Q89AG9 (FABG_BUCBP) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 70.
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 | Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 224915 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › ![]() |
Protein attributes
| Sequence length | 245 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. |
| Miscellaneous | Calcium ions stabilize the structure, and may inhibit FabG activity by obstructing access to the active site By similarity. |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism |
| Ligand | Calcium Metal-binding NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW 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 – 245 | 245 | 3-oxoacyl-[acyl-carrier-protein] reductase FabG | PRO_0000054668 | |||||
Regions | |||||||||
| Nucleotide binding | 12 – 15 | 4 | NADP By similarity | ||||||
| Nucleotide binding | 60 – 61 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 152 – 156 | 5 | NADP By similarity | ||||||
Sites | |||||||||
| Active site | 152 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 51 | 1 | Calcium 1; via carbonyl oxygen; shared with dimeric partner By similarity | ||||||
| Metal binding | 54 | 1 | Calcium 1; via carbonyl oxygen; shared with dimeric partner By similarity | ||||||
| Metal binding | 146 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 234 | 1 | Calcium 3; shared with dimeric partner By similarity | ||||||
| Metal binding | 235 | 1 | Calcium 3; via carbonyl oxygen; shared with dimeric partner By similarity | ||||||
| Binding site | 38 | 1 | NADP By similarity | ||||||
| Binding site | 87 | 1 | NADP; via carbonyl oxygen By similarity | ||||||
| Binding site | 139 | 1 | Substrate By similarity | ||||||
| Binding site | 185 | 1 | NADP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
Sequences
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References
| [1] | "Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bp. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016826 Genomic DNA. Translation: AAO27043.1. |
| RefSeq | NP_777938.1. NC_004545.1. |
3D structure databases | |
| ProteinModelPortal | Q89AG9. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224915.bbp321. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAO27043; AAO27043; bbp_321. |
| GeneID | 1058479. |
| KEGG | bab:bbp321. |
| PATRIC | 21245431. VBIBucAph80364_0315. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1028. |
| KO | K00059. |
| OMA | ISNDANY. |
Enzyme and pathway databases | |
| BioCyc | BAPH224915:GJ9D-321-MONOMER. |
| UniPathway | UPA00094. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| InterPro | IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view] |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PRINTS | PR00081. GDHRDH. PR00080. SDRFAMILY. |
| PROSITE | PS00061. ADH_SHORT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FABG_BUCBP | ||||||||
| Accession | Primary (citable) accession number: Q89AG9 | ||||||||
| 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 |

Clusters with
