Reviewed,
UniProtKB/Swiss-Prot A0RLN5 (GUAC_BACAH)
Last modified
June 16, 2009.
Version 17.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: GMP reductase EC=1.7.1.7 Alternative name(s): Guanosine 5'-monophosphate oxidoreductase Short name=Guanosine monophosphate reductase | ||||
| Gene names |
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| Organism | Bacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 412694 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 328 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides By similarity. |
| Catalytic activity | Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH. HAMAP MF_01511 |
| Sequence similarities | Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW purine nucleotide metabolic processInferred from electronic annotation. Source: HAMAP |
| Molecular function | GMP reductase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 328 | 328 | GMP reductase HAMAP MF_01511 | PRO_0000292049 | |||||
Regions | |||||||||
| Nucleotide binding | 205 – 228 | 24 | NADP Potential | ||||||
Sites | |||||||||
| Active site | 176 | 1 | Thioimidate intermediate By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Bacillus thuringiensis Al Hakam." Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Green L.D., Han C.S. Brettin T.S.J. Bacteriol. 189:3680-3681(2007) [PubMed: 17337577] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000485 Genomic DNA. Translation: ABK88128.1. | |
| RefSeq | YP_897635.1. |
3D structure databases | |
| SMR | A0RLN5. Positions 2-322. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 4543702. |
| GenomeReviews | Gene locus BALH_4963 in contig CP000485_GR. |
| KEGG | btl:BALH_4963. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | A0RLN5. NSRSECD. |
Family and domain databases | |
| HAMAP | MF_01511. [Tree] |
| InterPro | IPR013785. Aldolase_TIM. IPR005994. GMP_reduct2. IPR015875. IMP_DH/GMP_Rdtase_CS. IPR001093. IMP_DH_GMPRt. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. |
| Pfam | PF00478. IMPDH. 1 hit. [Graphical view] |
| PIRSF | PIRSF036500. GMP_red_Firmic. 1 hit. |
| TIGRFAMs | TIGR01306. GMP_reduct_2. 1 hit. |
| PROSITE | PS00487. IMP_DH_GMP_RED. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GUAC_BACAH | ||||||||
| Accession | Primary (citable) accession number: A0RLN5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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