HTDZ_MYCTU
ID HTDZ_MYCTU Reviewed; 151 AA.
AC P9WNP3; 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 42.
DE RecName: Full=3-hydroxyacyl-thioester dehydratase Z {ECO:0000303|PubMed:18375556};
DE EC=4.2.1.- {ECO:0000269|PubMed:16963641, ECO:0000269|PubMed:18375556, ECO:0000269|PubMed:19136596};
DE AltName: Full=3-hydroxybutyryl-CoA dehydratase {ECO:0000305};
DE EC=4.2.1.55 {ECO:0000269|PubMed:16963641};
DE AltName: Full=Enoyl-CoA hydratase 2 {ECO:0000305};
DE EC=4.2.1.119 {ECO:0000269|PubMed:16963641, ECO:0000269|PubMed:18375556, ECO:0000269|PubMed:19136596};
DE AltName: Full=N-related protein;
DE AltName: Full=Nodulation protein;
GN Name=htdZ {ECO:0000303|PubMed:18375556}; OrderedLocusNames=Rv0130;
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, AND CATALYTIC ACTIVITY.
RX PubMed=18375556; DOI=10.1128/jb.00016-08;
RA Gurvitz A., Hiltunen J.K., Kastaniotis A.J.;
RT "Identification of a novel mycobacterial 3-hydroxyacyl-thioester
RT dehydratase, HtdZ (Rv0130), by functional complementation in yeast.";
RL J. Bacteriol. 190:4088-4090(2008).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [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]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF ASP-40 AND
RP HIS-45.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16963641; DOI=10.1110/ps.062309306;
RA Johansson P., Castell A., Jones T.A., Backbro K.;
RT "Structure and function of Rv0130, a conserved hypothetical protein from
RT Mycobacterium tuberculosis.";
RL Protein Sci. 15:2300-2309(2006).
CC -!- FUNCTION: Shows trans-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydratase
CC activity. In vitro, can hydrate (2E)-butenoyl-CoA, (2E)-hexenoyl-CoA
CC and (2E)-decenoyl-CoA. {ECO:0000269|PubMed:16963641,
CC ECO:0000269|PubMed:18375556, ECO:0000269|PubMed:19136596}.
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:16963641, ECO:0000269|PubMed:18375556,
CC ECO:0000269|PubMed:19136596};
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:16963641, ECO:0000269|PubMed:18375556};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexanoyl-CoA = (2E)-hexenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:46720, ChEBI:CHEBI:15377, ChEBI:CHEBI:62077,
CC ChEBI:CHEBI:74280; Evidence={ECO:0000269|PubMed:18375556,
CC ECO:0000269|PubMed:19136596};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxydecanoyl-CoA = (2E)-decenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:45992, ChEBI:CHEBI:15377, ChEBI:CHEBI:61406,
CC ChEBI:CHEBI:74272; Evidence={ECO:0000269|PubMed:18375556,
CC ECO:0000269|PubMed:19136596};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=55 uM for 2-butenoyl-CoA {ECO:0000269|PubMed:16963641};
CC Note=kcat is 110 sec(-1) with butenoyl-CoA as substrate.
CC {ECO:0000269|PubMed:16963641};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16963641}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP42855.1; -; Genomic_DNA.
DR PIR; E70615; E70615.
DR RefSeq; NP_214644.1; NC_000962.3.
DR RefSeq; WP_003400912.1; NZ_NVQJ01000001.1.
DR PDB; 2C2I; X-ray; 1.80 A; A/B=1-151.
DR PDBsum; 2C2I; -.
DR AlphaFoldDB; P9WNP3; -.
DR SMR; P9WNP3; -.
DR STRING; 83332.Rv0130; -.
DR SwissLipids; SLP:000001286; -.
DR PaxDb; P9WNP3; -.
DR GeneID; 45424096; -.
DR GeneID; 886876; -.
DR KEGG; mtu:Rv0130; -.
DR TubercuList; Rv0130; -.
DR eggNOG; COG2030; Bacteria.
DR OMA; TVDQTMI; -.
DR PhylomeDB; P9WNP3; -.
DR Proteomes; UP000001584; Chromosome.
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:0004300; F:enoyl-CoA hydratase activity; IDA:MTBBASE.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Fatty acid metabolism; Lipid metabolism; Lyase;
KW Reference proteome.
FT CHAIN 1..151
FT /note="3-hydroxyacyl-thioester dehydratase Z"
FT /id="PRO_0000262761"
FT DOMAIN 11..131
FT /note="MaoC-like"
FT /evidence="ECO:0000255"
FT BINDING 60..63
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 86..89
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000305"
FT BINDING 97..99
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 124
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000305"
FT BINDING 148
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000305"
FT SITE 40
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305"
FT SITE 42
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT SITE 45
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305"
FT MUTAGEN 40
FT /note="D->N: 27% loss of activity."
FT /evidence="ECO:0000269|PubMed:16963641"
FT MUTAGEN 45
FT /note="H->Q: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:16963641"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2C2I"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:2C2I"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:2C2I"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:2C2I"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:2C2I"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:2C2I"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:2C2I"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:2C2I"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:2C2I"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:2C2I"
FT STRAND 84..95
FT /evidence="ECO:0007829|PDB:2C2I"
FT STRAND 105..119
FT /evidence="ECO:0007829|PDB:2C2I"
FT STRAND 122..133
FT /evidence="ECO:0007829|PDB:2C2I"
FT STRAND 140..150
FT /evidence="ECO:0007829|PDB:2C2I"
SQ SEQUENCE 151 AA; 16007 MW; 7A2613466BBFCD57 CRC64;
MRTFESVADL AAAAGEKVGQ SDWVTITQEE VNLFADATGD HQWIHVDPER AAAGPFGTTI
AHGFMTLALL PRLQHQMYTV KGVKLAINYG LNKVRFPAPV PVGSRVRATS SLVGVEDLGN
GTVQATVSTT VEVEGSAKPA CVAESIVRYV A
