Reviewed,
UniProtKB/Swiss-Prot P51831 (FABG_BACSU)
Last modified
November 3, 2009.
Version 67.
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: 3-oxoacyl-[acyl-carrier-protein] reductase EC=1.1.1.100 Alternative name(s): 3-ketoacyl-acyl carrier protein reductase | ||||||
| Gene names |
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| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 246 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH. |
| Pathway | |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
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 | 3-oxoacyl-[acyl-carrier-protein] reductase activity Inferred from electronic annotation. Source: EC NAD or NADH 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 – 246 | 246 | 3-oxoacyl-[acyl-carrier-protein] reductase | PRO_0000054665 | |||||
Regions | |||||||||
| Nucleotide binding | 9 – 33 | 25 | NADP By similarity | ||||||
Sites | |||||||||
| Active site | 154 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 141 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 23 | 1 | D → A in AAC44307. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Bacillus subtilis acyl carrier protein is encoded in a cluster of lipid biosynthesis genes." Morbidoni H.R., de Mendoza D., Cronan J.E. Jr. J. Bacteriol. 178:4794-4800(1996) [PubMed: 8759840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "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. |
| [3] | "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168 genome." Foulger D., Errington J. Microbiology 144:801-805(1998) [PubMed: 9534248] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-172. Strain: 168. |
| [4] | "The effect of Srb, a homologue of the mammalian SRP receptor alpha-subunit, on Bacillus subtilis growth and protein translocation." Oguro A., Kakeshita H., Takamatsu H., Nakamura K., Yamane K. Gene 172:17-24(1996) [PubMed: 8654983] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 230-246. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| U59433 Genomic DNA. Translation: AAC44307.1. AL009126 Genomic DNA. Translation: CAB13464.1. Y13937 Genomic DNA. Translation: CAA74250.1. D64116 Genomic DNA. Translation: BAA10974.1. | |
| PIR | A69621. |
| RefSeq | NP_389473.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1EDO based on UniProtKB Q93X62. |
| SMR | P51831. Positions 1-246. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 938113. |
| GenomeReviews | Gene locus BSU15910 in contig AL009126_GR. |
| KEGG | bsu:BSU15910. |
| NMPDR | fig|224308.1.peg.1593. |
Organism-specific databases | |
| SubtiList | BG11535. fabG. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P51831. |
| OMA | HIDGGMV. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU1592-MON. |
| BRENDA | 1.1.1.100. 150. |
Family and domain databases | |
| InterPro | IPR011284. 3oxo_ACP_reduc. 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. |
| TIGRFAMs | TIGR01830. 3oxo_ACP_reduc. 1 hit. |
| PROSITE | PS00061. ADH_SHORT. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FABG_BACSU | ||||||||
| Accession | Primary (citable) accession number: P51831 Secondary accession number(s): O31733 | ||||||||
| 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 |
