Q9X450 (FABI_RHIML) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
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 | Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti) | ||
| Taxonomic identifier | 382 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium![]() |
Protein attributes
| Sequence length | 55 AA. |
| Sequence status | Fragment. |
| 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 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 | Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological_process | fatty acid elongation Inferred 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 |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›55 | ›55 | Enoyl-[acyl-carrier-protein] reductase [NADH] FabI | PRO_0000054907 | |||||
Regions | |||||||||
| Nucleotide binding | 26 – 27 | 2 | NAD By similarity | ||||||
Sites | |||||||||
| Binding site | 20 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 55 | 1 | |||||||
Sequences
References
| [1] | "Genes coding for phosphotransacetylase and acetate kinase in Sinorhizobium meliloti are in an operon that is inducible by phosphate stress and controlled by phoB." Summers M.L., Denton M.C., McDermott T.R. J. Bacteriol. 181:2217-2224(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 104A14. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF095903 Genomic DNA. Translation: AAD24359.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| UniPathway | UPA00094. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| InterPro | IPR016040. NAD(P)-bd_dom. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FABI_RHIML | ||||||||
| Accession | Primary (citable) accession number: Q9X450 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
