| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01035647001 |
| Family | GT43 |
| Protein Properties | Length: 449 Molecular Weight: 51116.8 Isoelectric Point: 9.9109 |
| Chromosome | Chromosome/Scaffold: 4 Start: 2958242 End: 2971785 |
| Description | Nucleotide-diphospho-sugar transferases superfamily protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT43 | 216 | 424 | 0 |
| LAHTLKQVPPPLLWIVVEMMSQSAETADMLMRTGVMYRHLMCNKNLTDIKDRGVHLRNTALSHIETHRLDGTVYFADDDNIYSVDLFEQIRQIRRFGTWT VAKLMESKSKTLLEGPVCNGSQVIGWHTNEMTRRFRRFHTEMSGFAFNSTILWDPKRWHRPTLEPIRQLDTVKEGFQVSTFIERLVEDESQMEGLPEGCS TIMVWHLHL | |||
| Full Sequence |
|---|
| Protein Sequence Length: 449 Download |
| MASIRRTLSP APRDRTLLNG EACSVPSPLS KSSSSTQNYS PEGRLLSPSF SSSDSRLAWY 60 RIQAFIIGIL SQRSSRPLER SKSRGHVWRR ALFHFSICFM VGVFTGFTPF VSMNLSMNLM 120 SKHQAFYFGL IPPVGKLQAY GFVSSKREMP SLNSGITDNN VTLGPQAMKQ ELVNGTAGDV 180 NTPTLIQNSN LVSRKLLIIV TPTYARPFQA YYLNRLAHTL KQVPPPLLWI VVEMMSQSAE 240 TADMLMRTGV MYRHLMCNKN LTDIKDRGVH LRNTALSHIE THRLDGTVYF ADDDNIYSVD 300 LFEQIRQIRR FGTWTVAKLM ESKSKTLLEG PVCNGSQVIG WHTNEMTRRF RRFHTEMSGF 360 AFNSTILWDP KRWHRPTLEP IRQLDTVKEG FQVSTFIERL VEDESQMEGL PEGCSTIMVW 420 HLHLESSHSF YPREWLMKNN LDVIAQLA* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam03360 | Glyco_transf_43 | 7.0e-69 | 216 | 426 | 220 | + Glycosyltransferase family 43. | ||
| PLN02458 | PLN02458 | 2.0e-90 | 78 | 427 | 365 | + transferase, transferring glycosyl groups | ||
| cd00218 | GlcAT-I | 2.0e-98 | 195 | 425 | 237 | + 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 | |
|---|---|
| GO Term | Description |
| GO:0015018 | galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity |
| GO:0016020 | membrane |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAN81600.1 | 0 | 188 | 448 | 5 | 265 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI20871.1 | 0 | 1 | 448 | 1 | 448 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002281445.1 | 0 | 1 | 293 | 1 | 293 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002309550.1 | 0 | 1 | 448 | 1 | 442 | glycosyl transferase [Populus trichocarpa] |
| RefSeq | XP_002516557.1 | 0 | 1 | 448 | 1 | 438 | beta-1,3-glucuronyltransferase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1v84_B | 2e-26 | 199 | 426 | 7 | 235 | A Chain A, Pilus-Related Sortase C Of Group B Streptococcus |
| PDB | 1v84_A | 2e-26 | 199 | 426 | 7 | 235 | A Chain A, Pilus-Related Sortase C Of Group B Streptococcus |
| PDB | 1v83_B | 2e-26 | 199 | 426 | 7 | 235 | A Chain A, Pilus-Related Sortase C Of Group B Streptococcus |
| PDB | 1v83_A | 2e-26 | 199 | 426 | 7 | 235 | A Chain A, Pilus-Related Sortase C Of Group B Streptococcus |
| PDB | 1v82_B | 2e-26 | 199 | 426 | 7 | 235 | A Chain A, Crystal Structure Of Human Glcat-P Apo Form |
