FCOT_MYCTU
ID FCOT_MYCTU Reviewed; 183 AA.
AC P9WM67; L0T4B3; P64685; Q10894;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Long-chain fatty acyl-CoA thioesterase FcoT {ECO:0000303|PubMed:17524985};
DE EC=3.1.2.- {ECO:0000269|PubMed:17524985};
DE AltName: Full=Palmitoyl-CoA hydrolase {ECO:0000305};
DE EC=3.1.2.2 {ECO:0000269|PubMed:17524985};
GN Name=fcoT {ECO:0000303|PubMed:17524985}; OrderedLocusNames=Rv0098;
GN ORFNames=MTCY251.17;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION.
RX PubMed=19136596; DOI=10.1128/jb.01046-08;
RA Gurvitz A., Hiltunen J.K., Kastaniotis A.J.;
RT "Heterologous expression of mycobacterial proteins in Saccharomyces
RT cerevisiae reveals two physiologically functional 3-hydroxyacyl-thioester
RT dehydratases, HtdX and HtdY, in addition to HadABC and HtdZ.";
RL J. Bacteriol. 191:2683-2690(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4] {ECO:0007744|PDB:2PFC}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF TYR-33; TYR-66;
RP HIS-72; ASN-74; GLU-77; ASN-83 AND TYR-87.
RX PubMed=17524985; DOI=10.1016/j.chembiol.2007.04.005;
RA Wang F., Langley R., Gulten G., Wang L., Sacchettini J.C.;
RT "Identification of a type III thioesterase reveals the function of an
RT operon crucial for Mtb virulence.";
RL Chem. Biol. 14:543-551(2007).
RN [5] {ECO:0007744|PDB:3B18}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS), AND SUBUNIT.
RX PubMed=22292955; DOI=10.1080/07391102.2012.10507417;
RA Maity K., Bajaj P., Surolia N., Surolia A., Suguna K.;
RT "Insights into the substrate specificity of a thioesterase Rv0098 of
RT Mycobacterium tuberculosis through X-ray crystallographic and molecular
RT dynamics studies.";
RL J. Biomol. Struct. Dyn. 29:973-983(2012).
CC -!- FUNCTION: Thiesterase that shows a preference for long chain fatty acyl
CC groups. In vitro, cleaves the thioester linkage of palmitoyl-CoA,
CC stearoyl-CoA, lauroyl-CoA and hexanoyl-CoA (PubMed:17524985). Contains
CC low levels of trans-enoyl hydratase activity (PubMed:19136596).
CC {ECO:0000269|PubMed:17524985, ECO:0000269|PubMed:19136596}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+);
CC Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636;
CC Evidence={ECO:0000269|PubMed:17524985};
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; EC=3.1.2.2;
CC Evidence={ECO:0000269|PubMed:17524985};
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:17524985};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
CC Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
CC Evidence={ECO:0000269|PubMed:17524985};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanoyl-CoA = CoA + H(+) + hexanoate;
CC Xref=Rhea:RHEA:40115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000269|PubMed:17524985};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.87 uM for palmitoyl-CoA {ECO:0000269|PubMed:17524985};
CC KM=10.28 uM for stearoyl-CoA {ECO:0000269|PubMed:17524985};
CC KM=38.52 uM for lauroyl-CoA {ECO:0000269|PubMed:17524985};
CC KM=63.18 uM for hexanoyl-CoA {ECO:0000269|PubMed:17524985};
CC Note=kcat is 0.037 sec(-1) with palmitoyl-CoA as substrate. kcat is
CC 0.019 sec(-1) with stearoyl-CoA as substrate. kcat is 0.015 sec(-1)
CC with lauroyl-CoA as substrate. kcat is 0.012 sec(-1) with hexanoyl-
CC CoA as substrate. {ECO:0000269|PubMed:17524985};
CC -!- SUBUNIT: Homohexamer. Trimer of dimers. {ECO:0000269|PubMed:17524985,
CC ECO:0000269|PubMed:22292955}.
CC -!- SIMILARITY: Belongs to the FcoT family. {ECO:0000305}.
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DR EMBL; AL123456; CCP42823.1; -; Genomic_DNA.
DR PIR; B70751; B70751.
DR RefSeq; NP_214612.1; NC_000962.3.
DR RefSeq; WP_003899810.1; NZ_NVQJ01000053.1.
DR PDB; 2PFC; X-ray; 2.30 A; A=1-183.
DR PDB; 3B18; X-ray; 2.75 A; A=1-183.
DR PDBsum; 2PFC; -.
DR PDBsum; 3B18; -.
DR AlphaFoldDB; P9WM67; -.
DR SMR; P9WM67; -.
DR STRING; 83332.Rv0098; -.
DR SwissLipids; SLP:000001037; -.
DR PaxDb; P9WM67; -.
DR DNASU; 886935; -.
DR GeneID; 886935; -.
DR KEGG; mtu:Rv0098; -.
DR TubercuList; Rv0098; -.
DR eggNOG; ENOG5032SAE; Bacteria.
DR OMA; SCYIDDT; -.
DR BRENDA; 3.1.2.2; 3445.
DR BRENDA; 3.1.2.20; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:MTBBASE.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:MTBBASE.
DR Gene3D; 3.10.129.30; -; 1.
DR InterPro; IPR022598; FcoT_ThioEstase.
DR InterPro; IPR043064; FcoT_ThioEstase_Rv0098-like_sf.
DR Pfam; PF10862; FcoT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid metabolism; Hydrolase; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..183
FT /note="Long-chain fatty acyl-CoA thioesterase FcoT"
FT /id="PRO_0000103668"
FT MUTAGEN 33
FT /note="Y->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17524985"
FT MUTAGEN 66
FT /note="Y->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17524985"
FT MUTAGEN 72
FT /note="H->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:17524985"
FT MUTAGEN 74
FT /note="N->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17524985"
FT MUTAGEN 77
FT /note="E->Q: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:17524985"
FT MUTAGEN 83
FT /note="N->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:17524985"
FT MUTAGEN 87
FT /note="Y->F: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:17524985"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:2PFC"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:2PFC"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:2PFC"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:2PFC"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:2PFC"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2PFC"
FT HELIX 75..95
FT /evidence="ECO:0007829|PDB:2PFC"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2PFC"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:2PFC"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:2PFC"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:3B18"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:2PFC"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2PFC"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3B18"
FT STRAND 154..164
FT /evidence="ECO:0007829|PDB:2PFC"
FT STRAND 170..179
FT /evidence="ECO:0007829|PDB:2PFC"
SQ SEQUENCE 183 AA; 20529 MW; EC4FCF0B8032355F CRC64;
MSHTDLTPCT RVLASSGTVP IAEELLARVL EPYSCKGCRY LIDAQYSATE DSVLAYGNFT
IGESAYIRST GHFNAVELIL CFNQLAYSAF APAVLNEEIR VLRGWSIDDY CQHQLSSMLI
RKASSRFRKP LNPQKFSARL LCRDLQVIER TWRYLKVPCV IEFWDENGGA ASGEIELAAL
NIP
