Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0A6Q3 (FABA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_00405
Chain2 – 1721713-hydroxydecanoyl-[acyl-carrier-protein] dehydratase HAMAP-Rule MF_00405
PRO_0000091594

Sites

Active site711

Natural variations

Natural variant761P → L in allele FABA6; TS.
Natural variant1021G → D in allele FABA2; TS.

Secondary structure

............................ 172
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6Q3 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DFC508352D2DCF2C

FASTA17218,969
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 277:1453-1462(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.
PIRDWECHD. A64836.
RefSeqNP_415474.1. NC_000913.3.
YP_489226.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MKAX-ray2.00A/B2-172[»]
1MKBX-ray2.00A/B2-172[»]
4KEHX-ray1.90A/B2-172[»]
ProteinModelPortalP0A6Q3.
SMRP0A6Q3. Positions 2-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31864N.
IntActP0A6Q3. 29 interactions.
MINTMINT-1218658.
STRING511145.b0954.

Proteomic databases

PaxDbP0A6Q3.
PRIDEP0A6Q3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74040; AAC74040; b0954.
BAA35712; BAA35712; BAA35712.
GeneID12934245.
945568.
KEGGecj:Y75_p0926.
eco:b0954.
PATRIC32117127. VBIEscCol129921_0988.

Organism-specific databases

EchoBASEEB0269.
EcoGeneEG10273. fabA.

Phylogenomic databases

eggNOGCOG0764.
HOGENOMHOG000277828.
KOK01716.
OMAMGIADAT.
OrthoDBEOG6VB6SH.
PhylomeDBP0A6Q3.

Enzyme and pathway databases

BioCycEcoCyc:FABA-MONOMER.
ECOL316407:JW0937-MONOMER.
MetaCyc:FABA-MONOMER.
BRENDA5.3.3.14. 2026.
UniPathwayUPA00094.

Gene expression databases

GenevestigatorP0A6Q3.

Family and domain databases

Gene3D3.10.129.10. 1 hit.
HAMAPMF_00405. FabA.
InterProIPR010083. FabA.
IPR013114. FabA_FabZ.
IPR029069. HotDog_dom.
[Graphical view]
PfamPF07977. FabA. 1 hit.
[Graphical view]
SUPFAMSSF54637. SSF54637. 1 hit.
TIGRFAMsTIGR01749. fabA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A6Q3.
PROP0A6Q3.

Entry information

Entry nameFABA_ECOLI
AccessionPrimary (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: June 11, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene