Reviewed,
UniProtKB/Swiss-Prot Q03AR1 (GUAC_LACC3)
Last modified
February 9, 2010.
Version 23.
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 |
| ||||
| Organism | Lactobacillus casei (strain ATCC 334) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 321967 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus |
Protein attributes
| Sequence length | 329 AA. |
| Sequence status | Complete. |
| 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. HAMAP MF_01511 |
| 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 – 329 | 329 | GMP reductase HAMAP MF_01511 | PRO_0000292051 | |||||
Regions | |||||||||
| Nucleotide binding | 207 – 230 | 24 | NADP Potential | ||||||
Sites | |||||||||
| Active site | 178 | 1 | Thioimidate intermediate By similarity | ||||||
Sequences
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References
| [1] | "Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. Mills D.A.Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed: 17030793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000423 Genomic DNA. Translation: ABJ69711.1. |
| RefSeq | YP_806153.1. |
3D structure databases | |
| SMR | Q03AR1. Positions 7-324. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q03AR1. |
Genome annotation databases | |
| GeneID | 4419308. |
| GenomeReviews | Gene locus LSEI_0911 in contig CP000423_GR. |
| KEGG | lca:LSEI_0911. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0516. |
| HOGENOM | HBG298985. |
| OMA | FAGHEES. |
| PhylomeDB | Q03AR1. |
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. |
| 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_LACC3 | ||||||||
| Accession | Primary (citable) accession number: Q03AR1 | ||||||||
| 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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