FABA_ECOLI
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 03-AUG-2022, entry version 138.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 E-(2)-decenoyl-ACP and then its isomerization to
CC Z-(3)-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:8910376,
CC PubMed:7592873, PubMed:10629181). Is inactive in the dehydration of
CC long 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_STEB01000006.1.
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 PDBsum; 1MKA; -.
DR PDBsum; 1MKB; -.
DR PDBsum; 4KEH; -.
DR AlphaFoldDB; P0A6Q3; -.
DR SMR; P0A6Q3; -.
DR BioGRID; 4263239; 213.
DR BioGRID; 849942; 1.
DR DIP; DIP-31864N; -.
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; P0A6Q3; -.
DR PRIDE; P0A6Q3; -.
DR EnsemblBacteria; AAC74040; AAC74040; b0954.
DR EnsemblBacteria; BAA35712; BAA35712; BAA35712.
DR GeneID; 67414158; -.
DR GeneID; 945568; -.
DR KEGG; ecj:JW0937; -.
DR KEGG; eco:b0954; -.
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 PhylomeDB; P0A6Q3; -.
DR BioCyc; EcoCyc:FABA-MON; -.
DR BioCyc; MetaCyc:FABA-MON; -.
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; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IDA:EcoCyc.
DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IDA:EcoCyc.
DR GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
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 CDD; cd01287; FabA; 1.
DR HAMAP; MF_00405; FabA; 1.
DR InterPro; IPR010083; FabA.
DR InterPro; IPR013114; FabA_FabZ.
DR InterPro; IPR029069; HotDog_dom_sf.
DR PANTHER; PTHR30272; PTHR30272; 1.
DR PANTHER; PTHR30272:SF8; PTHR30272:SF8; 1.
DR Pfam; PF07977; FabA; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR01749; fabA; 1.
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 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
