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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

Enzyme regulationi

Irreversibly inactivated by 3-decynoyl-N-acetylcysteamine (DNAC) which binds to the active site and forms an adduct (PubMed:21276098).1 Publication

Pathwayi: 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)DescriptionActionsGraphical viewLength
Active sitei711 Publication1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10273. fabA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000915942 – 1723-hydroxydecanoyl-[acyl-carrier-protein] dehydrataseAdd BLAST171

Proteomic databases

EPDiP0A6Q3.
PaxDbiP0A6Q3.
PRIDEiP0A6Q3.

Expressioni

Inductioni

Mainly activated by FadR, but minor repression is also conferred by FabR (PubMed:11859088, PubMed:21276098).2 Publications

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4263239. 209 interactors.
DIPiDIP-31864N.
IntActiP0A6Q3. 29 interactors.
MINTiMINT-1218658.
STRINGi511145.b0954.

Structurei

Secondary structure

1172
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 17Combined sources8
Beta strandi24 – 26Combined sources3
Turni32 – 34Combined sources3
Beta strandi38 – 46Combined sources9
Turni48 – 51Combined sources4
Beta strandi54 – 60Combined sources7
Helixi66 – 70Combined sources5
Turni71 – 74Combined sources4
Helixi80 – 97Combined sources18
Beta strandi102 – 110Combined sources9
Beta strandi112 – 114Combined sources3
Beta strandi124 – 150Combined sources27
Beta strandi153 – 166Combined sources14
Helixi169 – 171Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0A6Q3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108RKI. Bacteria.
COG0764. LUCA.
HOGENOMiHOG000277828.
InParanoidiP0A6Q3.
KOiK01716.
OMAiFFDCHFK.
PhylomeDBiP0A6Q3.

Family and domain databases

CDDicd01287. FabA. 1 hit.
Gene3Di3.10.129.10. 1 hit.
HAMAPiMF_00405. FabA. 1 hit.
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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti76P → L in allele FABA6; TS. 1
Natural varianti102G → D in allele FABA2; TS. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03186 Genomic DNA. Translation: AAA96496.1.
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.
WP_000227927.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74040; AAC74040; b0954.
BAA35712; BAA35712; BAA35712.
GeneIDi945568.
KEGGiecj:JW0937.
eco:b0954.
PATRICi32117127. VBIEscCol129921_0988.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03186 Genomic DNA. Translation: AAA96496.1.
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.
WP_000227927.1. NZ_LN832404.1.

3D structure databases

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

Protein-protein interaction databases

BioGridi4263239. 209 interactors.
DIPiDIP-31864N.
IntActiP0A6Q3. 29 interactors.
MINTiMINT-1218658.
STRINGi511145.b0954.

Proteomic databases

EPDiP0A6Q3.
PaxDbiP0A6Q3.
PRIDEiP0A6Q3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74040; AAC74040; b0954.
BAA35712; BAA35712; BAA35712.
GeneIDi945568.
KEGGiecj:JW0937.
eco:b0954.
PATRICi32117127. VBIEscCol129921_0988.

Organism-specific databases

EchoBASEiEB0269.
EcoGeneiEG10273. fabA.

Phylogenomic databases

eggNOGiENOG4108RKI. Bacteria.
COG0764. LUCA.
HOGENOMiHOG000277828.
InParanoidiP0A6Q3.
KOiK01716.
OMAiFFDCHFK.
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

CDDicd01287. FabA. 1 hit.
Gene3Di3.10.129.10. 1 hit.
HAMAPiMF_00405. FabA. 1 hit.
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...

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: November 2, 2016
This is version 105 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

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 one 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.