P43713 (FABG_HAEIN) 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:	HI_0155

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	242 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 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 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 – 242	242	3-oxoacyl-[acyl-carrier-protein] reductase FabG		PRO_0000054673
Regions
	Nucleotide binding	10 – 13	4	NADP By similarity
	Nucleotide binding	57 – 58	2	NADP By similarity
	Nucleotide binding	149 – 153	5	NADP By similarity
Sites
	Active site	149	1	Proton acceptor By similarity
	Binding site	35	1	NADP By similarity
	Binding site	84	1	NADP; via carbonyl oxygen By similarity
	Binding site	136	1	Substrate By similarity
	Binding site	182	1	NADP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43713 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: B3DE2E2C020D2F71	FASTA	242	25,507
	10 20 30 40 50 60 MQGKIALVTG STRGIGRAIA EELSSKGAFV IGTATSEKGA EAISAYLGDK GKGLVLNVTD 70 80 90 100 110 120 KESIETLLEQ IKNDFGDIDI LVNNAGITRD NLLMRMKDEE WFDIMQTNLT SVYHLSKAML 130 140 150 160 170 180 RSMMKKRFGR IINIGSVVGS TGNPGQTNYC AAKAGVVGFS KSLAKEVAAR GITVNVVAPG 190 200 210 220 230 240 FIATDMTEVL TDEQKAGILS NVPAGRLGEA KDIAKAVAFL ASDDAGYITG TTLHVNGGLY LS

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC21824.1.
PIR	D64051.
RefSeq	NP_438325.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P43713.
SMR	P43713. Positions 2-241.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI0155.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC21824; AAC21824; HI_0155.
GeneID	951066.
KEGG	hin:HI0155.
PATRIC	20188805. VBIHaeInf48452_0159.
Phylogenomic databases
eggNOG	COG1028.
KO	K00059.
OMA	QSNYCAA.
ProtClustDB	PRK05557.
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]
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_HAEIN

Accession

Primary (citable) accession number: P43713

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program