Reviewed, UniProtKB/Swiss-Prot P0AEK4 (FABI_ECOLI)

Names and originHide

Protein names

Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH]
EC=1.3.1.9

Alternative name(s):
NADH-dependent enoyl-ACP reductase

Gene names

Name:	fabI
Synonyms:	envM
Ordered Locus Names:	b1288, JW1281

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributesHide

Sequence length	262 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)Hide

Catalytic activity	Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homotetramer.
Subcellular location	Cell inner membrane; Peripheral membrane protein.
Miscellaneous	The antibiotic diazaborine interferes with the activity by binding to the protein.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.

OntologiesHide

Keywords
Biological process	Antibiotic resistance Fatty acid biosynthesis Lipid synthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
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 response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	enoyl-[acyl-carrier-protein] reductase (NADH) activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactionsHide

With	Entry	#Exp.	IntAct	Notes
yjgD	P0AF90	1	EBI-370029,EBI-544031

Sequence annotation (Features)Hide

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1 Ref.7 Ref.8

Chain

2 – 262

261

Enoyl-[acyl-carrier-protein] reductase [NADH]

PRO_0000054899

Regions

Nucleotide binding

10 – 36

27

NAD By similarity

Sites

Active site

156

1

Proton acceptor By similarity

Experimental info

Mutagenesis

93

1

G → S: Diazaborine resistance.

Mutagenesis

241

1

S → F: Produces temperature-sensitive phenotype.

Secondary structure

1

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262

Helix Strand Turn

Details...

Turn

3 – 6

4

Beta strand

8 – 11

4

Helix

20 – 30

11

Beta strand

34 – 41

8

Turn

42 – 44

3

Helix

45 – 54

10

Beta strand

60 – 62

3

Helix

68 – 79

12

Beta strand

83 – 90

8

Helix

97 – 100

4

Helix

104 – 107

4

Helix

110 – 120

11

Helix

122 – 131

10

Helix

132 – 134

3

Beta strand

135 – 145

11

Helix

147 – 149

3

Turn

154 – 157

4

Helix

158 – 177

20

Helix

178 – 180

3

Beta strand

182 – 189

8

Helix

197 – 199

3

Helix

203 – 213

11

Helix

222 – 232

11

Helix

235 – 237

3

Beta strand

244 – 248

5

Helix

251 – 253

3

SequencesHide

	Sequence		Length	Mass (Da)
	P0AEK4-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 436A89AF349D1866	FASTA	262	27,864
	10 20 30 40 50 60 MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE FAAQLGSDIV 70 80 90 100 110 120 LQCDVAEDAS IDTMFAELGK VWPKFDGFVH SIGFAPGDQL DGDYVNAVTR EGFKIAHDIS 130 140 150 160 170 180 SYSFVAMAKA CRSMLNPGSA LLTLSYLGAE RAIPNYNVMG LAKASLEANV RYMANAMGPE 190 200 210 220 230 240 GVRVNAISAG PIRTLAASGI KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI 250 260 SGEVVHVDGG FSIAAMNELE LK

ReferencesHide

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequences of the envM gene and of two mutated alleles in Escherichia coli." Bergler H., Hoegenauer G., Turnowsky F. J. Gen. Microbiol. 138:2093-2100(1992) [PubMed: 1364817] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31, MUTAGENESIS.
[2]	"The use of a hybrid genetic system to study the functional relationship between prokaryotic and plant multi-enzyme fatty acid synthetase complexes." Kater M.M., Koningstein G.M., Nijkamp H.J.J., Stuitje A.R. Plant Mol. Biol. 25:771-790(1994) [PubMed: 8075395] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Protein EnvM is the NADH-dependent enoyl-ACP reductase (FabI) of Escherichia coli." Bergler H., Wallner P., Ebeling A., Leitinger B., Fuchsbichler S., Aschauer H., Kollenz G., Hoegenauer G., Turnowsky F. J. Biol. Chem. 269:5493-5496(1994) [PubMed: 8119879] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
[7]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[8]	Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F. Submitted (FEB-1996) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]	"A mechanism of drug action revealed by structural studies of enoyl reductase." Baldock C., Rafferty J.B., Sedelnikova S.E., Baker P.J., Stuitje A.R., Slabas A.R., Hawkes T.R., Rice D.W. Science 274:2107-2110(1996) [PubMed: 8953047] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[10]	"Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan." Ward W.H., Holdgate G.A., Rowsell S., McLean E.G., Pauptit R.A., Clayton E., Nichols W.W., Colls J.G., Minshull C.A., Jude D.A., Mistry A., Timms D., Camble R., Hales N.J., Britton C.J., Taylor I.W. Biochemistry 38:12514-12525(1999) [PubMed: 10493822] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[11]	"Structural basis and mechanism of enoyl reductase inhibition by triclosan." Stewart M.J., Parikh S., Xiao G., Tonge P.J., Kisker C. J. Mol. Biol. 290:859-865(1999) [PubMed: 10398587] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
[12]	"Molecular basis of triclosan activity." Levy C.W., Roujeinikova A., Sedelnikova S., Baker P.J., Stuitje A.R., Slabas A.R., Rice D.W., Rafferty J.B. Nature 398:383-384(1999) [PubMed: 10201369] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ

M97219 Unassigned DNA. Translation: AAA17755.1.
X78733 Genomic DNA. Translation: CAA55381.1.
U00096 Genomic DNA. Translation: AAC74370.1.
AP009048 Genomic DNA. Translation: BAA14841.1.

PIR

S48029.

RefSeq

AP_001914.1.
NP_415804.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C14	X-ray	2.00	A/B	1-262	[»]
1D8A	X-ray	2.20	A/B	2-262	[»]
1DFG	X-ray	2.50	A/B	2-262	[»]
1DFH	X-ray	2.20	A/B	2-262	[»]
1DFI	X-ray	2.09	A/B/C/D	2-262	[»]
1I2Z	X-ray	2.80	A/B	1-262	[»]
1I30	X-ray	2.40	A/B	1-262	[»]
1LX6	X-ray	2.40	A/B	1-262	[»]
1LXC	X-ray	2.40	A/B	1-262	[»]
1MFP	X-ray	2.33	A/B	1-262	[»]
1QG6	X-ray	1.90	A/B/C/D	2-262	[»]
1QSG	X-ray	1.75	A/B/C/D/E/F/G/H	1-262	[»]
2FHS	X-ray	2.70	A/B	1-262	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31867N.

IntAct

P0AEK4. 12 interactions.

MINT

MINT-1251203.

STRING

P0AEK4.

2-D gel databases

SWISS-2DPAGE

P0AEK4.

Genome annotation databases

EnsemblBacteria

EBESCT00000000533; EBESCP00000000533; EBESCG00000000449.
EBESCT00000014396; EBESCP00000013687; EBESCG00000013457.

GeneID

945870.

GenomeReviews

Gene locus JW1281 in contig AP009048_GR.
Gene locus b1288 in contig U00096_GR.

KEGG

ecj:JW1281.
eco:b1288.

Organism-specific databases

EchoBASE

EB1490.

EcoGene

EG11528. fabI.

CMR

Search...

Phylogenomic databases

eggNOG

COG0623.

HOGENOM

HBG750976.

OMA

DCDVGSD.

ProtClustDB

PRK07984.

Enzyme and pathway databases

BioCyc

EcoCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
ECOL168927:B1288-MONOMER.
MetaCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.

Gene expression databases

Genevestigator

P0AEK4.

Family and domain databases

InterPro

IPR002198. DH_sc/Rdtase_SDR.
IPR014358. Enoyl-ACP_Rdtase_NADH.
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.
PTHR19410:SF12. Enoyl-ACP_rdct. 1 hit.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.

ProtoNet

Search...

Other Resources

BindingDB

P0AEK4.

Entry informationHide

Entry name

FABI_ECOLI

Accession

Primary (citable) accession number: P0AEK4
Secondary accession number(s): P29132

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 23, 2007
Last modified:	July 13, 2010
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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