| Identification |
|---|
| HMDB Protein ID
| HMDBP13875 |
| Secondary Accession Numbers
| None |
| Name
| UTP--glucose-1-phosphate uridylyltransferase |
| Synonyms
|
- Alpha-D-glucosyl-1-phosphate uridylyltransferase
- UDP-glucose pyrophosphorylase
- Uridine diphosphoglucose pyrophosphorylase
- UDPGP
|
| Gene Name
| GTAB |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| Catalyzes the formation of UDP-glucose from glucose-1-phosphate and UTP. This is an intermediate step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. a glycolipid found in the membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA) (By similarity). |
| Pathways
|
- Amino sugar and nucleotide sugar metabolism
- Biosynthesis of cofactors
- Biosynthesis of secondary metabolites
- diglucosyl-diacylglycerol biosynthesis
- Galactose metabolism
- O-Antigen nucleotide sugar biosynthesis
- Pentose and glucuronate interconversions
- Starch and sucrose metabolism
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| UDP-glucose metabolic process |
| enterobacterial common antigen biosynthetic process |
| Molecular Function |
| UTP:glucose-1-phosphate uridylyltransferase activity |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| 288 |
| Molecular Weight
| 32677.235 |
| Theoretical pI
| 5.24 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| Q4L8Y7 |
| UniProtKB/Swiss-Prot Entry Name
| GTAB_STAHJ |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Takeuchi F, Watanabe S, Baba T, Yuzawa H, Ito T, Morimoto Y, Kuroda M, Cui L, Takahashi M, Ankai A, Baba S, Fukui S, Lee JC, Hiramatsu K: Whole-genome sequencing of staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species. J Bacteriol. 2005 Nov;187(21):7292-308. doi: 10.1128/JB.187.21.7292-7308.2005. [PubMed:16237012 ]
|
