| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G118959_T01 |
| Family | GT43 |
| Protein Properties | Length: 353 Molecular Weight: 37529.1 Isoelectric Point: 9.207 |
| Chromosome | Chromosome/Scaffold: 9 Start: 138241669 End: 138245692 |
| Description | Nucleotide-diphospho-sugar transferases superfamily protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GT43 | 122 | 339 | 0 |
| AHALRLVAPPLLWVVVEAAPDAPATARQLRATGLMYRHLTYRDNFTAAGAGKERHHQRNVALGHVEHHRLAGVVLFAGLDDVLDLRLFDQIREISAFGAW PVATMWRDEREVVVRGPACSSSAVTGWFSQDLSDGTAAAASTTSTARARPSGEVDVHGFAFNSSVLWDPERWGRYPTSEPDKSQDSTKFVQQVVLEDLSK VKGIPSDCSEVMVWHVDT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 353 Download |
| MGSSTDHGGA GWRGKKQGSQ LWKKALLHSS LCFVMGFFTG FAPSSVSDWT SAAAAAGSSS 60 SSSHVVRALP AGGALNRSLL AHGAGPGYDR AASPRPLLVV VTTTESTPVA SGERAAALTR 120 TAHALRLVAP PLLWVVVEAA PDAPATARQL RATGLMYRHL TYRDNFTAAG AGKERHHQRN 180 VALGHVEHHR LAGVVLFAGL DDVLDLRLFD QIREISAFGA WPVATMWRDE REVVVRGPAC 240 SSSAVTGWFS QDLSDGTAAA ASTTSTARAR PSGEVDVHGF AFNSSVLWDP ERWGRYPTSE 300 PDKSQDSTKF VQQVVLEDLS KVKGIPSDCS EVMVWHVDTA APSPSSPQNK RR* 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 | 6.0e-39 | 130 | 341 | 227 | + Glycosyltransferase family 43. | ||
| cd00218 | GlcAT-I | 4.0e-56 | 96 | 341 | 250 | + 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 | 1.0e-87 | 1 | 335 | 360 | + transferase, transferring glycosyl groups | ||
| 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 |
| GenBank | ABF95369.1 | 0 | 1 | 333 | 1 | 337 | Glycosyltransferase family 43 protein, expressed [Oryza sativa (japonica cultivar-group)] |
| DDBJ | BAF11694.2 | 0 | 1 | 333 | 1 | 337 | Os03g0287800 [Oryza sativa Japonica Group] |
| RefSeq | NP_001049780.1 | 0 | 1 | 351 | 1 | 357 | Os03g0287800 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001147664.1 | 0 | 1 | 352 | 1 | 350 | beta3-glucuronyltransferase [Zea mays] |
| RefSeq | XP_002468048.1 | 0 | 1 | 352 | 1 | 367 | hypothetical protein SORBIDRAFT_01g038640 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1v84_B | 0.000000000000008 | 96 | 342 | 3 | 236 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 1v84_A | 0.000000000000008 | 96 | 342 | 3 | 236 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 1v83_B | 0.000000000000008 | 96 | 342 | 3 | 236 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 1v83_A | 0.000000000000008 | 96 | 342 | 3 | 236 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 1v82_B | 0.000000000000008 | 96 | 342 | 3 | 236 | A Chain A, Crystal Structure Of Human Glcat-P Apo Form |
| Hydropathy |
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