O05269 (GUAC_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 76.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 subtilis | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 326 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
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 Probable. Ref.4 |
| Catalytic activity | Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH. HAMAP MF_01511 |
| Induction | Expression is regulated by PurR. Ref.4 |
| Sequence similarities | Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | purine nucleotide metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | GMP reductase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 326 | 326 | GMP reductase HAMAP MF_01511 | PRO_0000093752 | |||||
Regions | |||||||||
| Nucleotide binding | 204 – 227 | 24 | NADP By similarity | ||||||
Sites | |||||||||
| Active site | 175 | 1 | Thioimidate intermediate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 262 | 1 | Q → P in CAB07955. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Oudega B., Koningstein G., de Sales Ramon M., Rodrigues L. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 262. |
| [4] | "Definition of the Bacillus subtilis PurR operator using genetic and bioinformatic tools and expansion of the PurR regulon with glyA, guaC, pbuG, xpt-pbuX, yqhZ-folD, and pbuO." Saxild H.H., Brunstedt K., Nielsen K.I., Jarmer H., Nygaard P. J. Bacteriol. 183:6175-6183(2001) [PubMed: 11591660] [Abstract] Cited for: PROBABLE FUNCTION, REGULATION OF EXPRESSION. Strain: 168. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z93939 Genomic DNA. Translation: CAB07955.1. AL009126 Genomic DNA. Translation: CAB15203.2. |
| PIR | C70015. |
| RefSeq | NP_391093.2. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | O05269. |
| SMR | O05269. Positions 1-321. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000002308; EBBACP00000002308; EBBACG00000002304. |
| GeneID | 937189. |
| GenomeReviews | Gene locus BSU32130 in contig AL009126_GR. |
| KEGG | bsu:BSU32130. |
| NMPDR | fig|224308.1.peg.3219. |
| PATRIC | 18978398. VBIBacSub10457_3362. |
Organism-specific databases | |
| GenoList | BSU32130. [Micado] |
Phylogenomic databases | |
| GeneTree | EBGT00050000000995. |
| HOGENOM | HBG298985. |
| PhylomeDB | O05269. |
| ProtClustDB | PRK05458. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU32130-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01511. GMP_reduct_type2. [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. |
| KO | K00364. |
| PANTHER | PTHR11911:SF30. PTHR11911:SF30. 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_BACSU | ||||||||
| Accession | Primary (citable) accession number: O05269 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

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