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P0A6Q3

- FABA_ECOLI

UniProt

P0A6Q3 - FABA_ECOLI

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Protein
3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
Gene
fabA, b0954, JW0937
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Pathwayi

Sites

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

GO - Molecular functioni

  1. 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity Source: EcoCyc
  2. 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: EcoCyc
  3. trans-2-decenoyl-acyl-carrier-protein isomerase activity Source: EcoCyc

GO - Biological processi

  1. fatty acid biosynthetic process Source: EcoCyc
  2. 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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10273. fabA.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 1721713-hydroxydecanoyl-[acyl-carrier-protein] dehydrataseUniRule annotation
PRO_0000091594Add
BLAST

Proteomic databases

PaxDbiP0A6Q3.
PRIDEiP0A6Q3.

Expressioni

Gene expression databases

GenevestigatoriP0A6Q3.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP0A6Q3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0764.
HOGENOMiHOG000277828.
KOiK01716.
OMAiMGIADAT.
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

MVDKRESYTK EDLLASGRGE LFGAKGPQLP APNMLMMDRV VKMTETGGNF    50
DKGYVEAELD INPDLWFFGC HFIGDPVMPG CLGLDAMWQL VGFYLGWLGG 100
EGKGRALGVG EVKFTGQVLP TAKKVTYRIH FKRIVNRRLI MGLADGEVLV 150
DGRLIYTASD LKVGLFQDTS AF 172
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.

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:
EMBL
GenBank
DDBJ
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.
YP_489226.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74040; AAC74040; b0954.
BAA35712; BAA35712; BAA35712.
GeneIDi12934245.
945568.
KEGGiecj:Y75_p0926.
eco:b0954.
PATRICi32117127. VBIEscCol129921_0988.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A64836. DWECHD.
RefSeqi NP_415474.1. NC_000913.3.
YP_489226.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4KEH X-ray 1.90 A/B 2-172 [» ]
ProteinModelPortali P0A6Q3.
SMRi P0A6Q3. Positions 2-167.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-31864N.
IntActi P0A6Q3. 29 interactions.
MINTi MINT-1218658.
STRINGi 511145.b0954.

Proteomic databases

PaxDbi P0A6Q3.
PRIDEi P0A6Q3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74040 ; AAC74040 ; b0954 .
BAA35712 ; BAA35712 ; BAA35712 .
GeneIDi 12934245.
945568.
KEGGi ecj:Y75_p0926.
eco:b0954.
PATRICi 32117127. VBIEscCol129921_0988.

Organism-specific databases

EchoBASEi EB0269.
EcoGenei EG10273. fabA.

Phylogenomic databases

eggNOGi COG0764.
HOGENOMi HOG000277828.
KOi K01716.
OMAi MGIADAT.
OrthoDBi EOG6VB6SH.
PhylomeDBi P0A6Q3.

Enzyme and pathway databases

UniPathwayi UPA00094 .
BioCyci EcoCyc:FABA-MONOMER.
ECOL316407:JW0937-MONOMER.
MetaCyc:FABA-MONOMER.
BRENDAi 5.3.3.14. 2026.

Miscellaneous databases

EvolutionaryTracei P0A6Q3.
PROi P0A6Q3.

Gene expression databases

Genevestigatori P0A6Q3.

Family and domain databases

Gene3Di 3.10.129.10. 1 hit.
HAMAPi MF_00405. FabA.
InterProi IPR010083. FabA.
IPR013114. FabA_FabZ.
IPR029069. HotDog_dom.
[Graphical view ]
Pfami PF07977. FabA. 1 hit.
[Graphical view ]
SUPFAMi SSF54637. SSF54637. 1 hit.
TIGRFAMsi TIGR01749. fabA. 1 hit.
ProtoNeti Search...

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 11, 2014
This is version 90 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

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