Q2FV67 (ROCA_STAA8)
Reviewed,
UniProtKB/Swiss-Prot
Last modified
August 10, 2010.
Version 31.
History...
Customize displayNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents
Names and origin
| Protein names | Recommended name: 1-pyrroline-5-carboxylate dehydrogenase Short name=P5C dehydrogenase EC=1.5.1.12 | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain NCTC 8325) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 93061 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 514 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | (S)-1-pyrroline-5-carboxylate + NAD(P)+ + 2 H2O = L-glutamate + NAD(P)H. HAMAP MF_00733 |
| Pathway | Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2. HAMAP MF_00733 |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. RocA subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW proline biosynthetic processInferred from electronic annotation. Source: InterPro |
| Molecular function | 1-pyrroline-5-carboxylate dehydrogenase 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 – 514 | 514 | 1-pyrroline-5-carboxylate dehydrogenase HAMAP MF_00733 | PRO_1000045974 | |||||
Sites | |||||||||
| Active site | 286 | 1 | By similarity | ||||||
| Active site | 320 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "The Staphylococcus aureus NCTC8325 genome." Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000253 Genomic DNA. Translation: ABD31868.1. |
| RefSeq | YP_501325.1. |
3D structure databases | |
| ProteinModelPortal | Q2FV67. |
| SMR | Q2FV67. Positions 2-514. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q2FV67. |
Genome annotation databases | |
| EnsemblBacteria | EBSTAT00000029452; EBSTAP00000028403; EBSTAG00000029450. |
| GeneID | 3921541. |
| GenomeReviews | Gene locus SAOUHSC_02869 in contig CP000253_GR. |
| KEGG | sao:SAOUHSC_02869. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1012. |
| HOGENOM | HBG752218. |
| OMA | SINPANT. |
| ProtClustDB | PRK03137. |
Enzyme and pathway databases | |
| BioCyc | SAUR93061:SAOUHSC_02869-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00733. RocA. [Tree] |
| InterPro | IPR016161. Ald_DH/histidinol_DH. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. IPR005932. d-1-pyrroline-5-COlate_DH-2. [Graphical view] |
| Gene3D | G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit. |
| PANTHER | PTHR11699. Aldehyde_dehyd. 1 hit. |
| Pfam | PF00171. Aldedh. 1 hit. [Graphical view] |
| SUPFAM | SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit. |
| TIGRFAMs | TIGR01237. D1pyr5carbox2. 1 hit. |
| PROSITE | PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ROCA_STAA8 | ||||||||
| Accession | Primary (citable) accession number: Q2FV67 | ||||||||
| 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 |

Clusters with


