B5XWU5 (B5XWU5_KLEP3) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 27.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Gamma-aminobutyraldehyde dehydrogenase HAMAP MF_01275 EC=1.2.1.19 HAMAP MF_01275 Alternative name(s): 1-pyrroline dehydrogenase HAMAP MF_01275 4-aminobutanal dehydrogenase HAMAP MF_01275 | ||||||
| Gene names |
| ||||||
| Organism | Klebsiella pneumoniae (strain 342) [Complete proteome] [HAMAP] EMBL ACI11654.1 | ||||||
| Taxonomic identifier | 507522 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella |
Protein attributes
| Sequence length | 475 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 HAMAP MF_01275 EMBL ACI11654.1 |
| Technical term | Complete proteome |
| 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... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Nucleotide binding | 172 – 175 | 4 | NAD By similarity HAMAP MF_01275 | ||||||
| Nucleotide binding | 225 – 231 | 7 | NAD By similarity HAMAP MF_01275 | ||||||
Sites | |||||||||
| Active site | 246 | 1 | By similarity HAMAP MF_01275 | ||||||
| Active site | 280 | 1 | Nucleophile By similarity HAMAP MF_01275 | ||||||
| Binding site | 146 | 1 | NAD; via carbonyl oxygen By similarity HAMAP MF_01275 | ||||||
| Binding site | 209 | 1 | NAD By similarity HAMAP MF_01275 | ||||||
Sequences
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References
| [1] | "Complete genome sequence of the N2-fixing broad host range endophyte Klebsiella pneumoniae 342 and virulence predictions verified in mice." Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H., Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y., Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W., Methe B.A. PLoS Genet. 4:E1000141-E1000141(2008) [PubMed: 18654632] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000964 Genomic DNA. Translation: ACI11654.1. |
| RefSeq | YP_002238259.1. NC_011283.1. |
3D structure databases | |
| ProteinModelPortal | B5XWU5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B5XWU5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 6934957. |
| GenomeReviews | Gene locus KPK_2428 in contig CP000964_GR. |
| KEGG | kpe:KPK_2428. |
| PATRIC | 20438286. VBIKlePne121904_2515. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG752218. |
| OMA | CRIYAQQ. |
| ProtClustDB | PRK13473. |
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. |
| KO | K00137. |
| 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 | B5XWU5_KLEP3 | ||||||||
| Accession | Primary (citable) accession number: B5XWU5 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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