P99093 (FABG_STAAN) 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:	SA1074

Organism

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

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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 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 binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred 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 – 246	246	3-oxoacyl-[acyl-carrier-protein] reductase FabG		PRO_0000054685
Regions
	Nucleotide binding	11 – 14	4	NADP By similarity
	Nucleotide binding	62 – 63	2	NADP By similarity
	Nucleotide binding	154 – 158	5	NADP By similarity
Sites
	Active site	154	1	Proton acceptor By similarity
	Binding site	89	1	NADP; via carbonyl oxygen By similarity
	Binding site	141	1	Substrate By similarity
	Binding site	187	1	NADP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P99093 [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: N315.
[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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: N315.
[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 [LARGE SCALE ANALYSIS]. Strain: N315.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D85817 Genomic DNA. Translation: BAB20935.2. BA000018 Genomic DNA. Translation: BAB42326.1.
PIR	B89896.
RefSeq	NP_374347.1. NC_002745.2.
3D structure databases
ProteinModelPortal	P99093.
SMR	P99093. Positions 1-246.
ModBase	Search...
Protein-protein interaction databases
STRING	158879.SA1074.
2D gel databases
SWISS-2DPAGE	P99093.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB42326; BAB42326; BAB42326.
GeneID	1123905.
KEGG	sau:SA1074.
PATRIC	19574368. VBIStaAur116463_1153.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1028.
KO	K00059.
OMA	MSKAVMR.
ProtClustDB	CLSK885220.
Enzyme and pathway databases
BioCyc	SAUR158879:GJCB-1134-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]
Pfam	PF00106. adh_short. 1 hit. [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_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:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program