P57353 (FABI_BUCAI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 68.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Enoyl-[acyl-carrier-protein] reductase [NADH] FabI Short name=ENR EC=1.3.1.9 Alternative name(s): NADH-dependent enoyl-ACP reductase | ||||
| Gene names |
| ||||
| Organism | Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) | ||||
| Taxonomic identifier | 107806 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera |
Protein attributes
| Sequence length | 260 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis By similarity. |
| Catalytic activity | Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Biotin biosynthesis Fatty acid biosynthesis Lipid synthesis |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | biotin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW fatty acid elongationInferred from sequence or structural similarity. Source: UniProtKB protein homotetramerizationInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | enoyl-[acyl-carrier-protein] reductase (NADH) activity Inferred from sequence or structural similarity. Source: UniProtKB nucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 260 | 260 | Enoyl-[acyl-carrier-protein] reductase [NADH] FabI | PRO_0000054896 | |||||
Regions | |||||||||
| Nucleotide binding | 19 – 20 | 2 | NAD By similarity | ||||||
| Nucleotide binding | 64 – 65 | 2 | NAD By similarity | ||||||
| Nucleotide binding | 192 – 194 | 3 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 146 | 1 | Proton acceptor By similarity | ||||||
| Active site | 156 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 13 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 40 | 1 | NAD By similarity | ||||||
| Binding site | 92 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 163 | 1 | NAD By similarity | ||||||
| Site | 204 | 1 | Involved in acyl-ACP binding By similarity | ||||||
| Site | 205 | 1 | Involved in acyl-ACP binding By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000003 Genomic DNA. Translation: BAB12975.1. |
| RefSeq | NP_240089.1. NC_002528.1. |
3D structure databases | |
| ProteinModelPortal | P57353. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBUCT00000003298; EBBUCP00000003074; EBBUCG00000003298. |
| GeneID | 1109704. |
| GenomeReviews | Gene locus BU265 in contig BA000003_GR. |
| KEGG | buc:BU265. |
| PATRIC | 21244054. VBIBucAph127364_0275. |
Phylogenomic databases | |
| GeneTree | EBGT00050000007854. |
| HOGENOM | HBG750976. |
| OMA | DCDVGSD. |
| PhylomeDB | P57353. |
| ProtClustDB | CLSK315843. |
Enzyme and pathway databases | |
| BioCyc | BSP107806:BU265-MONOMER. |
Family and domain databases | |
| InterPro | IPR002198. DH_sc/Rdtase_SDR. IPR014358. Enoyl-ACP_Rdtase_NADH. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K00208. |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PIRSF | PIRSF000094. Enoyl-ACP_rdct. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | FABI_BUCAI | ||||||||
| Accession | Primary (citable) accession number: P57353 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Buchnera aphidicola (subsp. Acyrthosiphon pisum) Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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