Basic Information | |
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Species | Mimulus guttatus |
Cazyme ID | mgv1a023379m |
Family | GT64 |
Protein Properties | Length: 777 Molecular Weight: 86814 Isoelectric Point: 9.4179 |
Chromosome | Chromosome/Scaffold: 8 Start: 1394362 End: 1398202 |
Description | glycosyltransferase family protein 47 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT64 | 523 | 763 | 0 |
FTMLTMTYDARLWNLKMYVKHYSRCSSVREIVVVWNKGAPPKPSDFDSAVPVRIRVEAKNSLNNRFRVDPSIKTRAVLELDDDIMMTCGDIERGFRVWRE NPDRLVGFYPRLVNGSPRLKYRGERHARRHNGYNVILTGAAFMDGQVAFERYWSDEVAQGRALVDEYFNCEDVLMNYLYANSSSASSSSSKSAVEYVRPT WAIDTSKFSGVAISRNTQAHYGVRSNCLMKFAEMYGSLVHR |
Full Sequence |
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Protein Sequence Length: 777 Download |
MGSSPNVASA ASGGGGWRWH KGNSSIGGNR NGSGNGKNER CVLSSTFAYF VFSFVVLGSI 60 GSLYGRYMLA ANVRTGIAAQ GCEADSEGSW AVGVYYGDSP FSLKPIEAVN VWKDKSAAWP 120 VANPVITCAS LSDAGFPSNF VADPFLYQQG DTLYMFYETK NTITKQGDIG VAQSTDKGAT 180 WRQLGIALDE DWHLSYPYVF EYNGNIYMMP EGSKKGDLRL YVATDFPLKW TLDKIIMQKP 240 LIDSFIIPHE GRFFLFGSDH SEIGTKKNGQ LAIWHSDSPL GPWKPHRKNP IYNTDKAMGA 300 RNGGRPFVYK GQLYRTGQDC GETYGRRIRV FKVKVLTETI EYLILVQKVP FDFGGESMKG 360 RNSWNGARTH HLDVQQLNTG EWIAVLDGDR VPSGDAVRRF LVGSASVSAV AALVVLFGMF 420 VGVVKCLVPL SWCPHNMEKR SDTFLVYERP PKLTSKLRLI CSRLNRTCSF LHSKIRPKTC 480 TGSIVLILTI LIAVALTCTA VTYLYGGSGA EEPYPLNGHH SQFTMLTMTY DARLWNLKMY 540 VKHYSRCSSV REIVVVWNKG APPKPSDFDS AVPVRIRVEA KNSLNNRFRV DPSIKTRAVL 600 ELDDDIMMTC GDIERGFRVW RENPDRLVGF YPRLVNGSPR LKYRGERHAR RHNGYNVILT 660 GAAFMDGQVA FERYWSDEVA QGRALVDEYF NCEDVLMNYL YANSSSASSS SSKSAVEYVR 720 PTWAIDTSKF SGVAISRNTQ AHYGVRSNCL MKFAEMYGSL VHRKLDFNRR RDGWDL* 780 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd08978 | GH_F | 3.0e-5 | 91 | 303 | 232 | + Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 enzymes, is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. | ||
cd08978 | GH_F | 1.0e-6 | 142 | 399 | 279 | + Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 enzymes, is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. | ||
pfam09258 | Glyco_transf_64 | 1.0e-68 | 523 | 763 | 246 | + Glycosyl transferase family 64 domain. Members of this family catalyze the transfer reaction of N-acetylglucosamine and N-acetylgalactosamine from the respective UDP-sugars to the non-reducing end of [glucuronic acid]beta 1-3[galactose]beta 1-O-naphthalenemethanol, an acceptor substrate analog of the natural common linker of various glycosylaminoglycans. They are also required for the biosynthesis of heparan-sulphate. |
Gene Ontology | |
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GO Term | Description |
GO:0016758 | transferase activity, transferring hexosyl groups |
GO:0031227 | intrinsic to endoplasmic reticulum membrane |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAB85556.1 | 0 | 47 | 776 | 40 | 764 | putative protein [Arabidopsis thaliana] |
RefSeq | NP_196070.2 | 0 | 47 | 776 | 41 | 765 | glycosyltransferase family protein 47 [Arabidopsis thaliana] |
RefSeq | XP_002262646.1 | 0 | 77 | 776 | 68 | 756 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315348.1 | 0 | 67 | 776 | 87 | 847 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532924.1 | 0 | 76 | 776 | 15 | 704 | transferase, transferring glycosyl groups, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1on8_B | 2e-24 | 523 | 760 | 30 | 270 | A Chain A, E. Coli Gsp Amidase C59a Complexed With Gsp |
PDB | 1on8_A | 2e-24 | 523 | 760 | 30 | 270 | A Chain A, E. Coli Gsp Amidase C59a Complexed With Gsp |
PDB | 1on6_B | 2e-24 | 523 | 760 | 30 | 270 | A Chain A, E. Coli Gsp Amidase C59a Complexed With Gsp |
PDB | 1on6_A | 2e-24 | 523 | 760 | 30 | 270 | A Chain A, E. Coli Gsp Amidase C59a Complexed With Gsp |
PDB | 1omz_B | 2e-24 | 523 | 760 | 30 | 270 | A Chain A, E. Coli Gsp Amidase C59a Complexed With Gsp |