HSAD_MYCTO
ID HSAD_MYCTO Reviewed; 291 AA.
AC P9WNH4; L0TEJ3; P96851; Q7D596;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase;
DE EC=3.7.1.17;
DE AltName: Full=2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase;
DE Short=HOPDA hydrolase;
DE EC=3.7.1.8;
DE AltName: Full=Meta-cleavage product hydrolase;
DE Short=MCP hydrolase;
GN Name=hsaD; Synonyms=bphD; OrderedLocusNames=MT3674;
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: Catalyzes the hydrolysis of a carbon-carbon bond in 4,5:
CC 9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate (4,9-
CC DSHA) to yield 9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oate
CC (DOHNAA) and 2-hydroxy-hexa-2,4-dienoate (HHD). Is also able to
CC catalyze the hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic
CC acid (HOPDA) and the synthetic analog 8-(2-chlorophenyl)-2-hydroxy-5-
CC methyl-6-oxoocta-2,4-dienoic acid (HOPODA) (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1E,2Z)-3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-
CC 1(10),2-dien-4-oate + H2O = (2Z,4Z)-2-hydroxyhexa-2,4-dienoate + 3-
CC [(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoate
CC + H(+); Xref=Rhea:RHEA:32035, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:63690, ChEBI:CHEBI:63692, ChEBI:CHEBI:63693; EC=3.7.1.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,6-dioxo-6-phenylhexa-3-enoate + H2O = 2-oxopent-4-enoate +
CC benzoate + H(+); Xref=Rhea:RHEA:17161, ChEBI:CHEBI:11641,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16150,
CC ChEBI:CHEBI:64675; EC=3.7.1.8;
CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. HsaD family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK48033.1; -; Genomic_DNA.
DR PIR; G70605; G70605.
DR RefSeq; WP_003419381.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WNH4; -.
DR SMR; P9WNH4; -.
DR ESTHER; myctu-Rv3569c; Carbon-carbon_bond_hydrolase.
DR MEROPS; S33.016; -.
DR EnsemblBacteria; AAK48033; AAK48033; MT3674.
DR KEGG; mtc:MT3674; -.
DR PATRIC; fig|83331.31.peg.3956; -.
DR HOGENOM; CLU_020336_13_2_11; -.
DR UniPathway; UPA00062; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0018774; F:2,6-dioxo-6-phenylhexa-3-enoate hydrolase activity; IEA:UniProtKB-EC.
DR 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.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Hydrolase; Lipid degradation;
KW Lipid metabolism.
FT CHAIN 1..291
FT /note="4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-
FT 1(10),2-diene-4-oate hydrolase"
FT /id="PRO_0000427126"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 45..46
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT SITE 114
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ 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
