FADM_ECOLI
ID FADM_ECOLI Reviewed; 132 AA.
AC P77712; Q2MBY3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Long-chain acyl-CoA thioesterase FadM;
DE EC=3.1.2.- {ECO:0000269|PubMed:18576672};
DE AltName: Full=Acyl-CoA thioester hydrolase;
DE AltName: Full=Thioesterase 3;
DE AltName: Full=Thioesterase III {ECO:0000303|PubMed:18576672};
GN Name=fadM {ECO:0000303|PubMed:19684132}; Synonyms=tesC, ybaW;
GN OrderedLocusNames=b0443, JW0433;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Hatada E., Ohmori H., Qiao Y., Tsuji M., Fukuda R.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION
RP BY MASS SPECTROMETRY, AND INDUCTION.
RX PubMed=18576672; DOI=10.1021/bi800595f;
RA Nie L., Ren Y., Schulz H.;
RT "Identification and characterization of Escherichia coli thioesterase III
RT that functions in fatty acid beta-oxidation.";
RL Biochemistry 47:7744-7751(2008).
RN [6]
RP INDUCTION, AND GENE NAME.
RC STRAIN=K12;
RX PubMed=19684132; DOI=10.1128/jb.00835-09;
RA Feng Y., Cronan J.E.;
RT "A new member of the Escherichia coli fad regulon: transcriptional
RT regulation of fadM (ybaW).";
RL J. Bacteriol. 191:6320-6328(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT.
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of Escherichia coli hypothetical protein Ybaw.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: Long-chain acyl-CoA thioesterase that could be involved in
CC beta-oxidation of fatty acids (PubMed:18576672). Is most active with
CC 3,5-tetradecadienoyl-CoA, a metabolite of oleic acid that is hydrolyzed
CC during oleate beta-oxidation, but can also use other substrates such as
CC 3,5-dodecadienoyl-CoA, 9-cis-octadecenoyl-CoA, octadecanoyl-CoA,
CC hexadecanoyl-CoA, 3-hydroxytetradecanoyl-CoA and tetradecanoyl-CoA
CC (PubMed:18576672). {ECO:0000269|PubMed:18576672}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E,5Z)-tetradecadienoyl-CoA + H2O = (3E,5Z)-tetradecadienoate
CC + CoA + H(+); Xref=Rhea:RHEA:55044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:71586,
CC ChEBI:CHEBI:71590; Evidence={ECO:0000269|PubMed:18576672};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55045;
CC Evidence={ECO:0000269|PubMed:18576672};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E,5Z)-dodecadienoyl-CoA + H2O = (3E,5Z)-dodecadienoate + CoA
CC + H(+); Xref=Rhea:RHEA:55048, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:138558, ChEBI:CHEBI:138569;
CC Evidence={ECO:0000269|PubMed:18576672};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55049;
CC Evidence={ECO:0000269|PubMed:18576672};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+);
CC Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387;
CC Evidence={ECO:0000269|PubMed:18576672};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000269|PubMed:18576672};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
CC Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
CC Evidence={ECO:0000269|PubMed:18576672};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000269|PubMed:18576672};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379;
CC Evidence={ECO:0000269|PubMed:18576672};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000269|PubMed:18576672};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxytetradecanoyl-CoA + H2O = (3S)-
CC hydroxytetradecanoate + CoA + H(+); Xref=Rhea:RHEA:54976,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:62614, ChEBI:CHEBI:138437;
CC Evidence={ECO:0000269|PubMed:18576672};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54977;
CC Evidence={ECO:0000269|PubMed:18576672};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000269|PubMed:18576672};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000269|PubMed:18576672};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.0 uM for 3,5-cis-tetradecadienoyl-CoA
CC {ECO:0000269|PubMed:18576672};
CC KM=10.8 uM for 3,5-cis-dodecadienoyl-CoA
CC {ECO:0000269|PubMed:18576672};
CC KM=5.8 uM for 3-hydroxytetradecanoyl-CoA
CC {ECO:0000269|PubMed:18576672};
CC KM=6.0 uM for hexadecanoyl-CoA {ECO:0000269|PubMed:18576672};
CC KM=6.3 uM for tetradecanoyl-CoA {ECO:0000269|PubMed:18576672};
CC KM=13.0 uM for lauroyl-CoA {ECO:0000269|PubMed:18576672};
CC Vmax=101.3 umol/min/mg enzyme with 3,5-cis-tetradecadienoyl-CoA as
CC substrate {ECO:0000269|PubMed:18576672};
CC Vmax=92.3 umol/min/mg enzyme with 3,5-cis-dodecadienoyl-CoA as
CC substrate {ECO:0000269|PubMed:18576672};
CC Vmax=45.5 umol/min/mg enzyme with 3-hydroxytetradecanoyl-CoA as
CC substrate {ECO:0000269|PubMed:18576672};
CC Vmax=43.5 umol/min/mg enzyme with hexadecanoyl-CoA as substrate
CC {ECO:0000269|PubMed:18576672};
CC Vmax=26.4 umol/min/mg enzyme with tetradecanoyl-CoA as substrate
CC {ECO:0000269|PubMed:18576672};
CC Vmax=6.9 umol/min/mg enzyme with lauroyl-CoA as substrate
CC {ECO:0000269|PubMed:18576672};
CC -!- SUBUNIT: Homotetramer. {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by growth on oleic acid. Repressed by FadR and
CC by the cyclic AMP receptor protein-cAMP (CRP-cAMP) complex.
CC {ECO:0000269|PubMed:18576672, ECO:0000269|PubMed:19684132}.
CC -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D82943; BAA11647.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40199.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73546.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76223.1; -; Genomic_DNA.
DR PIR; C64774; C64774.
DR RefSeq; NP_414977.1; NC_000913.3.
DR RefSeq; WP_001194534.1; NZ_STEB01000007.1.
DR PDB; 1NJK; X-ray; 1.90 A; A/B/C/D=1-132.
DR PDBsum; 1NJK; -.
DR AlphaFoldDB; P77712; -.
DR SMR; P77712; -.
DR BioGRID; 4259836; 162.
DR IntAct; P77712; 4.
DR STRING; 511145.b0443; -.
DR SwissLipids; SLP:000001801; -.
DR jPOST; P77712; -.
DR PaxDb; P77712; -.
DR PRIDE; P77712; -.
DR EnsemblBacteria; AAC73546; AAC73546; b0443.
DR EnsemblBacteria; BAE76223; BAE76223; BAE76223.
DR GeneID; 66671255; -.
DR GeneID; 945812; -.
DR KEGG; ecj:JW0433; -.
DR KEGG; eco:b0443; -.
DR PATRIC; fig|1411691.4.peg.1833; -.
DR EchoBASE; EB3040; -.
DR eggNOG; COG0824; Bacteria.
DR HOGENOM; CLU_101141_4_2_6; -.
DR InParanoid; P77712; -.
DR OMA; HIDLFQH; -.
DR PhylomeDB; P77712; -.
DR BioCyc; EcoCyc:G6244-MON; -.
DR BioCyc; MetaCyc:G6244-MON; -.
DR BRENDA; 3.1.2.20; 2026.
DR EvolutionaryTrace; P77712; -.
DR PRO; PR:P77712; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:EcoCyc.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:RHEA.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:RHEA.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEP:EcoCyc.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR006684; YbgC/YbaW.
DR PIRSF; PIRSF003230; YbgC; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR00051; TIGR00051; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..132
FT /note="Long-chain acyl-CoA thioesterase FadM"
FT /id="PRO_0000168630"
FT ACT_SITE 13
FT /evidence="ECO:0000255"
FT STRAND 1..6
FT /evidence="ECO:0007829|PDB:1NJK"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1NJK"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1NJK"
FT HELIX 20..36
FT /evidence="ECO:0007829|PDB:1NJK"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:1NJK"
FT STRAND 49..60
FT /evidence="ECO:0007829|PDB:1NJK"
FT STRAND 69..80
FT /evidence="ECO:0007829|PDB:1NJK"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:1NJK"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:1NJK"
FT STRAND 97..110
FT /evidence="ECO:0007829|PDB:1NJK"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1NJK"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1NJK"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:1NJK"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:1NJK"
SQ SEQUENCE 132 AA; 15088 MW; EBB3539149A37383 CRC64;
MQTQIKVRGY HLDVYQHVNN ARYLEFLEEA RWDGLENSDS FQWMTAHNIA FVVVNININY
RRPAVLSDLL TITSQLQQLN GKSGILSQVI TLEPEGQVVA DALITFVCID LKTQKALALE
GELREKLEQM VK
