Q9PKF7 (FABG_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Names 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

Name:	fabG
Ordered Locus Names:	TC_0508

Organism

Chlamydia muridarum (strain MoPn / Nigg) [Complete proteome] [HAMAP]

Taxonomic identifier

243161 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Chlamydiae/Verrucomicrobia group › Chlamydiae › Chlamydiia › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia › Chlamydia muridarum

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	Lipid metabolism; fatty acid biosynthesis.
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
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 NAD binding Inferred 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 – 248	248	3-oxoacyl-[acyl-carrier-protein] reductase FabG		PRO_0000054669
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

Sequences

	Sequence		Length	Mass (Da)
	Q9PKF7 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 1F5C8968CB05FF58	FASTA	248	25,977
	10 20 30 40 50 60 MNSLLVNKAA IVTGGSRGIG FGIAKLFAEH GANVQIWGIN EEAGKSAAQD LSDKTGSKVS 70 80 90 100 110 120 FALVDVSKND MVSAQVQKFL AEYGTIDVVV NNAGITRDSL LMRMSEEEWS SVIDTNLGSI 130 140 150 160 170 180 YNVCSAVIRP MIKARSGAIV NISSIVGLRG SPGQTNYAAA KAGIIGFSKA LSKEVGSKNI 190 200 210 220 230 240 RVNCIAPGFI DTDMTKGLSD NLKNEWLKGV PLGRVGTPEE IAMAALFLAS NQSSYITGQV LSVDGGMA

References

[1]

"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M. Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MoPn / Nigg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002160 Genomic DNA. Translation: AAF39350.1.
PIR	E81695.
RefSeq	NP_296885.1. NC_002620.2.
3D structure databases
ProteinModelPortal	Q9PKF7.
ModBase	Search...
Protein-protein interaction databases
STRING	243161.TC0508.
Proteomic databases
PRIDE	Q9PKF7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF39350; AAF39350; TC_0508.
GeneID	1245868.
KEGG	cmu:TC0508.
PATRIC	20372460. VBIChlMur19118_0546.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1028.
KO	K00059.
OMA	CIAPGCI.
ProtClustDB	PRK05653.
Enzyme and pathway databases
BioCyc	CMUR243161:GHYU-501-MONOMER.
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_CHLMU

Accession

Primary (citable) accession number: Q9PKF7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program