| Basic Information | |
|---|---|
| Species | Populus trichocarpa |
| Cazyme ID | Potri.001G179000.5 |
| Family | GT4 |
| Protein Properties | Length: 682 Molecular Weight: 75938.6 Isoelectric Point: 10.7078 |
| Chromosome | Chromosome/Scaffold: 01 Start: 15425814 End: 15433015 |
| Description | UDP-Glycosyltransferase superfamily protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GT4 | 525 | 650 | 4.4e-24 |
| VLIGSVGSKSNKVPYVKEILRFISQHSNLSKSVLWTSATTRVASLYSAADVYITNSQGLGETFGRVTIEAMAFGLPVLGTDAGGTQEIVEHNITGLLHPV GRPGSRVLAQNIELLLKNPSVRKQMG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 682 Download |
| MEEGKSRGDL HVNVLKQTPS RQGGSFKSTT LSGRSTPRNS PTHRLLHSSR TPRREGRGSG 60 GIQWFRSNRL IYWLLLITLW TYLGFYVQSR WAHGDNKDEF LGFGGKSSNG LLDAEQHTRR 120 DLLANDSLVV VNNGTNKIQV RNAKKIDVVL AKKGNGVSSN RRATPKKKKS KRGGRRSRAK 180 AHDKQKATVV VESDDVEVAE PDVPKNNASY GLLVGPFGPI EDRILEWSPE KRSGTCDRKG 240 AFARLVWSRK FVLIFHELSM TGAPLSMLEL ATEFLSCGAT VSAVVLSKKG GLMPELARRR 300 IKVLEDRADL SFKTAMKADL VIAGSAVCTS WIDQYIARFP AGGSQVVWWI MENRREYFDR 360 SKIILNRVKM LVFLSESQMK QWQTWCEEEN IRLRSPPAVV QLSVNDELAF VAGIACSLNT 420 PTSSSEKMLE KRQLLRESVR KEMGLTDNDM LVMSLSSINA GKGQLLLLES ANLVIEPDPS 480 PKITNSVDKG NQSTLAAKHH LRALSHRKRK LLADSEGTHE QALKVLIGSV GSKSNKVPYV 540 KEILRFISQH SNLSKSVLWT SATTRVASLY SAADVYITNS QGLGETFGRV TIEAMAFGLP 600 VLGTDAGGTQ EIVEHNITGL LHPVGRPGSR VLAQNIELLL KNPSVRKQMG IKGRKKVEKM 660 YLKRHMYKKI WEVLYKCMRV K* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00534 | Glycos_transf_1 | 9.0e-20 | 504 | 655 | 159 | + Glycosyl transferases group 1. Mutations in this domain of human PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family. | ||
| TIGR00072 | hydrog_prot | 6.0e-20 | 541 | 672 | 133 | + hydrogenase maturation protease. HycI and HoxM are well-characterized as responsible for C-terminal protease activity on their respective hydrogenase large chains. A large number of homologous proteins appear responsible for the maturation of various forms of hydrogenase. | ||
| cd03825 | GT1_wcfI_like | 6.0e-21 | 559 | 670 | 119 | + This family is most closely related to the GT1 family of glycosyltransferases. wcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis. | ||
| cd03808 | GT1_cap1E_like | 2.0e-23 | 552 | 672 | 121 | + This family is most closely related to the GT1 family of glycosyltransferases. cap1E in Streptococcus pneumoniae is required for the synthesis of type 1 capsular polysaccharides. | ||
| cd03801 | GT1_YqgM_like | 6.0e-29 | 437 | 675 | 241 | + This family is most closely related to the GT1 family of glycosyltransferases and named after YqgM in Bacillus licheniformis about which little is known. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0009058 | biosynthetic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAN71826.1 | 0 | 1 | 681 | 1 | 734 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI36173.1 | 0 | 1 | 681 | 1 | 683 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002284822.1 | 0 | 15 | 681 | 4 | 691 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002298139.1 | 0 | 1 | 681 | 1 | 681 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002528176.1 | 0 | 1 | 681 | 1 | 686 | glycosyltransferase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3mbo_H | 0.0000000004 | 538 | 679 | 271 | 407 | A Chain A, Crystal Structure Of The Glycosyltransferase Babsha Bound With Udp And L-Malate |
| PDB | 3mbo_G | 0.0000000004 | 538 | 679 | 271 | 407 | A Chain A, Crystal Structure Of The Glycosyltransferase Babsha Bound With Udp And L-Malate |
| PDB | 3mbo_F | 0.0000000004 | 538 | 679 | 271 | 407 | A Chain A, Crystal Structure Of The Glycosyltransferase Babsha Bound With Udp And L-Malate |
| PDB | 3mbo_E | 0.0000000004 | 538 | 679 | 271 | 407 | A Chain A, Crystal Structure Of The Glycosyltransferase Babsha Bound With Udp And L-Malate |
| PDB | 3mbo_D | 0.0000000004 | 538 | 679 | 271 | 407 | A Chain A, Crystal Structure Of The Glycosyltransferase Babsha Bound With Udp And L-Malate |
