y
Basic Information | |
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Species | Sorghum bicolor |
Cazyme ID | Sb09g028220.1 |
Family | GT43 |
Protein Properties | Length: 452 Molecular Weight: 51452.4 Isoelectric Point: 9.0841 |
Chromosome | Chromosome/Scaffold: 9 Start: 57186325 End: 57188397 |
Description | Nucleotide-diphospho-sugar transferases superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT43 | 216 | 427 | 0 |
LAHVLKAVHAPLLWLVVEWPEQSYETAEILRSSGVMYRHLVCRKNTTSVRKIAVCQRNNAIYHIKRHHLDGIMHFADEERSYSADVFEEMQKIRRFGSWP VAIHVGTKYRAVLEGPICKGNRVMGWHTVQTAQKKSLTRRFPIGFSAFAFNSTMLWDPQRWNRPPMDSVIVHSGGRGGLQESRFIEKLVKNERQIEGLPD NCNRAMVWNFNL |
Full Sequence |
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Protein Sequence Length: 452 Download |
MVSSRRNSGV ILREGSVRDW SEFNDPSPSP KLLYSQSYVA MRGLLASLIS LDFFLLSSKL 60 KSACAAMTSQ RHSRSQERSK SKGLSCRRVA VHLLFFFMVG IFIGFMPLFS VDVYKKIVSE 120 NERLPFHEGV IETETMGTKV KELETVVVEK EVELIDEPQV QESPPVPAML DDEADFAESS 180 PALPGIEESD IVAKKLLIIV TITSVRPQQA YYLNRLAHVL KAVHAPLLWL VVEWPEQSYE 240 TAEILRSSGV MYRHLVCRKN TTSVRKIAVC QRNNAIYHIK RHHLDGIMHF ADEERSYSAD 300 VFEEMQKIRR FGSWPVAIHV GTKYRAVLEG PICKGNRVMG WHTVQTAQKK SLTRRFPIGF 360 SAFAFNSTML WDPQRWNRPP MDSVIVHSGG RGGLQESRFI EKLVKNERQI EGLPDNCNRA 420 MVWNFNLEPP LLNYPRGWAI YKNLEADMPV I* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03360 | Glyco_transf_43 | 5.0e-52 | 216 | 423 | 217 | + Glycosyltransferase family 43. | ||
PLN02458 | PLN02458 | 7.0e-58 | 160 | 427 | 275 | + transferase, transferring glycosyl groups | ||
cd00218 | GlcAT-I | 6.0e-97 | 195 | 429 | 241 | + 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 |
GenBank | ACL54619.1 | 0 | 1 | 451 | 1 | 441 | unknown [Zea mays] |
GenBank | ACN26728.1 | 0 | 1 | 450 | 1 | 450 | unknown [Zea mays] |
EMBL | CAI96159.1 | 0 | 1 | 435 | 1 | 435 | glycosyltransferase [Saccharum officinarum] |
RefSeq | NP_001152042.1 | 0 | 1 | 451 | 1 | 441 | LOC100285679 [Zea mays] |
RefSeq | XP_002440234.1 | 0 | 1 | 451 | 1 | 451 | hypothetical protein SORBIDRAFT_09g028220 [Sorghum bicolor] |
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 | 2e-21 | 199 | 432 | 7 | 238 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1v84_A | 2e-21 | 199 | 432 | 7 | 238 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1v83_B | 2e-21 | 199 | 432 | 7 | 238 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1v83_A | 2e-21 | 199 | 432 | 7 | 238 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1v82_B | 2e-21 | 199 | 432 | 7 | 238 | A Chain A, Crystal Structure Of Human Glcat-P Apo Form |