLLETARRAFSVDAMEPAEGILLIVESLTLEANESDSISAAQSALTVSNEETGTWEQAKKIVLMFLERLSHPSGLKKSNKQQRNTEMVARILPYLTYGEPAAMEALIEHFSPYLQNWSEFDQLQQRHEEDPKDDSIAQQAAKQRFTVENFVRVSESLKTSSCGERLKDIVLENGIIAVAVKHIKEIFAITGQTGFKSSKEWLLALKLPSVPLILSMLRGLSMGHLPTQTCIDEGGILTLLHALEGVSGENDIGARAENLLDTLADKEGKGDGFLGEKVRALRDATKDEMRRRALRKREELLQGLGMRQELSSDGGERIVVSQPILEGFEDVEEEEDGLACMVCREGYKLRPSDLLGVYSYSKRVNLGVGNSGSARGECVYTTVSYFNIIHFQCHQEAKRADAALKNPKKEWEGAMLRNNESLCNSLFPVKGPSVPLAQYLRYVDQYWDNLNALGRADGSRLRLLTYDIVLMLARFATGASFSADCRGGGRDSNSRFLPFMFQMARHLLDQGGPVQRTNMARSVSSYISSSSTSTATAPSSDSRPLTPGSQLSSTGTEETVQFMMVNSLLSESYESWLQHRRVFLQRGIYHTFMQHAHGRVASRAAEPTSSGGKTQDAETLTGDELLSIVKPMLVYTGMIEQLQQLFKPKKPVHIEPIKKEGTSSGVELEPWEIVMKEKLLNVKEMIGFSKELISWLDEINSATDLQEAFDIVGVLADVLSEGVTQCDQFVRSAIDKD | Required for auxin efflux and polar auxin transport (PAT) influencing auxin-mediated developmental responses (e.g. cell elongation, apical dominance, lateral root production, inflorescence architecture, general growth and development). Controls the elongation of the pedicels and stem internodes through auxin action. Involved in the expression modulation of light-regulated genes. Represses CAB1 and CAB3 genes expression in etiolated seedlings. Confers sensitivity to the auxin transport inhibitors N-1-naphthylphthalamic acid (NPA), 2-carboxyphenyl-3-phenylpropane-l,2-dione (CPD), and methyl-2-chloro-9-hydroxyfluorene-9-carboxylate (CFM). Influences the polarized subcellular distribution of the auxin transporter PIN1 in response to auxin transport inhibitors. Plays a role in the regulation of responses to phytohormones such as auxin, cytokinins, ethylene and gibberellic acid (GA), particularly during light-mediated stimuli (e.g. shade ovoidance, etiolation). Required for pericycle cell activation to form lateral root primordia (LRP) in both high and low phosphate P conditions. Necessary for the plant-growth promotion and lateral root development mediated by the fungus Trichoderma virens. Constitutively expressed in roots, rosette leaves, inflorescence stems, and flowers. Present in inflorescence meristems, floral meristems and vascular tissues. Altered expression of light-regulated genes; overexpression of CAB (photosystem II type I chlorophyll a/b-binding proteins) genes in the dark (e.g. CAB1 and CAB3). Reduced auxin transport. Under long-day growth conditions (18 hr light/6 hr dark), reduced apical dominance in mature plants. Reduced plant growth under both short-day (9 hr light/15 hr dark) and long-day conditions resulting in shorter plants. Strong deficiency in lateral root production. Reduced cell elongation in siliques, pedicels, roots, and the inflorescence leading to a compact rosette, more secondary corymb-like inflorescence, and small seeds. Delayed flowering. Reduced sensitivity to auxin transport inhibitors N-1-naphthylphthalamic acid (NPA), 2-carboxyphenyl-3-phenylpropane-l,2-dione (CPD), and methyl-2-chloro-9-hydroxyfluorene-9-carboxylate (CFM). Organ-specific defect in response to cytokinins, ethylene and gibberellic acid (GA). Increased expression of auxin transporters PIN1 and PIN6. Reduced growth-promotion and lateral root development stimulation mediated by the fungus T.virens. May be or regulate a N-1-naphthylphthalamic acid (NPA) binding protein (NBP), an auxin transport inhibitor. Belongs to the UBR4 family. |
Q6K4G1 | MSIMSSINECLATCKVLISPSMLPLHVLLSVEQVESTVVEIVERSLEFCLLYLEKSSYACEDYGLLNEVAYFMECVLLRGTPSKVYSLEPSVVNDVIEQWSSVQVDSERISPQEKYFCYLKGFNCSNSGDDLQRFRLTLSPECLQQDYVIAENTESSHTASPNGMVSIAQHFAVVHLHCIPVLLTLVQKLCQSPALDVIEDTNFNMRLSFGQRILKLVHGLAMEFPCDASDAMMLCSVARCTDSLPVLFKLKFKFANHDRVFSGDGVGTVLLQILDEFLQLIHIIFCNSDICCTVQVCILASLLEIFSPEKWKYDRSAACLMPPLVYSPHIVQYVLKLLNDTKRWTSRVDRDRPGKDVLGYSCNSETDGLSCHARSKKVPLLKKYTSEEYLQLIFPSEEQWLDDLVHLIFFLHEEGVKSMPLLEKPQMSCTKQVTLSELESVASHEEEALFGNLFAEARSTGVADSVEQPISLGSGPSSSQHGPIQLAADLICFMKMSIFSPEWCTAIYVDACRKFHSNHLEQFLSILQCPAFCSDESIATTSLSEVNSLHINTACFELLQMFLISHECPASLREDLVDKVFNAENGMYTYNNYTLALVARAIISGASSIYNLGRKVFVQENETASTWSKCIWTHKMGFTPVKTPACLAAYVVVSGNTSVMVAYEVKIQNEGDILLKEGQSRSMNDYLPSFTAEVVEGIFADTVKEYASTSSLFPQLIDVTPAHAEIYFDKSALEALGLNFANLGSNISEILGVWKGRKAEVAEDLIAERYLFLICWSTLSGIGYSGGYEGLLNPDFADVNFFISFALSVSDDASSLLDANLPSVIFGFLKLLQSEILCGPSVLESWDFLRKGAWLSLILSLINTGFWGHQTSGKPDVDLQGKQVVQDAEIFGKSLLTFISENSGHCLHVLSSLLETYLHAFKEAFISFVVEKGRVCEDHCYPSWLLKHSAFDKSKHPLLFEKVGSNIGMLEPICDLSSRIDRVATKLGDGRKEYFLLKCLLHGFPVNSASNNSAILSCVLVINEIIYMLNGCIKIMQPNDRDLVDVGVISKLLSMIMTIKSDGMFTSIHKLCDSIFMSLIDQKDDLAGYSDLFVLKQLEGYLADINSKEIMDNEVKEIIVFTIVDLVEDLRSKTNVFKFFLGEAEGAPERANSLFALEQADMSVFIDVLDKCQSEQVNLKILNLFTDILGDGLCPDLKQKLQHKFIGMDVSCFSSWLEFRTLGHSMKIESTNSTTSGPTALRELTMDFLMRLTCPSSETLAKELQHHLFDSMLLLLDKAFMSCDLQIVKAHFHFIAQLSTDESHFKELFEKTLKLMENMVGNEGLLHTLKFLFTCVESVFGDAGSNRSALKRLSSKSSGNSFGSGSLIPKQLKNSDSLVLRTNQESNSTVDCDASSGEEDEDDGTSDGELVSIDRDEEEDGNSERALATKVCTFTSSGSNFMEQHWYFCYTCDLTVSKGCCSVCAKVCHQGHRVVYSRSSRFFCDCGAGGVRGSSCQCLKPRKFTGTSSVSPPVTSSFQPILPYHEDVEPVADSGSDFEDDISTEAENCIKLSVPKGFSDELPVFLKNLDVEVRMLELCKKLLPMILSQRELNLLKDRKVFLGGEMPMSQASDIFQLKKAFKSGSLDLKIKADYPNSRELKSHLANGSLTKSLLSISIRGKLAVGEGDKVAIFDVGQIIGQPTAAPITADKTNVKPLSRNIVRFEIVHLIFNPLVEHYLSVAGYEDCQVLTLNSRGEVTDRLAIELALQGAYIRCVEWVPGSQVQLMVVTNKFVKIYDLSQDNISPLHYFTVADDIIVDATLVPSSMGKLVLLVLSEGGLLYRLNVALAGDVGAKTLTDTVLVKDAVSMHKGLSLYFSSTYRLLFVSHQDGTTYMGRLDGDSSSITELSYICENDQDGKSKPAGLYRWRELIAGSGALACLSKFKSNSPLAVSLGPHELFAHNMRHASGSNAPVVGIAAYKPLSKDKAHCLLLYDDGSLNIYSHTPNGSDSSTTLTAEQTKKLGSSILSSRAYAGTKPEFPLDFFEKTTCITCDVKFNSDTTKSSDSESIKQRLSSDDGYLESLTSAGFKVTISNPNPDIVMVGCRIHVGNTSASNIPSEITIFHRVIKLDEGMRSWYDIPFTTAESLLADEEFTIVVGRTFDGSSIPRIDSIEVYGRAKDEFGWKEKMDAALDMEAHVLGGSSASGKSGKKAQTMQAAPIQEQVLADALRILSRIYLLCQPGFCTDTIDADMELNNLKCRSLLETIFQSDREPLLHSAACRVLQAVFPKKEIYYHVKDTMRLLGVIKSLPSITSRIGVGGAASSWVTKEFIAQIHTVSKVAVHRKSNLASFLETHGTELVDGLMQVFWGILDLDRPDTQRINSLVVPCVEFIYSYAECLALHSNEKSGVSVAPAVALLKKLLFAPYEAVQTSSSLAISSRFLQVPFPKQTMIANDDAPDNHAKASAASNSTTGNAQVMIEEDPATSSVQYCCDGCSTVPILRRRWHCNICPDFDLCETCYEILDADRLPAPHSRDHPMSAIPIELDTFGGEGNEIHFSVDELTDSSVLQAPADRTIQTSPSSIHVLDASESVDFHGSMTEQRTVSISASKRAINSLLLSRLIEELSGWMETTAGTRAIPIMQLFYRLSSAVGGPFMDSTKPENLDLEKFVKWLIDEINISKPFPAKTRCSFGEVSILVFMFFTLMFRNWHQPGTDGSHSKSGGSSDLTEKGPVHVQVSTTTLQSSNDDHDKNEFASQLIRACSALRQQSFLNYLMDILQQLVHVFKSSSINGEGGSSSSGCGSLLTVRRELPAGNFSPFFSDSYAKSHPTDLFMDYYKLLLENTFRLVYSMVRPEKEKSADKDKSCKVPNTKDLKLDGYQDVLCSYISNAHTTFVRRYARRLFLHLCGSKTHYYSVRDSWQYSHEVKKLHKIINKSGGFRNPVPYERSVKLIKCLSTLCDVAASRPRNWQKFCLKHTDLLPFLMDNFYYFSEECIVQTLKLLNLAFYSGKDANHNAQKTESGDIGSSTRTGSQSSDSKKKRKGDDSSEGSSEKSCMDMEQAVVVFTGKDGDVLKRFVDTFLLEWNSTSVRHEAKSVLFGLWYHAKSSFKENMLTTLLQKVKYLPMYGQNIIEYTDLMTCLLGKANDSTAKQSDTELLNKCLTSDVVSCIFDTLHSQNELLANHPNSRIYNTLSCLVEFDGYYLESEPCVTCSCPDVPYSRMKLESLKSETKFTDNRIIVKCTGSFTIQSVTMNVYDARKSKSVKVLNLYYNNRPVTDLSELKNNWSLWKRAKSCHLTFNQTELKVEFPIPITACNFMIELDSFYENLQASSLESLQCPRCSRSVTDKHGICSNCHENAYQCRQCRNINYENLDSFLCNECGYSKYGRFEFHFMAKPSFSFDNMENDDDMRKGLTAIESESENAHRRYQQLMGFKKPLIKLVSSIGEQEIDSQQKDAVQQMMVSLPGPTGKVNRKIALLGVLYGEKCKAAFDSVSKSVQTLQGLRRVLMTYLHQKNSNDTDALPACSIPRSPSSCYGCSTTFVTQCLELLQVLSKHATSRKQLVSAGILSELFENNIHQGPRTARTLARAVLSSFSEGDADAVQELNNLIQKKVMYCLEHHRSMDISQSTREELLLLSETCALVDEFWEARLRVAFQLLFSSIKVGAKHPAISEHIILPCLRIISQACTPPKSDSGEKEPGMGKSSLMQAKNDDTVGHSVTNLSTSKTQSELSGKIPDGSRRRQDISLLSYSEWESGASYLDFVRRQYKVSQAVKGLQKTRHDSQKSDYLVLKYGLRWKRRACRKSSKGDFSKFALGSWVSDLILSSCSQSIRSEICTLISLLCPSNSSRQFQLLNLLMSLLPRTLSAGESAAEYFELLGTMIDTEASRLFLTVRGCLTTLCSLITKEVSNVESQERSLSIDISQGFILHKLVELLNKFLEIPNIRARFMSDNLLSDVLEAFLVIRGLVVQKTKLINDCNRLLKDLLDSLLVESTANKRQFIRACISGLQKHVKEKKRRTSLFILEQLCNLICPVKPEPVYLLILNKAHTQEEFIRGSMTRNPYSSAEIGPLMRDVKNKICHQLDLIGLLEDDYGMELLVAGNIISLDLSISQVYEQVWRKHHGQTQHSLSNASQLSAAASSVRDCPPMTVTYRLQGLDGEATEPMIKELEDEREESQDPEVEFAIAGAVRECGGLEIILSMIQSLREDELRSNQEELGSVLNLLKYCCKIRENRCALLRLGALGLLLETARRAFSVDAMEPAEGILLIVESLTMEANESDISIAQSVFTTTTEETGAGEEAKKIVLMFLERLCPPDGAKKSNKQQRNEEMVARILPNLTYGEPAAMEALVLHFEPYLMNWSEFDQLQKQHEENPKDETLSKNASMQRSAVENFVRVSESLKTSSCGERLKEIILEKGITKAAVGHLRESFASAGQASFRTSAEWTVGLKLPSIPLILSMLKGLAKGDLPTQKCVDEEDILPLLHALEGVPGENEIGARAENLLDTLANKENNGDGFLAEKIQELRHATRDEMRRRALKKREMLLQGLGMRQEFASDGGRRIVVSQPIIEGLDDVEEEEDGLACMVCREGYTLRPTDMLGVYAFSKRVNLGATSSGSGRGDCVYTTVSHFNIIHYQCHQEAKRADAALKNPKKEWDGATLRNNETLCNCIFPLRGPSVPPGQYTRCLDQYWDQLNSLGRADGSRLRLLTYDIVLMLARFATGASFSTDCKGGGRESNSRFLPFMIQMASHLVDGSANQQRHVMAKAVTSYLSSSPSTPESPVRLSALSGARGGSGSSEETVQFMMVNSLLSESYESWLQHRPAFLQRGIYHAYMQHKHGRSTLKLSADTSSSAVRSDEGSSADSNDSKRLFAIVQPMLVYTGLIEQLQQFFKKGKSSGTQKVGEKDGSSGGNLEAWEIMMKEKLGNMKEMLGFSKDVLSWLEDMTSSEDLQEAFDVMGALPDVFSGGHTTCEDFVRAIIHGAKS | Required for auxin efflux and polar auxin transport (PAT) influencing auxin-mediated developmental responses (e.g. cell elongation, apical dominance, lateral root production, inflorescence architecture, general growth and development) (By similarity). Belongs to the UBR4 family. |
O48814 | MGSCFSSRVKADIFHNGKSSDLYGLSLSSRKSSSTVAAAQKTEGEILSSTPVKSFTFNELKLATRNFRPDSVIGEGGFGCVFKGWLDESTLTPTKPGTGLVIAVKKLNQEGFQGHREWLTEINYLGQLSHPNLVKLIGYCLEDEHRLLVYEFMQKGSLENHLFRRGAYFKPLPWFLRVNVALDAAKGLAFLHSDPVKVIYRDIKASNILLDADYNAKLSDFGLARDGPMGDLSYVSTRVMGTYGYAAPEYMSSGHLNARSDVYSFGVLLLEILSGKRALDHNRPAKEENLVDWARPYLTSKRKVLLIVDNRLDTQYLPEEAVRMASVAVQCLSFEPKSRPTMDQVVRALQQLQDNLGKPSQTNPVKDTKKLGFKTGTTKSSEKRFTQKPFGRHLV | Plays a central role in immune responses (PubMed:20413097, PubMed:29649442). Required to activate the resistance responses to necrotrophic pathogens, including the regulation of defense hormone expression (e.g. jasmonic acid (JA) and salicylic acid (SA)) (PubMed:16339855, PubMed:29649442). Phosphorylates FLS2 and BAK1 (PubMed:20404519, PubMed:24104392). Involved in pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) signaling, including calcium signaling, and defense responses downstream of FLS2; upon PAMP recognition, first phosphorylated by FLS2 and SIK1 prior to being monoubiquitinated by ATL44/RHA3A and ATL45/RHA3B at the plasma membrane, then internalized dynamically into endocytic compartments together with FLS2 (PubMed:20413097, PubMed:25522736, Ref.20, PubMed:30212650). Acts additively with PBL1 in PTI defenses (PubMed:20413097). Acts as positive regulator of the PAMP flg22-induced increase of cytosolic calcium. Binds directly and phosphorylates the NADPH oxidase RBOHD at specific sites in a calcium-independent manner to enhance reactive oxygen species (ROS) generation upon flg22 perception. ROS production in response to flg22 controls stomatal movement and restriction of bacterial entry into leaf tissues (PubMed:24629339). Seems not required for flg22-induced MAPK activation (Probable). Required for Pep1-induced defenses. Pep1 is an endogenous elicitor that potentiates PAMP-inducible plant responses. In association with PEPR1, acts downstream of the canonical ethylene signaling cascade to regulate ethylene responses (PubMed:23431184). Involved in ethylene signaling. Destabilizes EIN3, the key transcription activator in ethylene signaling, and represses EIN3-dependent transcription (PubMed:26021844). Acts as a negative regulator in brassinosteroid (BR) signaling. Functions in BR signaling by direct interaction with the BR receptor BRI1 cytosolic kinase domain (PubMed:23818580). (Microbial infection) Xanthomonas campestris effector AvrAC/XopAC-mediated uridylylation prevents activation by phosphorylation at the same residues, thus affecting immune responses and reducing defense responses toward X.campestris, mediating avrAC/XopAC virulence functions. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Kinase activation is repressed by the phosphatase PP2C38. Interacts with FLS2 (PubMed:20413097, PubMed:20404519). Activation of FLS2 by flagellin (flg22) induces the dissociation of the complex (PubMed:20413097, Ref.20). Interacts with BAK1 (PubMed:20404519). Interacts with the Xanthomonas campestris effector XopAC/AvrAC (PubMed:22504181). Interacts with CPK28 (PubMed:25525792). Interacts with PEPR1 (PubMed:23431184). Interacts with PP2C38 (PubMed:27494702). Interacts with BRI1 (PubMed:23818580). Interacts with RBOHD (PubMed:24629339). Binds to EFR when not phosphorylated at Ser-89 and Thr-90, in the absence of pathogen elicitor; dissociates upon pathogen-associated molecular pattern (PAMP)-triggered activation by EFR-mediated phosphorylation (PubMed:29649442). Interacts directly with and phosphorylates WRKY transcription factors in the nucleus involved in the jasmonic acid (JA) and salicylic acid (SA) regulation (e.g. WRKY33, WRKY50, WRKY51 and WRKY57) to modulate defense hormones during plant immunity (PubMed:29649442). Binds to ATL44/RHA3A and ATL45/RHA3B (Ref.20). Binds to SIK1 to be phosphorylated and stabilized (PubMed:30212650). Linked to the plasma membrane when inactivated, but moves to the nucleus upon pathogen-mediated activation by phosphorylation (PubMed:29649442). Internalized dynamically into endocytic compartments upon the recognition of microbe-associated molecular patterns (MAMPs, e.g. flg22), when monoubiquitinated after phosphorylation and subsequent dissociation of the FLS2/BIK1 complex (Ref.20). By infection with necrotrophic pathogens and by paraquat. Not induced by salicylic acid, jasmonate or 1-aminocyclopropane-1-carboxylate (ACC) (PubMed:16339855). Induced by flagellin (flg22) (PubMed:20413097). Phosphorylated by SIK1 to be stabilized (PubMed:30212650). Phosphorylated by FLS2 and BAK1 (PubMed:20404519, Ref.20). Autophosphorylated (PubMed:22504181, PubMed:23431184, PubMed:24104392, PubMed:26021844). Autophosphorylation is reduced in presence of the Xanthomonas campestris effector XopAC/AvrAC (PubMed:22504181, Ref.20). Phosphorylated, especially by EFR at Ser-89 and Thr-90, in response to the microbe-associated molecular pattern (MAMP) flg22 (PubMed:20413097, PubMed:22504181, PubMed:25522736, PubMed:29649442, Ref.20). Phosphorylation in response to flg22 is abolished in presence of the Xanthomonas campestris effector XopAC/AvrAC (PubMed:22504181). Phosphorylated at Ser-233, Ser-236 and THR-237 by PEPR1 (PubMed:23431184). Phosphorylated at Tyr-150, Tyr-243 and Tyr-250. Tyrosine phosphorylation is required for BIK1 function in plant innate immunity (PubMed:24532660). Uridylylated at Ser-236 and Thr-237 by the Xanthomonas campestris effector XopAC/AvrAC. This conceals conserved phosphorylation sites in the activation loop, reducing BIK1 kinase activity and consequently inhibiting downstream signaling. Monoubiquitinated by ATL44/RHA3A and ATL45/RHA3B following phosphorylation upon the recognition of microbe-associated molecular patterns (MAMPs, e.g. flg22) by pattern recognition receptors (PRRs), then released from the FLS2/BAK1 complex and internalized dynamically into endocytic compartments followed by the activation of immune signaling. Altered growth traits, early flowering, weak stems, small siliques and reduced fertility. Mutant plants have a severely impaired resistance to Botrytis and A.brassicicola (PubMed:16339855). Reduced plant size (PubMed:20413097, PubMed:27679580). Enhanced resistance to Plasmodiophora brassicae, a soil-borne obligate pathogen that causes clubroot disease (PubMed:27679580). Hypersensitivity to the plant hormone brassinolide (PubMed:23818580). Reduced calcium levels after elicitation with peptides representing bacteria-derived microbe- and damage-associated molecular patterns (MAMPs, flg22 and elf18, and the endogenous DAMP AtPep1) (PubMed:25522736). The association with FLS2 and BAK1 is reduced after flagellin perception, BIK1 being probably released from the receptor complex upon phosphorylation. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. |
S0DZM7 | MASSADVYVFGDQSTPVLDKLQALVRVKDNALLTSFLGEAFLAVRREIVSLSSLERKSIPEAESLSLLLEGVRRSEPHAALDSAFVCIYEIGYYIDYLARSDKQHPPAAPSLLLGICTGSIAAAAVSCAKDVFEISRLGVEAATVAFRLGMHVRRRAENLGYSTPSSWSMILSSNQEELVSEALKEFSKEKNLTYSSRPYISATGPGFTTISGPPSILESVKSCDTFSGKRLYPAPIYGPYHNSSSYSESSLEHGLASILEDVGFLENEMLIPIISCASGSRLDQLSFGNLLKNVLSSALSQQIRMDLVTDALVETVSGTEATLIPVNAQTTVCSLADWLAKRGATTRIGPTLESLTKDRAEPNLAPGDENKIAIIGFSGRFPEADNLDEFWDLLIRGLDVHKPVPEERFARDHYDPTGQRKNTSQVQYGCWLKSAGYFDTQFFHMSPKEAMQTDPAQRLALLTAYEALEMAGVVPDRTPSTQRNRVGVYYGTTSNDWGEVNSSQDVDTYYIPGANRAFIPGRVNYFFKFTGPSIAVDTACSSSLAAINLAITSLKNRDCDTAIAGGTNVMTNPDNFAGLDRGHFLSRTGNCKAFDDGADGYCRADGIGTLILKRLPDAIADSDPIFGVILGAHTNHSAESVSITRPLADAQEYLFKKLLNETGIHPHDVSYVEMHGTGTQAGDAVEMRSVLNSFAFDHSRPRDKSLYLGSVKANVGHAESASGVLAIIKVLLMMQKNTIPPHCGIKTKINQGFPKDLDHRGVRIALKDSVDWSRPEGGKRRVLVNNFSAAGGNTSLLLEDGPAVHPARQHQDGDARTEHVVAVSARSTKALEENLKALEAYIANSWAPEGELLSQLSYTTTARRVHHSRRVAFVTNGLDDLRKSLLKAATDAGQVKGIPAVSPKVGFLFTGQGAQETAMAIGYYKSFSSFRSDIHQLDSIATLQGLPSVLPLIHGTTPVEDLSAVVVQLGTCIIQISLARFWISLGITPQYVIGHSLGEYAALQIAGVLSVNDAIFLCGHRAALLDKKCTAYTHGMVAVKAAADDLRQHISSDLKVEIACVNGAEDTVLSGPNADIESLCGKLTQAGYKLHKLEIPFAFHSSQVDPILDDLEELASQVGFHEPKLPIVSPLLRTLLTGDTLGPQYIRRHCRETVDFLGAIKMAESQGIMDRSGMCIEIGAHPILTRMVKSIIGQDFRCLASLRRKEDHFKTLADSLCALHLAGFSVNWDEYHRDFASSRNVLQLPKYSWQLANYWMQYKYSWCLTKGDAPVENGPVGAVVQARALRLSDSVHNVIEQVHGDKRSSITVESDMHDPSLLAIAQNHRVNGLTMAPSTLFADIAFTLAKHLIQNHGLDTHTNLPSINNMAVEKALIVGETGPQLFRASLDMDWTTMRGSVRIFSVGANGKQTTLHAVCDVAVENPSSHRESWQSNAYLIQRGIKQLVQGASDGSAHMMRRGLLYKIFSNSVQYGSAFQGIEQVWFDSEGLEGTGKVFMPSGKDTFALNPYCCDSLGHITGFIMNCSDSLDLDDHVYINHGWRTLRLVEPYQCDVQYQTYVKMQAVGSDDSTYSGDVHVLRDGKIIGICGGVTFKKVARKVLEMLLPKPSGAKAKHGVVKHVAPEPVKHVVLTPPSTTSHSVGTTSPPEPTESPVGSASGLIQKALEIIADEIGVDISQLTDTTLLADLGVDSLMSLTILGNFREELDLDIPAAQFYEFSTVQDLKSFLGANDQDFSSSNSEAESSASSAASTSPSDHGDDVVEEVKPVVAEIPRSTSTILQGTKHCSQTLFLFPDGAGSATSYVTLPSISSDMRVIGLNSPYLTKPHEFNCALQDITGSYLNEVRRRQPQGPYHLAGWSAGGVSAFDAARQLVSEGEVVESLILIDSPNPVGLGKLPKRMYDFLEKSGIFGAFEMGEEAQAPPDWLFQHFCVFIEALDRYVPEPFEHGMAPKTTIIWAADGVCKNPDDPRPEAQPDDPRGMNWLLNNREDFGPNGWDEFIGAGNISTMAIENANHFTMMREPIASALCAKIRETMGVN | Polyketide synthase; part of the gene cluster that mediates the biosynthesis of bikaverin, a red pigment also considered as a mycotoxin (PubMed:12409099, PubMed:17696354, PubMed:19400779). The first stage is catalyzed by the polyketide synthase bik1, which catalyzes the formation of the intermediate SMA76a also knowm as pre-bikaverin (PubMed:12409099, PubMed:17696354, PubMed:19400779). FAD-dependent monooxygenase bik2 might then be responsible for the oxidation of pre-bikaverin to oxo-pre-bikaverin which is in turn methylated by the O-methyltransferase bik3 to me-oxo-pre-bikaverin (PubMed:26382642). A further cycle of oxydation and methylation by bik2 and bik3 leads to the final product of bikaverin, via a nor-bikaverin intermediate (PubMed:19400779, PubMed:26382642). Secondary metabolite biosynthesis. Expression is repressed during the growth phase, but is induced as the growth rate decreases due to nitrogen depletion of the culture medium (PubMed:12409099). Highly expressed only under acidic culture conditions (PubMed:12409099, PubMed:19400779). Also induced by salt starvation (PubMed:19838698). Expression is repressed by regulatory gene, areA, a transcriptional regulator responsible for the activation of nitrogen assimilation genes (PubMed:12409099). Expression is also negatively regulated by vel1 (PubMed:20572938). Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide back- bone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm (By similarity). Impairs the production of bikaverin and its intermediate oxo-pre-bikaverin (PubMed:12409099, PubMed:19400779, PubMed:26382642). |
D6VQY6 | MDRYQRKIGCFIQIPNLGRGQLKYVGPVDTKAGMFAGVDLLANIGKNDGSFMGKKYFQTEYPQSGLFIQLQKVASLIEKASISQTSRRTTMEPLSIPKNRSIVRLTNQFSPMDDPKSPTPMRSFRITSRHSGNQQSMDQEASDHHQQQEFGYDNREDRMEVDSILSSDRKANHNTTSDWKPDNGHMNDLNSSEVTIELREAQLTIEKLQRKQLHYKRLLDDQRMVLEEVQPTFDRYEATIQEREKEIDHLKQQLELERRQQAKQKQFFDAENEQLLAVVSQLHEEIKENEERNLSHNQPTGANEDVELLKKQLEQLRNIEDQFELHKTKWAKEREQLKMHNDSLSKEYQNLSKELFLTKPQDSSSEEVASLTKKLEEANEKIKQLEQAQAQTAVESLPIFDPPAPVDTTAGRQQWCEHCDTMGHNTAECPHHNPDNQQFF | Required for nuclear fusion, chromosome disjunction, and nuclear segregation during mitosis. Probably required for the formation or stabilization of microtubules during mitosis and for spindle pole body fusion during conjugation. And mitotic spindle. Present with 300 molecules/cell in log phase SD medium. |
S0E2X6 | MAEPNQHYEVIIAGGGIAGVTLALMFEKLDISYFLLEGRDTLESDRGAGIGLQPNGLRILDQLGLVEDIEEATIPLEKWFSYDSEGNLMNDSDAMGQYRDKIGYPVAFIERRKLLPIMVRHIQRTECVKTSARVASIEESEDHVTVTTTDGLSLTADIVVGADGVRSAVRTHIDSKLPEPLTADDYISVACSTVYGMSAPTEGIAPGERFAVYRENQTVIGFTGKDGIVFWFVFENLNRNVPLSQAPRYTEAEAEALCLSVAHTQVTPKLKFGEIYKNSVVAVKIGVEEGVAKGWHTDRAVIVGDAACKTTPAGGQGANQAIESCAVFVNKLMAARKASQSGDKLSSDVVKSVLASYAQERAQPATTALERSQMVGKALLCTPGPATTLVKDMLKLSNEDWLLRAFMALSAAPYLEDVELTARGHLYNKAVEEARAEMARRQRVAKEVKEAEEKESKQAASIKESEQRNEFVGLRNPVQAATGVVEVGS | FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of bikaverin, a red pigment also considered as a mycotoxin (PubMed:19400779). The first stage is catalyzed by the polyketide synthase bik1, which catalyzes the formation of the intermediate SMA76a also knowm as pre-bikaverin (PubMed:19400779). FAD-dependent monooxygenase bik2 might then be responsible for the oxidation of pre-bikaverin to oxo-pre-bikaverin which is in turn methylated by the O-methyltransferase bik3 to me-oxo-pre-bikaverin (PubMed:26382642). A further cycle of oxydation and methylation by bik2 and bik3 leads to the final product of bikaverin, via a nor-bikaverin intermediate (PubMed:19400779, PubMed:26382642). Secondary metabolite biosynthesis. Expression is repressed by glutamine and at alkaline ambient pH and highly induced under nitrogen starvation and acidic pH conditions (PubMed:19400779). Expression is also negatively regulated by vel1 (PubMed:20572938). Impairs the production of bikaverin (PubMed:19400779). Leads to the accumulation of the intermediate pre-bikaverin (PubMed:26382642). Belongs to the paxM FAD-dependent monooxygenase family. |
S0E608 | MVSNGISNGTNGTNGTTTNGTNGVNGHAALSPLEVLVQDLNKNTTTLNGYLRANKLPEPSFERDAPIINLSPDAPEEAQVAKEKVLDSALQIFQLVSGPGEYLQNVITGYHYMEILRWMSHFKIFELVPLEGKISYTELASKAGVAELRLKTLARMGMTNHLFAEPEPGFIAHSATSAALVTNNRFSDQRVWMTSIIAPVIASMVTAHERWPDSTAPNKAAFNAAFNTDLRMYEYISKQPDVYKLFGRVMDAIATSPKSDLKHLVSGFDWAGLGKANVVDIGGNIGHSCVKLAEAFPDLNFIIQDIPHVVEEGAKVIKENNEASIANRIQFQEYDFFQKQPVVGADIYLLRQIFHNWDFENSVKILKNTVESMGQNSHVLIMDFVVPEPGTVSSVNERVLRSRDVGMMQLFNSLERDLEGWKAILEAVDSRLKINAVNTPYGSFMSVIDVVLG | O-methyltransferase; part of the gene cluster that mediates the biosynthesis of bikaverin, a red pigment also considered as a mycotoxin (PubMed:19400779). The first stage is catalyzed by the polyketide synthase bik1, which catalyzes the formation of the intermediate SMA76a also knowm as pre-bikaverin (PubMed:19400779). FAD-dependent monooxygenase bik2 might then be responsible for the oxidation of pre-bikaverin to oxo-pre-bikaverin which is in turn methylated by the O-methyltransferase bik3 to me-oxo-pre-bikaverin (PubMed:26382642). A further cycle of oxydation and methylation by bik2 and bik3 leads to the final product of bikaverin, via a nor-bikaverin intermediate (PubMed:19400779, PubMed:26382642). Secondary metabolite biosynthesis. Expression is repressed by glutamine and at alkaline ambient pH and highly induced under nitrogen starvation and acidic pH conditions (PubMed:19400779). Impairs the production of bikaverin (PubMed:19400779). Leads to the accumulation of the intermediate oxo-pre-bikaverin (PubMed:26382642). Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily. |
S0DZI6 | MPSPHFSKVLVFGATGEVGSAVALEAHALGAHVSIALRDTTKHNEWISPSQEHAADLQRISADLTDPDSLKRAVHDTGAQAAFIYAVRSKDTLRGAITALRDAGIQYLVFLSTSQVRTAGTTKGDIRSIKPDHFIPWQHAQVEIALEELEVPHAAVRAGFFASNPLRIYLDRSSEPKQVNLLAPEVPHDPIDPKDIGRAAAAVLVNPRLYASGYQGEPKKDVVYLSGPALLSQTEQWEIINRELVAAGKPEVKVNHITVEQYLENLAKLHVPDVVAKSLAKSMVETRALYAPEDYEKSRGNVELLTGRKATAFDEFVKREIPRYFD | Nitrogen metabolite regulation-like protein involved in the regulation of the gene cluster that mediates the biosynthesis of bikaverin, a red pigment also considered as a mycotoxin (PubMed:19400779). Expression is repressed at alkaline ambient pH and highly induced under nitrogen starvation and acidic pH conditions (PubMed:19400779). Leads to decreased production of bikaverin (PubMed:19400779). Belongs to the NmrA-type oxidoreductase family. |
S0E028 | MDSALGNLSMPGLAQSHVQVRTCIHCRQRRVKCDRQFPQCSNCIRSEVNCIYPPGRGRAPKRPKRSLAPQLSERLSRLESIIGQFGAAARENQDTPQTAQDSEGHSFEQDFSRLKVDESKSYYVNNALWVEELRDLLFEPASEDAGYEPSISSSATTAATSPSSPQLGLNAAIFGYRAIASPLYHYHPSLQQAVTLFAAFSENVAPLVRIFHMPTLTRIYWDAIASLGTVDKHTETLLFTIHYSAVISLNPEQCLNILDETREAALERYRFAVEQALAQGNLLSTQSMTMLQAAVLFLSALPNEDDSRAAWALTSLVFHIARTMGLHRDGTIFGLKPFETELRRRLWWQICIIDSRSSEYHCNEPIAQGFITDTKPPLHINDVDLSPEMVEPPAERWDHATDMTLTLVRCEAIQTGLKLGRMRHKQNKTSEDGSTPRVDDTSDTPKTLIQELESRLRDKYLPICDTSVPFQLLSSAVAQIILGRFWLITQYSVVSREREVDGKSTSNQFPPTPNTAGQLDNKVRDELFQTSIKILEVSGMLLTSKEIIQFTWYSKTHIQWGAMAFVLSELCARPQSAQCDQAWDCVTTVYEGWKVDESKQDETRLALWRPIKRLMAKARYVKEMQQTTPGRSSNAGRKVQRRDPVLYSPSPGLFSQYPTPAYSNNWYGPLQQTPPSIPGSEASLPGMATVPLDSSGQSDALQRVLGTETLGPFMDMIPEWPWVDAEHGASSLAGFDLGLPRFN | Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of bikaverin, a red pigment also considered as a mycotoxin (PubMed:19400779). Expression is repressed by glutamine and at alkaline ambient pH and highly induced under nitrogen starvation and acidic pH conditions (PubMed:19400779). Leads to decreased production of bikaverin (PubMed:19400779). |
S0DZN4 | MNEESNMGGVFKEEEAQSGDVVDFEGDSDTHNPQNWPMGKKVYTTALWALTTCWITFASAIYSAGTAEISEEFHVSYEVANAGTSLLIFGFALGPMLWAPLCEVYGRKWPALAPYFISAAFAFGTATAKDIQTILITRFFAGVFGSSPISITGGSIVDIWTPRQRGTPMVCYGITIAAAPTLGPIIGGAFIASGCGWRWTEYLTGIVMMVQFVLDALWLDESHADVLLTRKASRLRRSTGNFSLHAKWEETSPTFKSLLSTYLVRPFQMLLDPICLLLTIYTSFVYAILYASLESFALEYGRFRRWGPVVSQLPFLSLLIGCLFAAAANIFNNIYYGKKLVANNFKPVPEARLPPMMVGGFAFSAGLFLFGWTSVEHVSSPWPSIIGVFLTGVGFTTIFQSSLQYLVDTFTRYSASAIAANTFVRSMAAGAFPLFVWPMYEKIGIDWGSTIFACISVLLLPAPFLFFKWGYRIRARGEFSKLSTY | Efflux pump; part of the gene cluster that mediates the biosynthesis of bikaverin, a red pigment also considered as a mycotoxin (PubMed:19400779). Expression is repressed by glutamine and at alkaline ambient pH and highly induced under nitrogen starvation and acidic pH conditions (PubMed:19400779). Leads to decreased production of bikaverin (PubMed:19400779). Belongs to the major facilitator superfamily. |
Q5SHZ8 | MSLDLRARVREELERLKREGLYISPKVLEAPQEPVTRVEGREVVNLASNNYLGFANHPYLKEKARQYLEKWGAGSGAVRTIAGTFTYHVELEEALARFKGTESALVLQSGFTANQGVLGALLKEGDVVFSDELNHASIIDGLRLTKATRLVFRHADVAHLEELLKAHDTDGLKLIVTDGVFSMDGDIAPLDKIVPLAKKYKAVVYVDDAHGSGVLGEKGKGTVHHFGFHQDPDVVQVATLSKAWAGIGGYAAGARELKDLLINKARPFLFSTSHPPAVVGALLGALELIEKEPERVERLWENTRYFKRELARLGYDTLGSQTPITPVLFGEAPLAFEASRLLLEEGVFAVGIGFPTVPRGKARIRNIVTAAHTKEMLDKALEAYEKVGKRLGIIR | Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide (By similarity). Can also use pimeloyl-CoA instead of pimeloyl-ACP as substrate. It also converts 2-amino-3-ketobutyrate and CoA to glycine and acetyl-CoA. Activity is also observed with the following combinations of substrates: acetyl-CoA and either L-alanine or L-serine, pimeloyl-CoA and either glycine or L-serine, and palmitoyl-CoA with L-alanine. 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP] acetyl-CoA + glycine = (2S)-2-amino-3-oxobutanoate + CoA Optimum pH is 6.0. Stable at pH 4.5-5.0, and a loss of less than 10% of the initial activity is observed after 1 hour of incubation at these pH. Optimum temperature is 70 degrees Celsius. Stable at temperatures up to 70 degrees Celsius, with a loss of less than 10% of the initial activity observed after 1 hour of incubation at these temperatures. The enzyme shows a half-life of 1 hour at 80 degrees Celsius. Cofactor biosynthesis; biotin biosynthesis. Homodimer. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. |
Q6FH93 | MSEVRPLSRDILMETLLYEQLLEPPTMEVLGMTDSEEDLDPMEDFDSLECMEGSDALALRLACIGDEMDVSLRAPRLAQLSEVAMHSLGLAFIYDQTEDIRDVLRSFMDGFTTLKENIMRFWRSPNPGSWVSCEQVLLALLLLLALLLPLLSGGLHLLLK | Accelerates programmed cell death. Association to the apoptosis repressors Bcl-X(L), BHRF1, Bcl-2 or its adenovirus homolog E1B 19k protein suppresses this death-promoting activity. Does not interact with BAX. Interacts with RHBDL4/RHBDD1 (PubMed:18953687). Interacts with BCL2L10/BCL-B (PubMed:23235460, PubMed:23563182). Around the nuclear envelope, and in cytoplasmic membranes. Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family. Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage is a necessary step prior its degradation by the proteosome-dependent mechanism. |
O70337 | MSEARLMARDVIKTVPHDQVPQPPVASETPSMKEPVRDVDLMECVEGRNQVALRLACIGDEMDLCLRSPRLVQLPGIAIHRLAVTYSRTGVRGIFRSLIRSLTNLRENIWSWRVLTPGAWVSPDQDPGQLFPMVLLVFLLLGGAWYLQLQ | Accelerates programmed cell death. Binding to the apoptosis repressors Bcl-X(L), BHRF1 or Bcl-2 suppresses this death-promoting activity. Interacts with RHBDL4/RHBDD1 (By similarity). Interacts with BCL2L10/BCL-B (By similarity). Around the nuclear envelope, and in cytoplasmic membranes. Expressed in testis, kidney, liver, lung and heart. Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family. Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage is a necessary step prior its degradation by the proteosome-dependent mechanism (By similarity). |
Q3B169 | MGVPPLHPEISAAYSVLETGEPIGREAALMLAALPGEHALDIASLANKVRNRWGKGGVHACSIMNAKSGVCGENCRFCAQSRHNHSDIEVYPLVDEDAVLFEARGCVEQGVSHFGIVTSGYGYLKMSDEFQRILSMIDRLHSELPSLQVCASLGVLGPDTAKALAGRGIAHYNINIQVTPGRYGELIADTHAVEERMETVRLLRRNGVSVCCGGIIGVGEHMEDRVEMMFALRELDVSVIPINVLVPIKGTPLEGAPSLPLDEIVKTFAIMRLVHPRKTIKFAAGRETVMKDFQGLLMLSGADGLLTGGYLTTRGREVADDTRFRAQLASFS | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine. Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2. Homodimer. Belongs to the radical SAM superfamily. Biotin synthase family. |
B3QLR7 | MSSRLHPDIERAYRVLETGEPVSLELASALGRLPESEVLDLVSLANKVKNLYAPGEGGGVHACSIMNAKSGVCGENCRFCAQSKHNSAEVDVYGLVDEAKVLDQARALHEQGVGHFGIVTSGYGYRKVTPEFERILGMIDLLHRELPDLKVCASLGMLGDEPAAELARHGIAHYNINIQVDPGRYGELIADTHSVDERIDTIRRLRAHGIAVCCGGIIGTGETMQERIGMIFALQKLDVTVIPLNVLVPIDGTPLEGAAPVSVPEIAKTFAICRLAHPSKIIKFAAGRETVMKDFQGLLMLAGANGFLTGGYLTTRGRDMEADRQLAGQIARFS | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine. Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2. Homodimer. Belongs to the radical SAM superfamily. Biotin synthase family. |
B3EPW2 | MTVEMNKSIVKAYSVLETGEPLPFDVAVELAHLAGEDVPDLLSLANKVKNRYATLSEGALHSCSIINAKSGVCAENCRFCAQSLHNSADVEQYSLLDAEAIVRSAGDVYDEGIRHFGVVTSGYGYRKVNPEFLKIVAIIDQLRQEYPDLNVCASLGILGEEPVRMLAEHNVRHYNINIQVAPDRYSDLIADSHPLKDRIDTIRLLRKYGIPVCCGGILGVGETMRERLDFIYALQELDIAVIPLNVLVPIEGTPLQGAATPALTDIVKTFALCRLVHPGKIIKFAAGRETVMNDFQGLLMLAGANGFLTGGYLTTRGRKIGDDREFMRQLAGFAEVSCS | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine. Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2. Homodimer. Belongs to the radical SAM superfamily. Biotin synthase family. |
A1BCQ5 | MRPVPLHPDILQAYAVLETGEPVCRELAFALGELHGPDVLDLASLAHKVKLRHGGSSGSIHACSIMNARSGVCSENCRFCAQSAHHQAAIDVYGLVDVDAVLFHARQTASEGISHFGIVTSGFGYKTLSKEFRQILAMIDRLHQELPDLEICASLGVLGEEPALELARHGIAQYNINIQVAPRRYGELIADTHSVDDRIDTIKRLRRNNIDVCCGGIIGVGEQMKERVEMIFAFADLDVSVIPLNILVPIDGTPLEGSPGIPLDDIVKTFALCRLVHPRKIIKIAAGRETVMKDFQGLLMLSGADGLLTGGYLTTRGRATADDRMFMRQLQWFN | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine. Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2. Homodimer. Belongs to the radical SAM superfamily. Biotin synthase family. |
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