Reviewed,
UniProtKB/Swiss-Prot P54616 (FABI_BACSU)
Last modified
June 16, 2009.
Version 69.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Enoyl-[acyl-carrier-protein] reductase [NADH] EC=1.3.1.9 Alternative name(s): NADH-dependent enoyl-ACP reductase Cold shock-induced protein 15 Short name=CSI15 Vegetative protein 241 Short name=VEG241 | ||||||
| Gene names |
| ||||||
| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 258 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH. |
| Enzyme regulation | Inhibited by triclosan. |
| Pathway | |
| Induction | By cold shock. |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily. |
| biophysicochemical properties | Kinetic parameters: KM=7 µM for NADH |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis Stress response |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW response to stressInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro enoyl-[acyl-carrier-protein] reductase (NADH) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 258 | 258 | Enoyl-[acyl-carrier-protein] reductase [NADH] | PRO_0000054895 | |||||
Regions | |||||||||
| Nucleotide binding | 11 – 37 | 27 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 158 | 1 | Proton acceptor By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 20 | 1 | S → Q AA sequence Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.  Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [2] | "Cold shock stress-induced proteins in Bacillus subtilis." Graumann P., Schroeder K., Schmid R., Marahiel M.A. J. Bacteriol. 178:4611-4619(1996) [PubMed: 8755892] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21. Strain: 168 / JH642. |
| [3] | "First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis." Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M. Electrophoresis 18:1451-1463(1997) [PubMed: 9298659] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15. Strain: 168 / IS58. |
| [4] | "The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis." Heath R.J., Su N., Murphy C.K., Rock C.O. J. Biol. Chem. 275:40128-40133(2000) [PubMed: 11007778] [Abstract] Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. |
Cross-references
Sequence databases | |
|---|---|
| AL009126 Genomic DNA. Translation: CAB13029.2. | |
| PIR | G69845. |
| RefSeq | NP_389054.2. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1DFI based on UniProtKB P29132. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 939379. |
| GenomeReviews | Gene locus BSU11720 in contig AL009126_GR. |
| KEGG | bsu:BSU11720. |
| NMPDR | fig|224308.1.peg.1173. |
Organism-specific databases | |
| SubtiList | BG13152. fabI. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P54616. |
| OMA | P54616. LVHCLAF. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU1173-MON. |
| BRENDA | 1.3.1.9. 150. |
Family and domain databases | |
| InterPro | IPR002198. DH_sc/Rdtase_SDR. IPR014358. Enoyl-ACP_Rdtase_NADH. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| PANTHER | PTHR19410. ADH_short_C2. 1 hit. PTHR19410:SF12. Enoyl-ACP_rdct. 1 hit. |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PRINTS | PR00081. GDHRDH. |
| ProtoNet | Search... |
Entry information
| Entry name | FABI_BACSU | ||||||||
| Accession | Primary (citable) accession number: P54616 Secondary accession number(s): O31621 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
