Reviewed, UniProtKB/Swiss-Prot P57432 (FABG_BUCAI)

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

Name:	fabG
Ordered Locus Names:	BU351

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]

Taxonomic identifier

118099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	244 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	Lipid metabolism; fatty acid biosynthesis.
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 reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-oxoacyl-[acyl-carrier-protein] reductase activity Inferred from electronic annotation. Source: EC NAD or NADH 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 – 244	244	3-oxoacyl-[acyl-carrier-protein] reductase		PRO_0000054666
Regions
	Nucleotide binding	10 – 34	25	NADP By similarity
Sites
	Active site	151	1	Proton acceptor By similarity
	Binding site	138	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57432-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: A6A9AC8ACEADCE66	FASTA	244	26,894
	10 20 30 40 50 60 MNINRQTAFI TGANQGIGKA IAKKLIKKGI QVIGTSTTED GVKRINDYLE GNGFGFVLNL 70 80 90 100 110 120 KNIDSITEKI QEIYKKKHSI DILINNAGIK EDNLLVNMKS TEWDDVIKTN LSSVFHLVKS 130 140 150 160 170 180 VIRSMIKKRQ GRIITIGSVI AYTGNKGQVN YSASKSGLIG FHKSLALEVA SKGITVNIVS 190 200 210 220 230 240 PGLIKTNFTE KLNSIQYQKY LSNIPMKRFG QKEEVADAVI FLASKKASYI TGHTLHVNGG MYMI

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tokyo 1998.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000003 Genomic DNA. Translation: BAB13055.1.
RefSeq	NP_240169.1.
3D structure databases
HSSP	HSSP built from PDB template 1E7W based on UniProtKB Q01782.
ModBase	Search...
Genome annotation databases
GeneID	1110047.
GenomeReviews	Gene locus BU351 in contig BA000003_GR.
KEGG	buc:BU351.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P57432.
OMA	NDYLEGN.
Enzyme and pathway databases
BioCyc	BSP107806:BU351-MON.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FABG_BUCAI

Accession

Primary (citable) accession number: P57432

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)