P0A6Q3 (FABA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
EC=4.2.1.59

Alternative name(s):
3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA
Beta-hydroxydecanoyl thioester dehydrase
Trans-2-decenoyl-[acyl-carrier-protein] isomerase
EC=5.3.3.14

Gene names

Name:	fabA
Ordered Locus Names:	b0954, JW0937

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	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. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. Is inactive in the dehydration of long chain unsaturated beta-hydroxyacyl-ACP. Ref.7
Catalytic activity	A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O. Ref.7 (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] = trans-dec-2-enoyl-[acyl-carrier-protein] + H2O. Ref.7 Trans-dec-2-enoyl-[acyl-carrier-protein] = cis-dec-3-enoyl-[acyl-carrier-protein]. Ref.7
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_00405
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP-Rule 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 Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Molecular function	Isomerase 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 PubMed 19679654. 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: HAMAP 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Inferred from electronic annotation. Source: EC trans-2-decenoyl-acyl-carrier-protein isomerase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed HAMAP-Rule MF_00405

Chain

2 – 172

171

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

Helix

169 – 171

3

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: MUTANTS FABA6 AND FABA2. Strain: K12.
[7]	"Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis." Heath R.J., Rock C.O. J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
[8]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[9]	"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] [Europe PMC] [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.
YP_489226.1. NC_007779.1.

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.

STRING

511145.b0954.

Proteomic databases

PaxDb

P0A6Q3.

PRIDE

P0A6Q3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74040; AAC74040; b0954.
BAA35712; BAA35712; BAA35712.

GeneID

12934245.
945568.

KEGG

ecj:Y75_p0926.
eco:b0954.

PATRIC

32117127. VBIEscCol129921_0988.

Organism-specific databases

EchoBASE

EB0269.

EcoGene

EG10273. fabA.

Phylogenomic databases

eggNOG

COG0764.

HOGENOM

HOG000277828.

KO

K01716.

OMA

KGRAIST.

ProtClustDB

PRK05174.

Enzyme and pathway databases

BioCyc

EcoCyc:FABA-MONOMER.
ECOL316407:JW0937-MONOMER.
MetaCyc:FABA-MONOMER.

BRENDA

5.3.3.14. 2026.

UniPathway

UPA00094.

Gene expression databases

Genevestigator

P0A6Q3.

Family and domain databases

HAMAP

MF_00405. FabA.

InterPro

IPR010083. FabA.
IPR013114. FabA_FabZ.
[Graphical view]

Pfam

PF07977. FabA. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01749. fabA. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A6Q3.

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:	May 1, 2013
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program