Basic Information | |
---|---|
Species | Cucumis sativus |
Cazyme ID | Cucsa.102610.2 |
Family | GT43 |
Protein Properties | Length: 507 Molecular Weight: 57064.4 Isoelectric Point: 9.3677 |
Chromosome | Chromosome/Scaffold: 00927 Start: 1617122 End: 1622063 |
Description | Nucleotide-diphospho-sugar transferases superfamily protein |
View CDS |
External Links |
---|
NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GT43 | 184 | 418 | 0 |
MHSLMLVPYELVWIVVEAGGITNETASVLAKSGLETIHVGFNQRMPTSWEGRHRMEAQMRLHALRIVSKMMLDGIVTFVDDSNMHSMEFFDEIQNVKWFG ALSVGIIVQSDKQDESSDEMENPPIPAQGPACNSSNKLVGWHTFNALPYAGKSAKFIGDKTSVLPRKLEWCGFVLNSKLLWKDAEDKPEWVNEFDTLEVG DDALESPLFLLKDASMVEPLGSCGRQVLLWWLRVE |
Full Sequence |
---|
Protein Sequence Length: 507 Download |
MKLSALQQTY AARRANSFRG SPLDSSADSP IKSPAGIFWL ILHGLCCLIS LVLGFRFSRL 60 VFFLFFSTST TTNLYLTPFR SATDLNVHST SLSNPTVNLE IPVNKTTHTT IAASSSRVVV 120 GRHGIRIRPW PHPNPTEVMK AHQIIETVQR EQRRQFGVKN PRKIIAITPT YVRTFQALHM 180 TGVMHSLMLV PYELVWIVVE AGGITNETAS VLAKSGLETI HVGFNQRMPT SWEGRHRMEA 240 QMRLHALRIV SKMMLDGIVT FVDDSNMHSM EFFDEIQNVK WFGALSVGII VQSDKQDESS 300 DEMENPPIPA QGPACNSSNK LVGWHTFNAL PYAGKSAKFI GDKTSVLPRK LEWCGFVLNS 360 KLLWKDAEDK PEWVNEFDTL EVGDDALESP LFLLKDASMV EPLGSCGRQV LLWWLRVEAR 420 FDSKFPHGWL IDPPLEITVP AKRTPWPDVP PELPTNEKAQ TDNHEETTKL PAKSHSSRSR 480 RSSRSKRKRH EPKVVDTQTS VRHSEN* |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02458 | PLN02458 | 4.0e-16 | 135 | 364 | 233 | + transferase, transferring glycosyl groups | ||
pfam03360 | Glyco_transf_43 | 5.0e-43 | 183 | 419 | 247 | + Glycosyltransferase family 43. | ||
cd00218 | GlcAT-I | 6.0e-59 | 164 | 419 | 263 | + 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 | CAI93186.1 | 0 | 1 | 486 | 1 | 476 | glycosyltransferase [Gossypium raimondii] |
EMBL | CAI94900.1 | 0 | 1 | 506 | 1 | 491 | glycosyltransferase [Glycine max] |
RefSeq | XP_002283249.1 | 0 | 1 | 473 | 1 | 481 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002306485.1 | 0 | 1 | 506 | 1 | 502 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002310709.1 | 0 | 1 | 505 | 1 | 508 | glycosyl transferase, CAZy family GT43 [Populus trichocarpa] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2d0j_D | 0.00000004 | 164 | 326 | 5 | 155 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
PDB | 2d0j_C | 0.00000004 | 164 | 326 | 5 | 155 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
PDB | 2d0j_B | 0.00000004 | 164 | 326 | 5 | 155 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
PDB | 2d0j_A | 0.00000004 | 164 | 326 | 5 | 155 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
PDB | 1v84_B | 0.0000001 | 164 | 437 | 5 | 253 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |