Reviewed,
UniProtKB/Swiss-Prot P71079 (FABL_BACSU)
Last modified
November 3, 2009.
Version 61.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Enoyl-[acyl-carrier-protein] reductase [NADPH] EC=1.3.1.10 Alternative name(s): Enoyl-acyl carrier protein reductase III NADPH-dependent enoyl-ACP reductase | ||||||
| Gene names |
| ||||||
| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 250 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] + NADP+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH. Ref.5 |
| Enzyme regulation | Inhibited by triclosan. Ref.5 |
| Induction | Expressed during exponential growth. Ref.4 |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
| Biophysicochemical properties | Kinetic parameters: KM=16 µM for NADPH |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) 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 – 250 | 250 | Enoyl-[acyl-carrier-protein] reductase [NADPH] | PRO_0000377006 | |||||
Regions | |||||||||
| Nucleotide binding | 10 – 17 | 8 | NADP By similarity | ||||||
Sites | |||||||||
| Active site | 151 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 141 | 1 | Substrate By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and sequencing of a 27.8-kb nucleotide sequence of the 79 degrees-81 degrees region of the Bacillus subtilis genome containing the sspE locus." Yamamoto H., Uchiyama S., Sekiguchi J. DNA Res. 3:257-262(1996) [PubMed: 8946165] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The Bacillus subtilis 168 chromosome from sspE to katA." Cummings N.J., Connerton I.F. Microbiology 143:1855-1859(1997) [PubMed: 9202460] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [3] | "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. |
| [4] | "Transcription of genes near the sspE locus of the Bacillus subtilis genome." Yamamoto H., Mori M., Sekiguchi J. Microbiology 145:2171-2180(1999) [PubMed: 10463184] [Abstract] Cited for: INDUCTION. Strain: 168. |
| [5] | "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. |
| [6] | "Crystallization and preliminary X-ray crystallographic analysis of enoyl-ACP reductase III (FabL) from Bacillus subtilis." Kim K.-H., Park J.K., Ha B.H., Moon J.H., Kim E.E. Acta Crystallogr. F 63:246-248(2007) [PubMed: 17329825] [Abstract] Cited for: CRYSTALLIZATION. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| D85082 Genomic DNA. Translation: BAA24484.1. Z82044 Genomic DNA. Translation: CAB04808.1. AL009126 Genomic DNA. Translation: CAB12693.1. | |
| PIR | B69802. |
| RefSeq | NP_388745.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1E7W based on UniProtKB Q01782. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 939223. |
| GenomeReviews | Gene locus BSU08650 in contig AL009126_GR. |
| KEGG | bsu:BSU08650. |
| NMPDR | fig|224308.1.peg.864. |
Organism-specific databases | |
| SubtiList | BG12221. fabL. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P71079. |
| OMA | RPLMELE. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU0864-MON. |
Family and domain databases | |
| InterPro | IPR002198. DH_sc/Rdtase_SDR. 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. |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PRINTS | PR00081. GDHRDH. PR00080. SDRFAMILY. |
| PROSITE | PS00061. ADH_SHORT. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FABL_BACSU | ||||||||
| Accession | Primary (citable) accession number: P71079 Secondary accession number(s): Q796Z2 | ||||||||
| 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 |
| SIMILARITY comments Index of protein domains and families |

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