Q1RH28 (FABI_RICBR) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 60.
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 | Rickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 336407 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › belli group › ![]() |
Protein attributes
| Sequence length | 262 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 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 |
| Technical term | Complete proteome |
| 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 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 – 262 | 262 | Enoyl-[acyl-carrier-protein] reductase [NADH] FabI | PRO_0000286635 | |||||
Regions | |||||||||
| Nucleotide binding | 21 – 22 | 2 | NAD By similarity | ||||||
| Nucleotide binding | 66 – 67 | 2 | NAD By similarity | ||||||
| Nucleotide binding | 193 – 197 | 5 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 147 | 1 | Proton acceptor By similarity | ||||||
| Active site | 157 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 15 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 42 | 1 | NAD By similarity | ||||||
| Binding site | 94 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 97 | 1 | Substrate; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 164 | 1 | NAD By similarity | ||||||
| Site | 205 | 1 | Involved in acyl-ACP binding By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens." Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D. PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RML369-C. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000087 Genomic DNA. Translation: ABE05336.1. |
| RefSeq | YP_538425.1. NC_007940.1. |
3D structure databases | |
| ProteinModelPortal | Q1RH28. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 336407.RBE_1255. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABE05336; ABE05336; RBE_1255. |
| GeneID | 3995181. |
| KEGG | rbe:RBE_1255. |
| PATRIC | 17884136. VBIRicBel102610_1417. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0623. |
| KO | K00208. |
| OMA | LVHCLAF. |
| ProtClustDB | PRK06603. |
Enzyme and pathway databases | |
| BioCyc | RBEL336407:GJCY-1292-MONOMER. |
| UniPathway | UPA00094. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| InterPro | IPR014358. Enoyl-ACP_Rdtase_NADH. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| PIRSF | PIRSF000094. Enoyl-ACP_rdct. 1 hit. |
| PRINTS | PR00081. GDHRDH. |
| ProtoNet | Search... |
Entry information
| Entry name | FABI_RICBR | ||||||||
| Accession | Primary (citable) accession number: Q1RH28 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Rickettsia bellii strain RML369-C Rickettsia bellii (strain RML369-C): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
