Reviewed, UniProtKB/Swiss-Prot P99093 (FABG_STAAN)

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:	SA1074

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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 – 246	246	3-oxoacyl-[acyl-carrier-protein] reductase		PRO_0000054685
Regions
	Nucleotide binding	9 – 34	26	NADP By similarity
Sites
	Active site	154	1	Proton acceptor By similarity
	Binding site	141	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P99093-1 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: 2BD7CA319D3A37C5	FASTA	246	26,146
	10 20 30 40 50 60 MKMTKSALVT GASRGIGRSI ALQLAEEGYN VAVNYAGSKE KAEAVVEEIK AKGVDSFAIQ 70 80 90 100 110 120 ANVADADEVK AMIKEVVSQF GSLDVLVNNA GITRDNLLMR MKEQEWDDVI DTNLKGVFNC 130 140 150 160 170 180 IQKATPQMLR QRSGAIINLS SVVGAVGNPG QANYVATKAG VIGLTKSAAR ELASRGITVN 190 200 210 220 230 240 AVAPGFIVSD MTDALSDELK EQMLTQIPLA RFGQDTDIAN TVAFLASDKA KYITGQTIHV NGGMYM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Eagle-type methicillin resistance: new phenotype of high methicillin resistance under mec regulator gene control." Kondo N., Kuwahara-Arai K., Kuroda-Murakami H., Tateda-Suzuki E., Hiramatsu K. Antimicrob. Agents Chemother. 45:815-824(2001) [PubMed: 11181367] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth." Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J. J. Microbiol. Methods 60:247-257(2005) [PubMed: 15590099] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[4]	"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D85817 Genomic DNA. Translation: BAB20935.2. BA000018 Genomic DNA. Translation: BAB42326.1.
PIR	B89896.
RefSeq	NP_374347.1.
3D structure databases
HSSP	HSSP built from PDB template 1EDO based on UniProtKB Q93X62.
ModBase	Search...
Protein-protein interaction databases
STRING	P99093.
2-D gel databases
SWISS-2DPAGE	P99093.
Genome annotation databases
GeneID	1123905.
GenomeReviews	Gene locus SA1074 in contig BA000018_GR.
KEGG	sau:SA1074.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P99093.
OMA	DEDWLAV.
Enzyme and pathway databases
BioCyc	SAUR158879:SA1074-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_STAAN

Accession

Primary (citable) accession number: P99093
Secondary accession number(s): Q99QK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	November 3, 2009
This is version 33 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)