Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_007_00731.1 |
Family | GT43 |
Protein Properties | Length: 516 Molecular Weight: 58460.7 Isoelectric Point: 8.0831 |
Chromosome | Chromosome/Scaffold: 7 Start: 5714303 End: 5719375 |
Description | Nucleotide-diphospho-sugar transferases superfamily protein |
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 |
GT43 | 185 | 427 | 0 |
LMHSLMLVPYDLVWIVVEAGGVSNETASILEKSKLQTIHIGFDEKMPISWDERHRMEARMRFKGLRVVREERLDGIVMFADDSNMHSMELFDEIQSVKWM GAVSVGILAHSANSVESFSLTQMEEDETENVPMPVQGPACNSSGQLAGWHTFNSLPYVEKSATYIDDMAMVLPRKLEWAGFVLNSRLLWKEAEDKPEWIR DLDTLVDDGDTLESPLSLLKDSSFVEPLGNCGRKVLLWWLRVE |
Full Sequence |
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Protein Sequence Length: 516 Download |
MKFSILQQNF NNRRSNSFRQ TNSIDSSVLD SKSPASLFWL VLHGLCCLIS LVLGFRFSRI 60 IFFLLFSSTT IDHFTSSTPF FKTDSSQTLT FHHQSPPSLE ITSLNRSRSS ISSSNSGGGV 120 VVGRHGILIR PWPHPNPTEV MKAHRIMERV QREQRVQYGI KNPRNLIVIT PTYVRTFQTL 180 HLTGLMHSLM LVPYDLVWIV VEAGGVSNET ASILEKSKLQ TIHIGFDEKM PISWDERHRM 240 EARMRFKGLR VVREERLDGI VMFADDSNMH SMELFDEIQS VKWMGAVSVG ILAHSANSVE 300 SFSLTQMEED ETENVPMPVQ GPACNSSGQL AGWHTFNSLP YVEKSATYID DMAMVLPRKL 360 EWAGFVLNSR LLWKEAEDKP EWIRDLDTLV DDGDTLESPL SLLKDSSFVE PLGNCGRKVL 420 LWWLRVEARA DSKFPPGWII DPPLEITVPA KRTPWPDAPP ELPSDEKLNG VQEHAEKRNP 480 KTGRTSRSRH GSRSKKKHDS RLLDTQGSGR RSEEK* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02458 | PLN02458 | 1.0e-15 | 135 | 334 | 201 | + transferase, transferring glycosyl groups | ||
pfam03360 | Glyco_transf_43 | 5.0e-47 | 185 | 428 | 251 | + Glycosyltransferase family 43. | ||
cd00218 | GlcAT-I | 1.0e-57 | 166 | 428 | 267 | + Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan synthesis. Beta1,3-glucuronyltransferase I (GlcAT-I) domain; GlcAT-I is a Key enzyme involved in the initial steps of proteoglycan synthesis. GlcAT-I catalyzes the transfer of a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region of trisaccharide Gal-beta-(1-3)-Gal-beta-(1-4)-Xyl of proteoglycans. The enzyme has two subdomains that bind the donor and acceptor substrate separately. The active site is located at the cleft between both subdomains in which the trisaccharide molecule is oriented perpendicular to the UDP. This family has been classified as Glycosyltransferase family 43 (GT-43). |
Gene Ontology | |
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GO Term | Description |
GO:0015018 | galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity |
GO:0016020 | 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 | CAI93188.1 | 0 | 2 | 514 | 3 | 504 | glycosyltransferase [Solanum lycopersicum] |
EMBL | CAI94901.1 | 0 | 1 | 512 | 1 | 504 | glycosyltransferase [Poncirus trifoliata] |
EMBL | CBI21374.1 | 0 | 1 | 514 | 1 | 475 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002283249.1 | 0 | 1 | 514 | 1 | 513 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002306485.1 | 0 | 1 | 514 | 1 | 502 | predicted protein [Populus trichocarpa] |
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 | 1v84_B | 0.0000000007 | 168 | 446 | 7 | 253 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
PDB | 1v84_A | 0.0000000007 | 168 | 446 | 7 | 253 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
PDB | 1v83_B | 0.0000000007 | 168 | 446 | 7 | 253 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
PDB | 1v83_A | 0.0000000007 | 168 | 446 | 7 | 253 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
PDB | 1v82_B | 0.0000000007 | 168 | 446 | 7 | 253 | A Chain A, Crystal Structure Of Human Glcat-P Apo Form |