ID   HTDZ_MYCTO              Reviewed;         151 AA.
AC   P9WNP2; L0T2P7; P96807; Q7DAF4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=3-hydroxyacyl-thioester dehydratase Z {ECO:0000250|UniProtKB:P9WNP3};
DE            EC=4.2.1.- {ECO:0000250|UniProtKB:P9WNP3};
DE   AltName: Full=Enoyl-CoA hydratase 2 {ECO:0000305};
DE            EC=4.2.1.119 {ECO:0000250|UniProtKB:P9WNP3};
DE   AltName: Full=N-related protein;
DE   AltName: Full=Nodulation protein;
GN   Name=htdZ {ECO:0000250|UniProtKB:P9WNP3}; OrderedLocusNames=MT0138;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Shows trans-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydratase
CC       activity. {ECO:0000250|UniProtKB:P9WNP3}.
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:0000250|UniProtKB:P9WNP3};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WNP3}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK44362.1; -; Genomic_DNA.
DR   PIR; E70615; E70615.
DR   RefSeq; WP_003400912.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNP2; -.
DR   SMR; P9WNP2; -.
DR   EnsemblBacteria; AAK44362; AAK44362; MT0138.
DR   GeneID; 45424096; -.
DR   KEGG; mtc:MT0138; -.
DR   PATRIC; fig|83331.31.peg.150; -.
DR   HOGENOM; CLU_108911_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd03450; NodN; 1.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR002539; MaoC-like_dom.
DR   InterPro; IPR039375; NodN-like.
DR   Pfam; PF01575; MaoC_dehydratas; 1.
DR   SUPFAM; SSF54637; SSF54637; 1.
PE   3: Inferred from homology;
KW   Fatty acid metabolism; Lipid metabolism; Lyase.
FT   CHAIN           1..151
FT                   /note="3-hydroxyacyl-thioester dehydratase Z"
FT                   /id="PRO_0000427092"
FT   DOMAIN          11..131
FT                   /note="MaoC-like"
FT                   /evidence="ECO:0000255"
FT   BINDING         60..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WNP3"
FT   BINDING         86..89
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000250|UniProtKB:P9WNP3"
FT   BINDING         97..99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WNP3"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000250|UniProtKB:P9WNP3"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000250|UniProtKB:P9WNP3"
FT   SITE            40
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P9WNP3"
FT   SITE            42
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255"
FT   SITE            45
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P9WNP3"
SQ   SEQUENCE   151 AA;  16007 MW;  7A2613466BBFCD57 CRC64;
     MRTFESVADL AAAAGEKVGQ SDWVTITQEE VNLFADATGD HQWIHVDPER AAAGPFGTTI
     AHGFMTLALL PRLQHQMYTV KGVKLAINYG LNKVRFPAPV PVGSRVRATS SLVGVEDLGN
     GTVQATVSTT VEVEGSAKPA CVAESIVRYV A