ID   FABA_ECOLI              Reviewed;         172 AA.
AC   P0A6Q3; P18391; Q59383;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   10-JUN-2026, entry version 155.
DE   RecName: Full=3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase;
DE            EC=4.2.1.59 {ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8910376};
DE   AltName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA;
DE   AltName: Full=Beta-hydroxydecanoyl thioester dehydrase;
DE   AltName: Full=Trans-2-decenoyl-[acyl-carrier-protein] isomerase;
DE            EC=5.3.3.14 {ECO:0000269|PubMed:8910376};
GN   Name=fabA; OrderedLocusNames=b0954, JW0937;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=K12;
RX   PubMed=2832401; DOI=10.1016/s0021-9258(18)68830-1;
RA   Cronan J.E. Jr., Li W.-B., Coleman R., Narasimhan M., de Mendoza D.,
RA   Schwab J.M.;
RT   "Derived amino acid sequence and identification of active site residues of
RT   Escherichia coli beta-hydroxydecanoyl thioester dehydrase.";
RL   J. Biol. Chem. 263:4641-4646(1988).
RN   [2]
RP   SEQUENCE REVISION TO 170-172.
RX   PubMed=1505031; DOI=10.1016/0092-8674(92)90435-f;
RA   Henry M.F., Cronan J.E. Jr.;
RT   "A new mechanism of transcriptional regulation: release of an activator
RT   triggered by small molecule binding.";
RL   Cell 70:671-679(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=7592873; DOI=10.1074/jbc.270.44.26538;
RA   Heath R.J., Rock C.O.;
RT   "Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in
RT   completing cycles of fatty acid elongation in Escherichia coli.";
RL   J. Biol. Chem. 270:26538-26542(1995).
RN   [7]
RP   MUTANTS FABA6 AND FABA2.
RC   STRAIN=K12;
RX   PubMed=8808925; DOI=10.1128/jb.178.18.5382-5387.1996;
RA   Rock C.O., Tsay J.-T., Heath R., Jackowski S.;
RT   "Increased unsaturated fatty acid production associated with a suppressor
RT   of the fabA6(Ts) mutation in Escherichia coli.";
RL   J. Bacteriol. 178:5382-5387(1996).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=8910376; DOI=10.1074/jbc.271.44.27795;
RA   Heath R.J., Rock C.O.;
RT   "Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein
RT   dehydratases in Escherichia coli fatty acid biosynthesis.";
RL   J. Biol. Chem. 271:27795-27801(1996).
RN   [9]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [10]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10629181; DOI=10.1128/jb.182.2.365-370.2000;
RA   Choi K.-H., Heath R.J., Rock C.O.;
RT   "Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining
RT   factor in branched-chain fatty acid biosynthesis.";
RL   J. Bacteriol. 182:365-370(2000).
RN   [11]
RP   INDUCTION.
RX   PubMed=11859088; DOI=10.1074/jbc.m201399200;
RA   Zhang Y.-M., Marrakchi H., Rock C.O.;
RT   "The FabR (YijC) transcription factor regulates unsaturated fatty acid
RT   biosynthesis in Escherichia coli.";
RL   J. Biol. Chem. 277:15558-15565(2002).
RN   [12]
RP   ACTIVITY REGULATION, ACTIVE SITE, AND INDUCTION.
RX   PubMed=21276098; DOI=10.1111/j.1365-2958.2011.07564.x;
RA   Feng Y., Cronan J.E.;
RT   "Complex binding of the FabR repressor of bacterial unsaturated fatty acid
RT   biosynthesis to its cognate promoters.";
RL   Mol. Microbiol. 80:195-218(2011).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=8805534; DOI=10.1016/s0969-2126(96)00030-5;
RA   Leesong M., Henderson B.S., Gillig J.R., Schwab J.M., Smith J.L.;
RT   "Structure of a dehydratase-isomerase from the bacterial pathway for
RT   biosynthesis of unsaturated fatty acids: two catalytic activities in one
RT   active site.";
RL   Structure 4:253-264(1996).
CC   -!- FUNCTION: Necessary for the introduction of cis unsaturation into fatty
CC       acids (PubMed:8910376). Catalyzes the dehydration of (3R)-3-
CC       hydroxydecanoyl-ACP to (2E)-decenoyl-ACP and then its isomerization to
CC       (3Z)-decenoyl-ACP (PubMed:8910376). Can catalyze the dehydratase
CC       reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to
CC       16:0, being most active on intermediate chain length (PubMed:10629181,
CC       PubMed:7592873, PubMed:8910376). Is inactive in the dehydration of long
CC       chain unsaturated beta-hydroxyacyl-ACP (PubMed:8910376).
CC       {ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873,
CC       ECO:0000269|PubMed:8910376}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC         Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873,
CC         ECO:0000269|PubMed:8910376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP];
CC         Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927,
CC         ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23569;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41808, Rhea:RHEA-COMP:9626, Rhea:RHEA-COMP:9627,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78451, ChEBI:CHEBI:78453;
CC         Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873,
CC         ECO:0000269|PubMed:8910376};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41809;
CC         Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873,
CC         ECO:0000269|PubMed:8910376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41828, Rhea:RHEA-COMP:9630, Rhea:RHEA-COMP:9631,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78457, ChEBI:CHEBI:78458;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41844, Rhea:RHEA-COMP:9634, Rhea:RHEA-COMP:9635,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78461, ChEBI:CHEBI:78462;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41845;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41876, Rhea:RHEA-COMP:9642, Rhea:RHEA-COMP:9643,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78470, ChEBI:CHEBI:78472;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41877;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] +
CC         H2O; Xref=Rhea:RHEA:41892, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9647,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78474, ChEBI:CHEBI:78475;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41893;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] +
CC         H2O; Xref=Rhea:RHEA:41908, Rhea:RHEA-COMP:9650, Rhea:RHEA-COMP:9651,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78480, ChEBI:CHEBI:78481;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41909;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxy-5-methylhexanoyl-[ACP] = (2E)-5-methylhexenoyl-
CC         [ACP] + H2O; Xref=Rhea:RHEA:55128, Rhea:RHEA-COMP:14095, Rhea:RHEA-
CC         COMP:14097, ChEBI:CHEBI:15377, ChEBI:CHEBI:78986, ChEBI:CHEBI:138610;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55129;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC   -!- ACTIVITY REGULATION: Irreversibly inactivated by 3-decynoyl-N-
CC       acetylcysteamine (DNAC) which binds to the active site and forms an
CC       adduct (PubMed:21276098). {ECO:0000305|PubMed:21276098}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Mainly activated by FadR, but minor repression is also
CC       conferred by FabR (PubMed:11859088, PubMed:21276098).
CC       {ECO:0000269|PubMed:11859088, ECO:0000269|PubMed:21276098}.
CC   -!- SIMILARITY: Belongs to the thioester dehydratase family. FabA
CC       subfamily. {ECO:0000305}.
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DR   EMBL; J03186; AAA96496.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74040.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35712.1; -; Genomic_DNA.
DR   EMBL; U37057; AAC44389.1; -; Genomic_DNA.
DR   EMBL; U56977; AAC44399.1; -; Genomic_DNA.
DR   PIR; A64836; DWECHD.
DR   RefSeq; NP_415474.1; NC_000913.3.
DR   RefSeq; WP_000227927.1; NZ_CP009789.1.
DR   PDB; 1MKA; X-ray; 2.00 A; A/B=2-172.
DR   PDB; 1MKB; X-ray; 2.00 A; A/B=2-172.
DR   PDB; 4KEH; X-ray; 1.90 A; A/B=2-172.
DR   AlphaFoldDB; P0A6Q3; -.
DR   SMR; P0A6Q3; -.
DR   BioGRID; 4263239; 222.
DR   BioGRID; 849942; 1.
DR   DIP; DIP-31864N; -.
DR   FunCoup; P0A6Q3; 291.
DR   IntAct; P0A6Q3; 30.
DR   STRING; 511145.b0954; -.
DR   DrugBank; DB03813; 2-Decenoyl N-acetyl cysteamine.
DR   SwissLipids; SLP:000001782; -.
DR   jPOST; P0A6Q3; -.
DR   PaxDb; 511145-b0954; -.
DR   EnsemblBacteria; AAC74040; AAC74040; b0954.
DR   GeneID; 67173067; -.
DR   GeneID; 93776460; -.
DR   GeneID; 945568; -.
DR   KEGG; ecj:JW0937; -.
DR   KEGG; eco:b0954; -.
DR   KEGG; ecoc:C3026_05835; -.
DR   PATRIC; fig|511145.12.peg.988; -.
DR   EchoBASE; EB0269; -.
DR   eggNOG; COG0764; Bacteria.
DR   HOGENOM; CLU_097925_0_0_6; -.
DR   InParanoid; P0A6Q3; -.
DR   OMA; FDCHFKG; -.
DR   OrthoDB; 9786735at2; -.
DR   PhylomeDB; P0A6Q3; -.
DR   BioCyc; EcoCyc:FABA-MONOMER; -.
DR   BioCyc; MetaCyc:FABA-MONOMER; -.
DR   BRENDA; 4.2.1.59; 2026.
DR   BRENDA; 5.3.3.14; 2026.
DR   UniPathway; UPA00094; -.
DR   EvolutionaryTrace; P0A6Q3; -.
DR   PRO; PR:P0A6Q3; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P0A6Q3; -.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0019171; F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; IDA:EcoCyc.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0034017; F:trans-2-decenoyl-acyl-carrier-protein isomerase activity; IDA:EcoCyc.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01287; FabA; 1.
DR   FunFam; 3.10.129.10:FF:000003; 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase; 1.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR   HAMAP; MF_00405; FabA; 1.
DR   InterPro; IPR010083; FabA.
DR   InterPro; IPR013114; FabA_FabZ.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   NCBIfam; TIGR01749; fabA; 1.
DR   NCBIfam; NF003509; PRK05174.1; 1.
DR   PANTHER; PTHR30272; 3-HYDROXYACYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE; 1.
DR   PANTHER; PTHR30272:SF8; 3-HYDROXYDECANOYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE; 1.
DR   Pfam; PF07977; FabA; 1.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
DR   PDBsum; 1MKA; -.
DR   PDBsum; 1MKB; -.
DR   PDBsum; 4KEH; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Isomerase;
KW   Lipid biosynthesis; Lipid metabolism; Lyase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..172
FT                   /note="3-hydroxydecanoyl-[acyl-carrier-protein]
FT                   dehydratase"
FT                   /id="PRO_0000091594"
FT   ACT_SITE        71
FT                   /evidence="ECO:0000305|PubMed:21276098"
FT   VARIANT         76
FT                   /note="P -> L (in allele FABA6; TS)"
FT   VARIANT         102
FT                   /note="G -> D (in allele FABA2; TS)"
FT   HELIX           10..17
FT                   /evidence="ECO:0007829|PDB:4KEH"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:1MKA"
FT   HELIX           29..31
FT                   /evidence="ECO:0007829|PDB:4KEH"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:4KEH"
FT   STRAND          38..46
FT                   /evidence="ECO:0007829|PDB:4KEH"
FT   TURN            48..51
FT                   /evidence="ECO:0007829|PDB:1MKA"
FT   STRAND          54..60
FT                   /evidence="ECO:0007829|PDB:4KEH"
FT   HELIX           66..70
FT                   /evidence="ECO:0007829|PDB:4KEH"
FT   TURN            71..74
FT                   /evidence="ECO:0007829|PDB:4KEH"
FT   HELIX           80..97
FT                   /evidence="ECO:0007829|PDB:4KEH"
FT   STRAND          102..110
FT                   /evidence="ECO:0007829|PDB:4KEH"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:4KEH"
FT   STRAND          124..150
FT                   /evidence="ECO:0007829|PDB:4KEH"
FT   STRAND          153..166
FT                   /evidence="ECO:0007829|PDB:4KEH"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:1MKB"
SQ   SEQUENCE   172 AA;  18969 MW;  DFC508352D2DCF2C CRC64;
     MVDKRESYTK EDLLASGRGE LFGAKGPQLP APNMLMMDRV VKMTETGGNF DKGYVEAELD
     INPDLWFFGC HFIGDPVMPG CLGLDAMWQL VGFYLGWLGG EGKGRALGVG EVKFTGQVLP
     TAKKVTYRIH FKRIVNRRLI MGLADGEVLV DGRLIYTASD LKVGLFQDTS AF
//