P0A6Q3 (FABA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
EC=4.2.1.60

Alternative name(s):
Beta-hydroxydecanoyl thioester dehydrase

Gene names

Name:	fabA
Ordered Locus Names:	b0954, JW0937

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	172 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)

Function	Necessary for the introduction of cis unsaturation into fatty acids. Catalyzed the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. HAMAP MF_00405
Catalytic activity	(3R)-3-hydroxydecanoyl-[acyl-carrier-protein] = trans-dec-2-enoyl-[acyl-carrier-protein] + H2O. HAMAP MF_00405 (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] = cis-dec-3-enoyl-[acyl-carrier-protein] + H2O.
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP MF_00405
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP MF_00405.
Sequence similarities	Belongs to the thioester dehydratase family. FabA subfamily.
Sequence caution	The sequence AAA96496.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from genetic interaction. Source: EcoliWiki
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed HAMAP MF_00405

Chain

2 – 172

171

3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase HAMAP MF_00405

PRO_0000091594

Sites

Active site

71

1

Natural variations

Natural variant

76

1

P → L in allele FABA6; TS.

Natural variant

102

1

G → D in allele FABA2; TS.

Secondary structure

1

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172

Helix Strand Turn

Details...

Helix

10 – 17

8

Beta strand

24 – 26

3

Turn

32 – 34

3

Beta strand

38 – 46

9

Turn

48 – 51

4

Beta strand

54 – 60

7

Helix

66 – 69

4

Turn

70 – 74

5

Helix

80 – 97

18

Beta strand

102 – 110

9

Beta strand

112 – 114

3

Beta strand

124 – 150

27

Beta strand

153 – 167

15

Sequences

	Sequence		Length	Mass (Da)
	P0A6Q3 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: DFC508352D2DCF2C	FASTA	172	18,969
	10 20 30 40 50 60 MVDKRESYTK EDLLASGRGE LFGAKGPQLP APNMLMMDRV VKMTETGGNF DKGYVEAELD 70 80 90 100 110 120 INPDLWFFGC HFIGDPVMPG CLGLDAMWQL VGFYLGWLGG EGKGRALGVG EVKFTGQVLP 130 140 150 160 170 TAKKVTYRIH FKRIVNRRLI MGLADGEVLV DGRLIYTASD LKVGLFQDTS AF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Derived amino acid sequence and identification of active site residues of Escherichia coli beta-hydroxydecanoyl thioester dehydrase." Cronan J.E. Jr., Li W.-B., Coleman R., Narasimhan M., de Mendoza D., Schwab J.M. J. Biol. Chem. 263:4641-4646(1988) [PubMed: 2832401] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12.
[2]	"A new mechanism of transcriptional regulation: release of an activator triggered by small molecule binding." Henry M.F., Cronan J.E. Jr. Cell 70:671-679(1992) [PubMed: 1505031] [Abstract] Cited for: SEQUENCE REVISION TO 170-172.
[3]	"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: 8905232] [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]	"Increased unsaturated fatty acid production associated with a suppressor of the fabA6(Ts) mutation in Escherichia coli." Rock C.O., Tsay J.-T., Heath R., Jackowski S. J. Bacteriol. 178:5382-5387(1996) [PubMed: 8808925] [Abstract] Cited for: MUTANTS FABA6 AND FABA2. Strain: K12.
[7]	"Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site." Leesong M., Henderson B.S., Gillig J.R., Schwab J.M., Smith J.L. Structure 4:253-264(1996) [PubMed: 8805534] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03186 Genomic DNA. Translation: AAA96496.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74040.1.
AP009048 Genomic DNA. Translation: BAA35712.1.
U37057 Genomic DNA. Translation: AAC44389.1.
U56977 Genomic DNA. Translation: AAC44399.1.

PIR

DWECHD. A64836.

RefSeq

NP_415474.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MKA	X-ray	2.00	A/B	2-172	[»]
1MKB	X-ray	2.00	A/B	2-172	[»]

ProteinModelPortal

P0A6Q3.

SMR

P0A6Q3. Positions 2-172.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31864N.

IntAct

P0A6Q3. 28 interactions.

MINT

MINT-1218658.

2D gel databases

ECO2DBASE

H017.2. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001221; EBESCP00000001221; EBESCG00000001007.
EBESCT00000015558; EBESCP00000014849; EBESCG00000014618.

GeneID

945568.

GenomeReviews

Gene locus JW0937 in contig AP009048_GR.
Gene locus b0954 in contig U00096_GR.

KEGG

ecj:JW0937.
eco:b0954.

PATRIC

32117127. VBIEscCol129921_0988.

Organism-specific databases

EchoBASE

EB0269.

EcoGene

EG10273. fabA.

Phylogenomic databases

eggNOG

COG0764.

GeneTree

EBGT00050000010541.

HOGENOM

HBG433282.

OMA

CHFKGDP.

PhylomeDB

P0A6Q3.

ProtClustDB

PRK05174.

Enzyme and pathway databases

BioCyc

EcoCyc:FABA-MONOMER.
MetaCyc:FABA-MONOMER.

BRENDA

5.3.3.14. 2026.

Gene expression databases

Genevestigator

P0A6Q3.

Family and domain databases

HAMAP

MF_00405. FabA.
[Tree]

InterPro

IPR000794. Beta-ketoacyl_synthase.
IPR010083. FabA.
IPR013114. FabA_FabZ.
[Graphical view]

KO

K01716.

PANTHER

PTHR11712. Ketoacyl_synth. 1 hit.

Pfam

PF07977. FabA. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01749. FabA. 1 hit.

ProtoNet

Search...

Entry information

Entry name

FABA_ECOLI

Accession

Primary (citable) accession number: P0A6Q3
Secondary accession number(s): P18391, Q59383

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program