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4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase (EC 3.7.1.17) (2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase) (HOPDA hydrolase) (EC 3.7.1.8) (Meta-cleavage product hydrolase) (MCP hydrolase)

 HSAD_MYCTU              Reviewed;         291 AA.
P9WNH5; L0TEJ3; P96851; Q7D596;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
23-MAY-2018, entry version 24.
RecName: Full=4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase;
EC=3.7.1.17;
AltName: Full=2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase;
Short=HOPDA hydrolase;
EC=3.7.1.8;
AltName: Full=Meta-cleavage product hydrolase;
Short=MCP hydrolase;
Name=hsaD; Synonyms=bphD; OrderedLocusNames=Rv3569c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
INDUCTION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=17635188; DOI=10.1111/j.1365-2958.2007.05827.x;
Kendall S.L., Withers M., Soffair C.N., Moreland N.J., Gurcha S.,
Sidders B., Frita R., Ten Bokum A., Besra G.S., Lott J.S.,
Stoker N.G.;
"A highly conserved transcriptional repressor controls a large regulon
involved in lipid degradation in Mycobacterium smegmatis and
Mycobacterium tuberculosis.";
Mol. Microbiol. 65:684-699(2007).
[3]
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 25618 / H37Rv;
PubMed=17264217; DOI=10.1073/pnas.0605728104;
Van der Geize R., Yam K., Heuser T., Wilbrink M.H., Hara H.,
Anderton M.C., Sim E., Dijkhuizen L., Davies J.E., Mohn W.W.,
Eltis L.D.;
"A gene cluster encoding cholesterol catabolism in a soil actinomycete
provides insight into Mycobacterium tuberculosis survival in
macrophages.";
Proc. Natl. Acad. Sci. U.S.A. 104:1947-1952(2007).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[5]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), AND SUBUNIT.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18097091; DOI=10.1107/S1744309107065931;
Lack N., Lowe E.D., Liu J., Eltis L.D., Noble M.E., Sim E.,
Westwood I.M.;
"Structure of HsaD, a steroid-degrading hydrolase, from Mycobacterium
tuberculosis.";
Acta Crystallogr. F 64:2-7(2008).
[6]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT SER-114 IN COMPLEX
WITH SUBSTRATE ANALOGS, FUNCTION AS A HYDROLASE, CATALYTIC ACTIVITY,
MUTAGENESIS OF SER-114, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND SUBUNIT.
PubMed=19875455; DOI=10.1074/jbc.M109.058081;
Lack N.A., Yam K.C., Lowe E.D., Horsman G.P., Owen R.L., Sim E.,
Eltis L.D.;
"Characterization of a carbon-carbon hydrolase from Mycobacterium
tuberculosis involved in cholesterol metabolism.";
J. Biol. Chem. 285:434-443(2010).
-!- FUNCTION: Catalyzes the hydrolysis of a carbon-carbon bond in 4,5:
9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate
(4,9-DSHA) to yield 9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-
oate (DOHNAA) and 2-hydroxy-hexa-2,4-dienoate (HHD). Is also able
to catalyze the hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-
dienoic acid (HOPDA) and the synthetic analog 8-(2-chlorophenyl)-
2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid (HOPODA).
{ECO:0000269|PubMed:19875455}.
-!- CATALYTIC ACTIVITY: (1E,2Z)-3-hydroxy-5,9,17-trioxo-4,5:9,10-
disecoandrosta-1(10),2-dien-4-oate + H(2)O = 3-((3aS,4S,7aS)-7a-
methyl-1,5-dioxo-octahydro-1H-inden-4-yl)propanoate + (2Z,4Z)-2-
hydroxyhexa-2,4-dienoate. {ECO:0000269|PubMed:19875455}.
-!- CATALYTIC ACTIVITY: 2,6-dioxo-6-phenylhexa-3-enoate + H(2)O =
benzoate + 2-oxopent-4-enoate. {ECO:0000269|PubMed:19875455}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=8 uM for 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (at pH
7.5 and at 25 degrees Celsius) {ECO:0000269|PubMed:17264217,
ECO:0000269|PubMed:19875455};
KM=17 uM for 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-
1(10),2-diene-4-oic acid (4,9-DSHA) (at pH 7.5 and at 25 degrees
Celsius) {ECO:0000269|PubMed:17264217,
ECO:0000269|PubMed:19875455};
KM=310 uM for 8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-
2,4-dienoic acid (at pH 7.5 and at 25 degrees Celsius)
{ECO:0000269|PubMed:17264217, ECO:0000269|PubMed:19875455};
Vmax=0.06 umol/sec/mg enzyme with 4,9-DSHA as substrate (at pH 8
and at 25 degrees Celsius) {ECO:0000269|PubMed:17264217,
ECO:0000269|PubMed:19875455};
Vmax=0.009 umol/sec/mg enzyme with 2-hydroxy-6-oxo-6-phenylhexa-
2,4-dienoic acid as substrate (at pH 8 and at 25 degrees
Celsius) {ECO:0000269|PubMed:17264217,
ECO:0000269|PubMed:19875455};
-!- PATHWAY: Lipid metabolism; steroid biosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18097091,
ECO:0000269|PubMed:19875455}.
-!- INDUCTION: Induced by KstR. {ECO:0000269|PubMed:17635188}.
-!- MISCELLANEOUS: Cholesterol metabolism contributes to the survival
of M.tuberculosis in the host by helping the bacterial
multiplication during earlier stages of infection and to the
dissemination of the pathogen in the host.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. HsaD family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL123456; CCP46392.1; -; Genomic_DNA.
PIR; G70605; G70605.
RefSeq; NP_218086.1; NC_000962.3.
RefSeq; WP_003419381.1; NZ_KK339374.1.
PDB; 2VF2; X-ray; 2.35 A; A/B=1-291.
PDB; 2WUD; X-ray; 2.10 A; A/B=1-291.
PDB; 2WUE; X-ray; 1.80 A; A/B=1-291.
PDB; 2WUF; X-ray; 1.90 A; A/B=1-291.
PDB; 2WUG; X-ray; 1.80 A; A/B=1-291.
PDB; 5JZB; X-ray; 2.10 A; A/B=7-288.
PDB; 5JZS; X-ray; 2.27 A; A/B=7-290.
PDBsum; 2VF2; -.
PDBsum; 2WUD; -.
PDBsum; 2WUE; -.
PDBsum; 2WUF; -.
PDBsum; 2WUG; -.
PDBsum; 5JZB; -.
PDBsum; 5JZS; -.
ProteinModelPortal; P9WNH5; -.
SMR; P9WNH5; -.
STRING; 83332.Rv3569c; -.
SwissLipids; SLP:000001006; -.
ESTHER; myctu-Rv3569c; Carbon-carbon_bond_hydrolase.
PaxDb; P9WNH5; -.
PRIDE; P9WNH5; -.
EnsemblBacteria; CCP46392; CCP46392; Rv3569c.
GeneID; 887378; -.
KEGG; mtu:Rv3569c; -.
TubercuList; Rv3569c; -.
eggNOG; ENOG4105D4W; Bacteria.
eggNOG; ENOG410XPIC; LUCA.
KO; K16050; -.
OMA; CGHAAMM; -.
PhylomeDB; P9WNH5; -.
BioCyc; MetaCyc:G185E-7847-MONOMER; -.
UniPathway; UPA00062; -.
PRO; PR:P9WNH5; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0018774; F:2,6-dioxo-6-phenylhexa-3-enoate hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102296; F:4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0034820; F:4,9-DSHA hydrolase activity; IDA:MTBBASE.
GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
GO; GO:0044117; P:growth of symbiont in host; IMP:MTBBASE.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR000073; AB_hydrolase_1.
Pfam; PF12697; Abhydrolase_6; 1.
PRINTS; PR00111; ABHYDROLASE.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
3D-structure; Aromatic hydrocarbons catabolism; Complete proteome;
Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome.
CHAIN 1 291 4,5:9,10-diseco-3-hydroxy-5,9,17-
trioxoandrosta-1(10),2-diene-4-oate
hydrolase.
/FTId=PRO_0000404509.
REGION 45 46 Substrate binding.
ACT_SITE 269 269 Proton acceptor.
BINDING 54 54 Substrate.
BINDING 113 113 Substrate. {ECO:0000255}.
BINDING 115 115 Substrate; via amide nitrogen.
BINDING 192 192 Substrate. {ECO:0000255}.
BINDING 270 270 Substrate. {ECO:0000255}.
SITE 114 114 Transition state stabilizer.
{ECO:0000250}.
MUTAGEN 114 114 S->A: Reduces the hydrolase activity.
{ECO:0000269|PubMed:19875455}.
HELIX 9 12 {ECO:0000244|PDB:2WUE}.
STRAND 13 31 {ECO:0000244|PDB:2WUE}.
STRAND 36 42 {ECO:0000244|PDB:2WUE}.
HELIX 51 54 {ECO:0000244|PDB:2WUE}.
TURN 55 58 {ECO:0000244|PDB:2WUE}.
HELIX 59 62 {ECO:0000244|PDB:2WUE}.
TURN 63 65 {ECO:0000244|PDB:2WUE}.
STRAND 66 71 {ECO:0000244|PDB:2WUE}.
HELIX 88 103 {ECO:0000244|PDB:2WUE}.
STRAND 107 113 {ECO:0000244|PDB:2WUE}.
HELIX 115 126 {ECO:0000244|PDB:2WUE}.
TURN 128 130 {ECO:0000244|PDB:2WUE}.
STRAND 131 138 {ECO:0000244|PDB:2WUE}.
STRAND 140 142 {ECO:0000244|PDB:2WUE}.
STRAND 146 148 {ECO:0000244|PDB:2WUE}.
HELIX 153 163 {ECO:0000244|PDB:2WUE}.
HELIX 167 175 {ECO:0000244|PDB:2WUE}.
HELIX 181 183 {ECO:0000244|PDB:2WUE}.
HELIX 186 196 {ECO:0000244|PDB:2WUE}.
HELIX 199 212 {ECO:0000244|PDB:2WUE}.
HELIX 217 220 {ECO:0000244|PDB:2WUE}.
HELIX 222 224 {ECO:0000244|PDB:2WUE}.
HELIX 226 228 {ECO:0000244|PDB:2WUE}.
STRAND 233 238 {ECO:0000244|PDB:2WUE}.
STRAND 242 244 {ECO:0000244|PDB:2WUE}.
HELIX 246 249 {ECO:0000244|PDB:2WUE}.
HELIX 250 255 {ECO:0000244|PDB:2WUE}.
STRAND 259 266 {ECO:0000244|PDB:2WUE}.
HELIX 271 274 {ECO:0000244|PDB:2WUE}.
HELIX 276 286 {ECO:0000244|PDB:2WUE}.
SEQUENCE 291 AA; 31875 MW; FF706824615601F2 CRC64;
MTATEELTFE STSRFAEVDV DGPLKLHYHE AGVGNDQTVV LLHGGGPGAA SWTNFSRNIA
VLARHFHVLA VDQPGYGHSD KRAEHGQFNR YAAMALKGLF DQLGLGRVPL VGNSLGGGTA
VRFALDYPAR AGRLVLMGPG GLSINLFAPD PTEGVKRLSK FSVAPTRENL EAFLRVMVYD
KNLITPELVD QRFALASTPE SLTATRAMGK SFAGADFEAG MMWREVYRLR QPVLLIWGRE
DRVNPLDGAL VALKTIPRAQ LHVFGQCGHW VQVEKFDEFN KLTIEFLGGG R


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