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Protein

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

Gene

fabA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.1 Publication
(3R)-3-hydroxydecanoyl-[acyl-carrier-protein] = trans-dec-2-enoyl-[acyl-carrier-protein] + H2O.1 Publication
Trans-dec-2-enoyl-[acyl-carrier-protein] = cis-dec-3-enoyl-[acyl-carrier-protein].1 Publication

Pathway: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711

GO - Molecular functioni

  • 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity Source: EcoCyc
  • 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: EcoCyc
  • trans-2-decenoyl-acyl-carrier-protein isomerase activity Source: EcoCyc

GO - Biological processi

  • fatty acid biosynthetic process Source: EcoCyc
  • lipid biosynthetic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciEcoCyc:FABA-MONOMER.
ECOL316407:JW0937-MONOMER.
MetaCyc:FABA-MONOMER.
BRENDAi5.3.3.14. 2026.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
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 namesi
Name:fabA
Ordered Locus Names:b0954, JW0937
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10273. fabA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 1721713-hydroxydecanoyl-[acyl-carrier-protein] dehydratasePRO_0000091594Add
BLAST

Proteomic databases

PaxDbiP0A6Q3.
PRIDEiP0A6Q3.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-31864N.
IntActiP0A6Q3. 29 interactions.
MINTiMINT-1218658.
STRINGi511145.b0954.

Structurei

Secondary structure

1
172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 178Combined sources
Beta strandi24 – 263Combined sources
Turni32 – 343Combined sources
Beta strandi38 – 469Combined sources
Turni48 – 514Combined sources
Beta strandi54 – 607Combined sources
Helixi66 – 705Combined sources
Turni71 – 744Combined sources
Helixi80 – 9718Combined sources
Beta strandi102 – 1109Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi124 – 15027Combined sources
Beta strandi153 – 16614Combined sources
Helixi169 – 1713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MKAX-ray2.00A/B2-172[»]
1MKBX-ray2.00A/B2-172[»]
4KEHX-ray1.90A/B2-172[»]
ProteinModelPortaliP0A6Q3.
SMRiP0A6Q3. Positions 2-167.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6Q3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0764.
HOGENOMiHOG000277828.
InParanoidiP0A6Q3.
KOiK01716.
OMAiFFDCHFK.
OrthoDBiEOG6VB6SH.
PhylomeDBiP0A6Q3.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
HAMAPiMF_00405. FabA.
InterProiIPR010083. FabA.
IPR013114. FabA_FabZ.
IPR029069. HotDog_dom.
[Graphical view]
PfamiPF07977. FabA. 1 hit.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 1 hit.
TIGRFAMsiTIGR01749. fabA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6Q3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDKRESYTK EDLLASGRGE LFGAKGPQLP APNMLMMDRV VKMTETGGNF
60 70 80 90 100
DKGYVEAELD INPDLWFFGC HFIGDPVMPG CLGLDAMWQL VGFYLGWLGG
110 120 130 140 150
EGKGRALGVG EVKFTGQVLP TAKKVTYRIH FKRIVNRRLI MGLADGEVLV
160 170
DGRLIYTASD LKVGLFQDTS AF
Length:172
Mass (Da):18,969
Last modified:January 23, 2007 - v2
Checksum:iDFC508352D2DCF2C
GO

Sequence cautioni

The sequence AAA96496.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761P → L in allele FABA6; TS.
Natural varianti102 – 1021G → D in allele FABA2; TS.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA64836. DWECHD.
RefSeqiNP_415474.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC74040; AAC74040; b0954.
BAA35712; BAA35712; BAA35712.
GeneIDi945568.
KEGGiecj:Y75_p0926.
eco:b0954.
PATRICi32117127. VBIEscCol129921_0988.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA64836. DWECHD.
RefSeqiNP_415474.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MKAX-ray2.00A/B2-172[»]
1MKBX-ray2.00A/B2-172[»]
4KEHX-ray1.90A/B2-172[»]
ProteinModelPortaliP0A6Q3.
SMRiP0A6Q3. Positions 2-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-31864N.
IntActiP0A6Q3. 29 interactions.
MINTiMINT-1218658.
STRINGi511145.b0954.

Proteomic databases

PaxDbiP0A6Q3.
PRIDEiP0A6Q3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74040; AAC74040; b0954.
BAA35712; BAA35712; BAA35712.
GeneIDi945568.
KEGGiecj:Y75_p0926.
eco:b0954.
PATRICi32117127. VBIEscCol129921_0988.

Organism-specific databases

EchoBASEiEB0269.
EcoGeneiEG10273. fabA.

Phylogenomic databases

eggNOGiCOG0764.
HOGENOMiHOG000277828.
InParanoidiP0A6Q3.
KOiK01716.
OMAiFFDCHFK.
OrthoDBiEOG6VB6SH.
PhylomeDBiP0A6Q3.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciEcoCyc:FABA-MONOMER.
ECOL316407:JW0937-MONOMER.
MetaCyc:FABA-MONOMER.
BRENDAi5.3.3.14. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A6Q3.
PROiP0A6Q3.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
HAMAPiMF_00405. FabA.
InterProiIPR010083. FabA.
IPR013114. FabA_FabZ.
IPR029069. HotDog_dom.
[Graphical view]
PfamiPF07977. FabA. 1 hit.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 1 hit.
TIGRFAMsiTIGR01749. fabA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. 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).

Entry informationi

Entry nameiFABA_ECOLI
AccessioniPrimary (citable) accession number: P0A6Q3
Secondary accession number(s): P18391, Q59383
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.