HTDX_MYCTU
ID HTDX_MYCTU Reviewed; 280 AA.
AC O53664; F2GM41; I6X8T8; Q7DA70;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=3-hydroxyacyl-thioester dehydratase X {ECO:0000305};
DE EC=4.2.1.- {ECO:0000269|PubMed:20511508};
DE AltName: Full=3-hydroxybutyryl-CoA dehydratase {ECO:0000305};
DE EC=4.2.1.55 {ECO:0000269|PubMed:20511508};
DE AltName: Full=Enoyl-CoA hydratase 2 {ECO:0000305};
DE EC=4.2.1.119 {ECO:0000269|PubMed:20511508};
GN Name=htdX {ECO:0000303|PubMed:19136596};
GN OrderedLocusNames=Rv0241c {ECO:0000312|EMBL:CCP42970.1};
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 FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20511508; DOI=10.1128/jb.00386-10;
RA Sacco E., Slama N., Baeckbro K., Parish T., Laval F., Daffe M., Eynard N.,
RA Quemard A.;
RT "Revisiting the assignment of Rv0241c to fatty acid synthase type II of
RT Mycobacterium tuberculosis.";
RL J. Bacteriol. 192:4037-4044(2010).
RN [4]
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 [5] {ECO:0007744|PDB:3WEW, ECO:0007744|PDB:4OOB}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 29-280.
RC STRAIN=H37Rv;
RX PubMed=24100560; DOI=10.1107/s1744309113023452;
RA Biswas R., Dutta D., Das A.K.;
RT "Cloning, overexpression, purification, crystallization and preliminary X-
RT ray diffraction analysis of Rv0241c (HtdX) from Mycobacterium tuberculosis
RT H37Rv.";
RL Acta Crystallogr. F 69:1110-1113(2013).
CC -!- FUNCTION: Shows trans-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydratase
CC activity (PubMed:19136596, PubMed:20511508). Displays a broad chain
CC length specificity, with a predilection for the C8 to C12 substrates
CC (PubMed:20511508). {ECO:0000269|PubMed:19136596,
CC ECO:0000269|PubMed:20511508}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:26526, ChEBI:CHEBI:15377, ChEBI:CHEBI:57319,
CC ChEBI:CHEBI:58856; EC=4.2.1.119;
CC Evidence={ECO:0000269|PubMed:20511508};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-octenoyl-CoA + H2O = (3R)-hydroxyoctanoyl-CoA;
CC Xref=Rhea:RHEA:40187, ChEBI:CHEBI:15377, ChEBI:CHEBI:62242,
CC ChEBI:CHEBI:74279; Evidence={ECO:0000269|PubMed:20511508};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxydodecanoyl-CoA = (2E)-dodecenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:44024, ChEBI:CHEBI:15377, ChEBI:CHEBI:57330,
CC ChEBI:CHEBI:74276; Evidence={ECO:0000269|PubMed:20511508};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39159, ChEBI:CHEBI:15377, ChEBI:CHEBI:61526,
CC ChEBI:CHEBI:74278; Evidence={ECO:0000269|PubMed:20511508};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyeicosanoyl-CoA = (2E)-eicosenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39175, ChEBI:CHEBI:15377, ChEBI:CHEBI:74691,
CC ChEBI:CHEBI:76373; Evidence={ECO:0000269|PubMed:20511508};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:17849, ChEBI:CHEBI:15377, ChEBI:CHEBI:57315,
CC ChEBI:CHEBI:57332; EC=4.2.1.55;
CC Evidence={ECO:0000269|PubMed:20511508};
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene does not affect the
CC biosynthesis of all three types of mycolic acid.
CC {ECO:0000269|PubMed:20511508}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP42970.1; -; Genomic_DNA.
DR RefSeq; NP_214755.1; NC_000962.3.
DR RefSeq; WP_003401305.1; NZ_NVQJ01000001.1.
DR PDB; 3WEW; X-ray; 2.40 A; A=29-280.
DR PDB; 4OOB; X-ray; 2.30 A; A=29-280.
DR PDBsum; 3WEW; -.
DR PDBsum; 4OOB; -.
DR AlphaFoldDB; O53664; -.
DR SMR; O53664; -.
DR STRING; 83332.Rv0241c; -.
DR SwissLipids; SLP:000001024; -.
DR PaxDb; O53664; -.
DR PRIDE; O53664; -.
DR DNASU; 886686; -.
DR GeneID; 45424214; -.
DR GeneID; 886686; -.
DR KEGG; mtu:Rv0241c; -.
DR PATRIC; fig|83332.111.peg.274; -.
DR TubercuList; Rv0241c; -.
DR eggNOG; COG2030; Bacteria.
DR OMA; YPHVLGF; -.
DR PhylomeDB; O53664; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0019171; F:3-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; IMP:MTBBASE.
DR GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; IDA:MTBBASE.
DR GO; GO:0003859; F:3-hydroxybutyryl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:MTBBASE.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:MTBBASE.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SUPFAM; SSF54637; SSF54637; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid metabolism; Lipid metabolism; Lyase;
KW Reference proteome.
FT CHAIN 1..280
FT /note="3-hydroxyacyl-thioester dehydratase X"
FT /id="PRO_0000448719"
FT DOMAIN 162..256
FT /note="MaoC-like"
FT /evidence="ECO:0000255"
FT REGION 149..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4OOB"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:4OOB"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4OOB"
FT HELIX 63..77
FT /evidence="ECO:0007829|PDB:4OOB"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3WEW"
FT STRAND 89..99
FT /evidence="ECO:0007829|PDB:4OOB"
FT STRAND 106..119
FT /evidence="ECO:0007829|PDB:4OOB"
FT STRAND 122..133
FT /evidence="ECO:0007829|PDB:4OOB"
FT STRAND 136..148
FT /evidence="ECO:0007829|PDB:4OOB"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:4OOB"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:4OOB"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:4OOB"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:4OOB"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:4OOB"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:4OOB"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:4OOB"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:4OOB"
FT STRAND 230..238
FT /evidence="ECO:0007829|PDB:4OOB"
FT STRAND 243..254
FT /evidence="ECO:0007829|PDB:4OOB"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:4OOB"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:3WEW"
FT STRAND 271..279
FT /evidence="ECO:0007829|PDB:4OOB"
SQ SEQUENCE 280 AA; 30195 MW; AE356A650624FB8C CRC64;
MTQPSGLKNL LRAAAGALPV VPRTDQLPNR TVTVEELPID PANVAAYAAV TGLRYGNQVP
LTYPFALTFP SVMSLVTGFD FPFAAMGAIH TENHITQYRP IAVTDAVGVR VRAENLREHR
RGLLVDLVTN VSVGNDVAWH QVTTFLHQQR TSLSGEPKPP PQKKPKLPPP AAVLRITPAK
IRRYAAVGGD HNPIHTNPIA AKLFGFPTVI AHGMFTAAAV LANIEARFPD AVRYSVRFAK
PVLLPATAGL YVAEGDGGWD LTLRNMAKGY PHLTATVRGL
