O54438 (FABG_PSEAE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 79.
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: 3-oxoacyl-[acyl-carrier-protein] reductase FabG EC=1.1.1.100 Alternative name(s): 3-ketoacyl-acyl carrier protein reductase Beta-Ketoacyl-acyl carrier protein reductase Beta-ketoacyl-ACP reductase | ||||
| Gene names |
| ||||
| Organism | Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) | ||||
| Taxonomic identifier | 208964 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 247 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis By similarity. |
| Catalytic activity | (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Inferred from electronic annotation. Source: EC NAD 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 – 247 | 247 | 3-oxoacyl-[acyl-carrier-protein] reductase FabG | PRO_0000054678 | |||||
Regions | |||||||||
| Nucleotide binding | 12 – 15 | 4 | NADP By similarity | ||||||
| Nucleotide binding | 62 – 63 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 154 – 158 | 5 | NADP By similarity | ||||||
Sites | |||||||||
| Active site | 154 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 37 | 1 | NADP By similarity | ||||||
| Binding site | 89 | 1 | NADP; via carbonyl oxygen By similarity | ||||||
| Binding site | 141 | 1 | Substrate By similarity | ||||||
| Binding site | 187 | 1 | NADP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of a Pseudomonas aeruginosa fatty acid biosynthetic gene cluster: purification of acyl carrier protein (ACP) and malonyl-coenzyme A:ACP transacylase (fabD)." Kutchma A.J., Hoang T.T., Schweizer H.P. J. Bacteriol. 181:5498-5504(1999) [PubMed: 10464226] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228. |
| [2] | "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. Olson M.V.Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U91631 Genomic DNA. Translation: AAB94395.1. AE004091 Genomic DNA. Translation: AAG06355.1. |
| PIR | T12020. |
| RefSeq | NP_251657.1. NC_002516.2. |
3D structure databases | |
| ProteinModelPortal | O54438. |
| SMR | O54438. Positions 2-246. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 880433. |
| GenomeReviews | Gene locus PA2967 in contig AE004091_GR. |
| KEGG | pae:PA2967. |
| PATRIC | 19840487. VBIPseAer58763_3113. |
Organism-specific databases | |
| PseudoCAP | PA2967. |
Phylogenomic databases | |
| HOGENOM | HBG750976. |
| OMA | DNLMLRM. |
| ProtClustDB | PRK05653. |
Enzyme and pathway databases | |
| BioCyc | PAER208964:PA2967-MONOMER. |
Family and domain databases | |
| InterPro | IPR011284. 3oxo_ACP_reduc. IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K00059. |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PRINTS | PR00081. GDHRDH. PR00080. SDRFAMILY. |
| TIGRFAMs | TIGR01830. 3oxo_ACP_reduc. 1 hit. |
| PROSITE | PS00061. ADH_SHORT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FABG_PSEAE | ||||||||
| Accession | Primary (citable) accession number: O54438 | ||||||||
| 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 |

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