P0AEK2 (FABG_ECOLI) 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:	b1093, JW1079

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	244 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. Ref.7 Ref.8
Catalytic activity	(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH. Ref.7
Enzyme regulation	Inhibited by cinnamic acid derivatives. Ref.9
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homotetramer. Ref.10 Ref.11
Miscellaneous	Calcium ions stabilize the structure, and may inhibit FabG activity by obstructing access to the active site.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Biophysicochemical properties	pH dependence: Optimum pH is between 6.0 and 7.0. Ref.6

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Ligand	Calcium Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	biotin biosynthetic process Inferred from mutant phenotype PubMed 20693992. Source: EcoCyc fatty acid elongation Inferred from mutant phenotype Ref.8. Source: UniProtKB
Molecular_function	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Inferred from mutant phenotype Ref.8. Source: UniProtKB NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from direct assay Ref.11. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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 FabG

PRO_0000054672

Regions

Nucleotide binding

12 – 15

4

NADP

Nucleotide binding

59 – 60

2

NADP

Nucleotide binding

151 – 155

5

NADP

Sites

Active site

151

1

Proton acceptor By similarity

Metal binding

50

1

Calcium 1; via carbonyl oxygen; shared with dimeric partner

Metal binding

53

1

Calcium 1; via carbonyl oxygen; shared with dimeric partner

Metal binding

145

1

Calcium 2

Metal binding

233

1

Calcium 3; shared with dimeric partner

Metal binding

234

1

Calcium 3; via carbonyl oxygen; shared with dimeric partner

Binding site

37

1

NADP

Binding site

86

1

NADP; via carbonyl oxygen

Binding site

138

1

Substrate By similarity

Binding site

184

1

NADP; via amide nitrogen and carbonyl oxygen

Experimental info

Mutagenesis

151

1

Y → F: Defect in the affinity for NADPH. Ref.11

Mutagenesis

154

1

A → T: Decreases in the thermolability of the reductase; when associated with K-233. Ref.8

Mutagenesis

155

1

K → A: Defect in the affinity for NADPH. Ref.11

Mutagenesis

233

1

E → K: Decreases in the thermolability of the reductase; when associated with T-154. Ref.8

Sequence conflict

30

1

A → G in AAA23739. Ref.1

Sequence conflict

43

1

Q → R in AAA23739. Ref.1

Secondary structure

1

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244

Helix Strand Turn

Details...

Beta strand

7 – 12

6

Helix

16 – 27

12

Beta strand

31 – 38

8

Helix

39 – 49

11

Helix

50 – 52

3

Beta strand

53 – 57

5

Helix

63 – 76

14

Beta strand

81 – 85

5

Helix

95 – 97

3

Helix

100 – 110

11

Helix

112 – 128

17

Beta strand

131 – 136

6

Helix

139 – 143

5

Helix

149 – 169

21

Helix

170 – 172

3

Beta strand

174 – 181

8

Helix

187 – 190

4

Helix

194 – 201

8

Helix

212 – 223

12

Helix

225 – 227

3

Beta strand

234 – 238

5

Sequences

	Sequence		Length	Mass (Da)
	P0AEK2 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 48EC1F2A7F7EEFD9	FASTA	244	25,560
	10 20 30 40 50 60 MNFEGKIALV TGASRGIGRA IAETLAARGA KVIGTATSEN GAQAISDYLG ANGKGLMLNV 70 80 90 100 110 120 TDPASIESVL EKIRAEFGEV DILVNNAGIT RDNLLMRMKD EEWNDIIETN LSSVFRLSKA 130 140 150 160 170 180 VMRAMMKKRH GRIITIGSVV GTMGNGGQAN YAAAKAGLIG FSKSLAREVA SRGITVNVVA 190 200 210 220 230 240 PGFIETDMTR ALSDDQRAGI LAQVPAGRLG GAQEIANAVA FLASDEAAYI TGETLHVNGG MYMV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes." Rawlings M., Cronan J.E. Jr. J. Biol. Chem. 267:5751-5754(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], NOMENCLATURE. Strain: K12.
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Cloning, nucleotide sequence, and expression of the Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl carrier protein transacylase." Verwoert I.I.G.S., Verbree E.C., van der Linden K.H., Nijkamp H.J., Stuitje A.R. J. Bacteriol. 174:2851-2857(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45. Strain: K12.
[6]	"Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of beta-ketoacyl acyl carrier protein reductase from Escherichia coli." Toomey R.E., Wakil S.J. Biochim. Biophys. Acta 116:189-197(1966) [PubMed] [Europe PMC] [Abstract] Cited for: SUBSTRATES SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[7]	"Inhibition of beta-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli." Heath R.J., Rock C.O. J. Biol. Chem. 271:10996-11000(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A BETA-KETOACYL-ACP REDUCTASE, CATALYTIC ACTIVITY.
[8]	"Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium." Lai C.Y., Cronan J.E. J. Bacteriol. 186:1869-1878(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN FATTY ACID BIOSYNTHESIS AND AS A BETA-KETOACYL-ACP REDUCTASE, MUTAGENESIS OF ALA-154 AND GLU-233.
[9]	"Novel inhibitors of beta-ketoacyl-ACP reductase from Escherichia coli." Kristan K., Bratkovic T., Sova M., Gobec S., Prezelj A., Urleb U. Chem. Biol. Interact. 178:310-316(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[10]	"Structure of beta-ketoacyl-[acyl carrier-protein] reductase from Escherichia coli: negative cooperativity and its structural basis." Price A.C., Zhang Y.-M., Rock C.O., White S.W. Biochemistry 40:12772-12781(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT.
[11]	"Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG." Price A.C., Zhang Y.M., Rock C.O., White S.W. Structure 12:417-428(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH NADP, MUTAGENESIS OF TYR-151 AND LYS-155, REACTION MECHANISM, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M84991 Genomic DNA. Translation: AAA23739.1.
U00096 Genomic DNA. Translation: AAC74177.1.
AP009048 Genomic DNA. Translation: BAA35901.1.
M87040 Genomic DNA. Translation: AAA23743.1.

PIR

B42147. B64853.

RefSeq

NP_415611.1. NC_000913.2.
YP_489361.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I01	X-ray	2.60	A/B/C/D/E/F/G/H	1-244	[»]
1Q7B	X-ray	2.05	A/B/C/D	1-244	[»]
1Q7C	X-ray	2.50	A/B	1-244	[»]

ProteinModelPortal

P0AEK2.

SMR

P0AEK2. Positions 2-244.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31869N.

IntAct

P0AEK2. 6 interactions.

MINT

MINT-1232516.

STRING

511145.b1093.

Proteomic databases

PaxDb

P0AEK2.

PRIDE

P0AEK2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74177; AAC74177; b1093.
BAA35901; BAA35901; BAA35901.

GeneID

12931086.
945645.

KEGG

ecj:Y75_p1063.
eco:b1093.

PATRIC

32117427. VBIEscCol129921_1136.

Organism-specific databases

EchoBASE

EB1294.

EcoGene

EG11318. fabG.

Phylogenomic databases

eggNOG

COG1028.

KO

K00059.

OMA

GMELNVT.

ProtClustDB

PRK05557.

Enzyme and pathway databases

BioCyc

EcoCyc:3-OXOACYL-ACP-REDUCT-MONOMER.
ECOL316407:JW1079-MONOMER.
MetaCyc:3-OXOACYL-ACP-REDUCT-MONOMER.

UniPathway

UPA00094.

Gene expression databases

Genevestigator

P0AEK2.

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]

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

TIGRFAMs

TIGR01830. 3oxo_ACP_reduc. 1 hit.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AEK2.

Entry information

Entry name

FABG_ECOLI

Accession

Primary (citable) accession number: P0AEK2
Secondary accession number(s): P25716, P78221, Q47202

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program