| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G160585_T01 |
| Family | GT43 |
| Protein Properties | Length: 452 Molecular Weight: 48406.4 Isoelectric Point: 6.9098 |
| Chromosome | Chromosome/Scaffold: 2 Start: 5229654 End: 5233677 |
| 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 | 196 | 404 | 0 |
| LAHTLRLVDAQLVWIVVEPGHRTDAVAAVLSRSNLDFLHITGPGDSTASLRMHALREIRAKRMDGIVVFADENSILRTELFDEAQKVTTVGAVPVGILGE DDGTSESFLQAPSCDAEGKLVGYHVSEETVLPANRSDMLMASRLEWAGFVVNARALWEDTKERPLWVRDLSAIDDADARAASPLALVTDAGRVEPLASCA QAALAWSLR | |||
| Full Sequence |
|---|
| Protein Sequence Length: 452 Download |
| MKLPLLRPLW LGLGSAAGPP DAAPEPAKPS LPAAWLLLHA LFCATSMAVG FRFSRLIVYL 60 LFLPTPPINP AAHLVSLVSP PAVVLAGGNA TAMATITTTT TTTTTVTTTT TVAAEISARP 120 QHHHHHGPVF VGRHPIRVRA WPHPNPSELL DAHRILAAVQ NAQRSAKRRG AGPARPVIAV 180 TPTTTSALQV PSLTSLAHTL RLVDAQLVWI VVEPGHRTDA VAAVLSRSNL DFLHITGPGD 240 STASLRMHAL REIRAKRMDG IVVFADENSI LRTELFDEAQ KVTTVGAVPV GILGEDDGTS 300 ESFLQAPSCD AEGKLVGYHV SEETVLPANR SDMLMASRLE WAGFVVNARA LWEDTKERPL 360 WVRDLSAIDD ADARAASPLA LVTDAGRVEP LASCAQAALA WSLRSDSLHE VKFPHEWKID 420 PALLNTGARQ QTVQPETQPM QTTLASTEDQ H* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02458 | PLN02458 | 7.0e-14 | 173 | 353 | 191 | + transferase, transferring glycosyl groups | ||
| pfam03360 | Glyco_transf_43 | 9.0e-26 | 196 | 407 | 230 | + Glycosyltransferase family 43. | ||
| cd00218 | GlcAT-I | 2.0e-55 | 175 | 406 | 244 | + 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 | CAI93182.1 | 0 | 1 | 451 | 1 | 453 | glycosyltransferase [Sorghum bicolor] |
| GenBank | EEC78139.1 | 0 | 1 | 451 | 1 | 446 | hypothetical protein OsI_17696 [Oryza sativa Indica Group] |
| RefSeq | NP_001105810.1 | 0 | 1 | 416 | 1 | 416 | glycosyltransferase [Zea mays] |
| RefSeq | NP_001148104.1 | 0 | 1 | 451 | 1 | 454 | LOC100281712 [Zea mays] |
| RefSeq | XP_002448650.1 | 0 | 1 | 451 | 1 | 454 | hypothetical protein SORBIDRAFT_06g030810 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2d0j_D | 0.00000000007 | 177 | 409 | 5 | 230 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
| PDB | 2d0j_C | 0.00000000007 | 177 | 409 | 5 | 230 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
| PDB | 2d0j_B | 0.00000000007 | 177 | 409 | 5 | 230 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
| PDB | 2d0j_A | 0.00000000007 | 177 | 409 | 5 | 230 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
| PDB | 1v84_B | 0.000000004 | 180 | 432 | 8 | 247 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
| Hydropathy |
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