Reviewed,
UniProtKB/Swiss-Prot A7H432 (GLMU_CAMJD)
Last modified
February 9, 2010.
Version 23.
History...
Clusters with 100%,
90%,
50% identity |
 Documents (2) |
 Third-party data |
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Names and origin
| Protein names | Recommended name: Bifunctional protein glmU Including the following 2 domains: 1- Recommended name: UDP-N-acetylglucosamine pyrophosphorylase EC=2.7.7.23 Alternative name(s): N-acetylglucosamine-1-phosphate uridyltransferase 2- Recommended name: Glucosamine-1-phosphate N-acetyltransferase EC=2.3.1.157 | ||||
| Gene names |
| ||||
| Organism | Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 360109 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 429 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-GlcNAc. Responsible for the acetylation of Glc-N-1-P to give GlcNAc-1-P and for the uridyl transfer from UTP to GlcNAc-1-P which produces UDP-GlcNAc By similarity. HAMAP MF_01631 |
| Catalytic activity | Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. HAMAP MF_01631 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-D-glucosamine. HAMAP MF_01631 |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01631 |
| Pathway | Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. HAMAP MF_01631 Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. HAMAP MF_01631 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_01631. |
| Sequence similarities | In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family. In the C-terminal section; belongs to the transferase hexapeptide repeat family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 429 | 429 | Bifunctional protein glmU HAMAP MF_01631 | PRO_1000056147 | |||||
Regions | |||||||||
| Region | 1 – 223 | 223 | Pyrophosphorylase By similarity | ||||||
| Region | 8 – 11 | 4 | Substrate binding By similarity | ||||||
| Region | 81 – 82 | 2 | Substrate binding By similarity | ||||||
| Region | 224 – 244 | 21 | Linker By similarity | ||||||
| Region | 245 – 429 | 185 | N-acetyltransferase By similarity | ||||||
Sites | |||||||||
| Active site | 336 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 102 | 1 | Magnesium By similarity | ||||||
| Metal binding | 221 | 1 | Magnesium By similarity | ||||||
| Binding site | 74 | 1 | Substrate By similarity | ||||||
| Binding site | 135 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 149 | 1 | Substrate By similarity | ||||||
| Binding site | 164 | 1 | Substrate By similarity | ||||||
| Binding site | 360 | 1 | Acetyl-CoA By similarity | ||||||
| Binding site | 378 | 1 | Acetyl-CoA By similarity | ||||||
| Binding site | 396 | 1 | Acetyl-CoA; via amide nitrogen By similarity | ||||||
| Binding site | 413 | 1 | Acetyl-CoA By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97 isolated from human blood." Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E. Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000768 Genomic DNA. Translation: ABS44851.1. |
| RefSeq | YP_001398262.1. |
3D structure databases | |
| SMR | A7H432. Positions 5-417. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A7H432. |
Genome annotation databases | |
| GeneID | 5388849. |
| GenomeReviews | Gene locus JJD26997_1193 in contig CP000768_GR. |
| KEGG | cjd:JJD26997_1193. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1207. |
| HOGENOM | HBG688195. |
| OMA | GSKVNHL. |
Family and domain databases | |
| HAMAP | MF_01631. GlmU. [Tree] |
| InterPro | IPR005882. Bifunctional_GlmU. IPR005835. NTP_transferase. IPR011004. Trimer_LpxA-like. [Graphical view] |
| Pfam | PF00483. NTP_transferase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01173. glmU. 1 hit. |
| PROSITE | PS00101. HEXAPEP_TRANSFERASES. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GLMU_CAMJD | ||||||||
| Accession | Primary (citable) accession number: A7H432 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
