Reviewed,
UniProtKB/Swiss-Prot Q88SV5 (GUAC_LACPL)
Last modified
November 25, 2008.
Version 35.
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 | Lactobacillus plantarum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1590 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus |
Protein attributes
| Sequence length | 325 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 + NH(3) + NADP(+) = guanosine 5'-phosphate + NADPH. |
| 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: InterPro 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)
Sequences
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References
| [1] | "Complete genome sequence of Lactobacillus plantarum WCFS1." Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., Siezen R.J. Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003) [PubMed: 12566566] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-793 / NCIMB 8826 / WCFS1. |
Cross-references
Sequence databases | |
|---|---|
| AL935261 Genomic DNA. Translation: CAD65404.1. | |
| RefSeq | NP_786532.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1B3O based on UniProtKB P12268. |
| SMR | Q88SV5. Positions 5-321. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1061982. |
| GenomeReviews | Gene locus lp_3271 in contig AL935263_GR. |
| KEGG | lpl:lp_3271. |
| NMPDR | fig|220668.1.peg.2666. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q88SV5. |
Enzyme and pathway databases | |
| BioCyc | LPLA220668:LP_3271-MON. |
Family and domain databases | |
| HAMAP | MF_01511. [Tree] |
| InterPro | IPR013785. Aldolase_TIM. IPR005994. GMP_reduct2. IPR015875. IMP_DH/GMP_Rdtase_CS. IPR001093. IMP_DHase_GMPRtase. [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_LACPL | ||||||||
| Accession | Primary (citable) accession number: Q88SV5 | ||||||||
| 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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