C3TAP2 (C3TAP2_ECOLX) Unreviewed, UniProtKB/TrEMBL
Last modified
January 25, 2012.
Version 22.
History...
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Gamma-aminobutyraldehyde dehydrogenase 1 HAMAP MF_01275 EC=1.2.1.19 HAMAP MF_01275 Alternative name(s): 1-pyrroline dehydrogenase 1 HAMAP MF_01275 4-aminobutanal dehydrogenase 1 HAMAP MF_01275 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli EMBL ACI83776.1 | ||||
| Taxonomic identifier | 562 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 474 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the oxidation of 1-pyrroline, which is spontaneously formed from 4-aminobutanal, leading to 4-aminobutanoate (GABA) By similarity. HAMAP MF_01275 |
| Catalytic activity | 4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH. HAMAP MF_01275 |
| Pathway | Amine and polyamine degradation; putrescine degradation; 4-aminobutanoate from 4-aminobutanal: step 1/1. HAMAP MF_01275 |
| Subunit structure | Homotetramer By similarity. HAMAP MF_01275 |
| Miscellaneous | 4-aminobutanal is also called gamma-aminobutyraldehyde By similarity. HAMAP MF_01275 |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. Gamma-aminobutyraldehyde dehydrogenase subfamily. HAMAP MF_01275 |
Ontologies
| Keywords | |
|---|---|
| Ligand | NAD HAMAP MF_01275 |
| Molecular function | Oxidoreductase RuleBase RU003344 HAMAP MF_01275 |
| Gene Ontology (GO) | |
| Biological process | putrescine catabolic process Inferred from electronic annotation. Source: HAMAP |
| Molecular function | 1-pyrroline dehydrogenase activity Inferred from electronic annotation. Source: EC NAD bindingInferred from electronic annotation. Source: HAMAP aminobutyraldehyde dehydrogenase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequences
| ||||||||||||||||||
References
| [1] | "A precise reconstruction of the emergence and constrained radiations of Escherichia coli O157 portrayed by backbone concatenomic analysis." Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J., Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E., Sawyer S.A., Whittam T.S., Tarr P.I. Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009) [PubMed: 19439656] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: 493/89 EMBL ACI83776.1, 86-24 EMBL ACI83777.1, 87-14 EMBL ACI83778.1 and TW14359 EMBL ACI83780.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | EU901230 Genomic DNA. Translation: ACI83776.1. EU901231 Genomic DNA. Translation: ACI83777.1. EU901232 Genomic DNA. Translation: ACI83778.1. EU901234 Genomic DNA. Translation: ACI83780.1. |
3D structure databases | |
| ProteinModelPortal | C3TAP2. |
| SMR | C3TAP2. Positions 1-474. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| HAMAP | MF_01275. Aldedh_Prr. [Tree] |
| InterPro | IPR017749. 1-pyrroline_dehydrogenase. IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit. |
| Pfam | PF00171. Aldedh. 1 hit. [Graphical view] |
| SUPFAM | SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit. |
| TIGRFAMs | TIGR03374. ABALDH. 1 hit. |
| PROSITE | PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | C3TAP2_ECOLX | ||||||||
| Accession | Primary (citable) accession number: C3TAP2 | ||||||||
| Entry history |
| ||||||||
| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with