P38004 (FABG_CHLTR) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 88.
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 | Chlamydia trachomatis (strain D/UW-3/Cx) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 272561 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia › ![]() |
Protein attributes
| Sequence length | 248 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 Fatty acid metabolism Lipid biosynthesis Lipid metabolism |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | fatty acid elongation Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Inferred from sequence or structural similarity. Source: UniProtKB NAD bindingInferred from electronic annotation. Source: InterPro NADP bindingInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 248 | 248 | 3-oxoacyl-[acyl-carrier-protein] reductase FabG | PRO_0000054671 | |||||
Regions | |||||||||
| Nucleotide binding | 14 – 17 | 4 | NADP By similarity | ||||||
| Nucleotide binding | 65 – 66 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 157 – 161 | 5 | NADP By similarity | ||||||
Sites | |||||||||
| Active site | 157 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 92 | 1 | NADP; via carbonyl oxygen By similarity | ||||||
| Binding site | 144 | 1 | Substrate By similarity | ||||||
| Binding site | 190 | 1 | NADP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 3 | 1 | G → T in AAC67830. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis." Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W. Science 282:754-759(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: D/UW-3/Cx. |
| [2] | Bini L., Santucci A., Magi B., Marzocchi B., Sanchez-Campillo M., Comanducci M., Christianen G., Birkelund S., Vtretou E., Ratti G., Pallini V. Submitted (SEP-1994) to UniProtKB Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11. Strain: L2/434/Bu. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE001273 Genomic DNA. Translation: AAC67830.1. |
| PIR | F71538. |
| RefSeq | NP_219742.1. NC_000117.1. |
3D structure databases | |
| ProteinModelPortal | P38004. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 272561.CT237. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAC67830; AAC67830; CT_237. |
| GeneID | 884887. |
| KEGG | ctr:CT237. |
| PATRIC | 20379991. VBIChlTra43535_0254. |
Phylogenomic databases | |
| eggNOG | COG1028. |
| KO | K00059. |
| OMA | CIAPGCI. |
| ProtClustDB | PRK05653. |
Enzyme and pathway databases | |
| UniPathway | UPA00094. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| 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] |
| PIRSF | PIRSF000126. 11-beta-HSD1. 1 hit. |
| 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_CHLTR | ||||||||
| Accession | Primary (citable) accession number: P38004 Secondary accession number(s): O84240 | ||||||||
| 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
