y
Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 902844 |
Family | GT43 |
Protein Properties | Length: 352 Molecular Weight: 40039.9 Isoelectric Point: 9.8991 |
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 | 137 | 342 | 0 |
MANTLRLVPPPLLWIVVEKHSDAEEKSSSTMLRKTGIMYRRIVFKEDFTSLESELDHQRNLALRHIEHHKLSGIVHFAGLNNIYDLDFFDKIRDIEVFGT WPMALLSANRKRVIVEGPVCESSQVLGWHLRKINNETETKPPIHISSFAFNSSILWDPERWGRPSSVEGTKQDSIKYVKQVVLEDDTKLKGLPAQDCSKI MLWRLN |
Full Sequence |
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Protein Sequence Length: 352 Download |
MGSLERSKKK AQVWKKAVIQ FSLCFVMGFF TGFAPAGKAS FFSNSETTPY TSTKSQISAQ 60 PFENSTYTSH SLLNRTLTNS QGQAPAPAEW REAEAETRSL SETEDENQVK VTPRGLVIVV 120 TPIITKDRYK NVLLRRMANT LRLVPPPLLW IVVEKHSDAE EKSSSTMLRK TGIMYRRIVF 180 KEDFTSLESE LDHQRNLALR HIEHHKLSGI VHFAGLNNIY DLDFFDKIRD IEVFGTWPMA 240 LLSANRKRVI VEGPVCESSQ VLGWHLRKIN NETETKPPIH ISSFAFNSSI LWDPERWGRP 300 SSVEGTKQDS IKYVKQVVLE DDTKLKGLPA QDCSKIMLWR LNFPTRTRLS P* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03360 | Glyco_transf_43 | 4.0e-74 | 137 | 345 | 223 | + Glycosyltransferase family 43. | ||
cd00218 | GlcAT-I | 1.0e-88 | 116 | 345 | 235 | + 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). | ||
PLN02458 | PLN02458 | 0 | 1 | 350 | 353 | + transferase, transferring glycosyl groups |
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 | AAX33319.1 | 0 | 1 | 345 | 1 | 341 | secondary cell wall-related glycosyltransferase family 43 [Populus tremula x Populus tremuloides] |
GenBank | ABP65661.1 | 0 | 1 | 345 | 1 | 341 | secondary wall-associated glycosyltransferase family 43B [Populus tremula x Populus alba] |
RefSeq | NP_181246.1 | 0 | 1 | 350 | 1 | 350 | IRX9 (IRREGULAR XYLEM 9); transferase, transferring glycosyl groups / xylosyltransferase [Arabidopsis thaliana] |
RefSeq | XP_002323456.1 | 0 | 1 | 345 | 1 | 342 | glycosyl transferase [Populus trichocarpa] |
RefSeq | XP_002326337.1 | 0 | 1 | 345 | 1 | 338 | glycosyl transferase [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 | 0.000000000008 | 119 | 339 | 7 | 229 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1v84_A | 0.000000000008 | 119 | 339 | 7 | 229 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1v83_B | 0.000000000008 | 119 | 339 | 7 | 229 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1v83_A | 0.000000000008 | 119 | 339 | 7 | 229 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1v82_B | 0.000000000008 | 119 | 339 | 7 | 229 | A Chain A, Crystal Structure Of Human Glcat-P Apo Form |