HSAD_RHOJR
ID HSAD_RHOJR Reviewed; 292 AA.
AC Q9KWQ6;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=Meta-cleavage product hydrolase;
DE Short=MCP hydrolase;
GN Name=hsaD; Synonyms=bphD2; OrderedLocusNames=RHA1_ro04540;
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN THE DEGRADATION OF
RP BIPHENYL AND POLYCHLORINATED BIPHENYLS.
RC STRAIN=RHA1;
RX PubMed=16233225; DOI=10.1016/s1389-1723(02)80078-0;
RA Sakai M., Masai E., Asami H., Sugiyama K., Kimbara K., Fukuda M.;
RT "Diversity of 2,3-dihydroxybiphenyl dioxygenase genes in a strong PCB
RT degrader, Rhodococcus sp. strain RHA1.";
RL J. Biosci. Bioeng. 93:421-427(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
RN [3]
RP FUNCTION IN CHOLESTEROL DEGRADATION.
RC STRAIN=RHA1;
RX PubMed=17264217; DOI=10.1073/pnas.0605728104;
RA Van der Geize R., Yam K., Heuser T., Wilbrink M.H., Hara H., Anderton M.C.,
RA Sim E., Dijkhuizen L., Davies J.E., Mohn W.W., Eltis L.D.;
RT "A gene cluster encoding cholesterol catabolism in a soil actinomycete
RT provides insight into Mycobacterium tuberculosis survival in macrophages.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1947-1952(2007).
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). Also involved in
CC biphenyl and polychlorinated biphenyls (PCBs) degradation.
CC {ECO:0000269|PubMed:16233225, ECO:0000269|PubMed:17264217}.
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 -!- 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; CP000431; ABG96326.1; -; Genomic_DNA.
DR EMBL; AB030672; BAA98136.1; -; Genomic_DNA.
DR RefSeq; WP_011596918.1; NC_008268.1.
DR AlphaFoldDB; Q9KWQ6; -.
DR SMR; Q9KWQ6; -.
DR STRING; 101510.RHA1_ro04540; -.
DR ESTHER; rhosp-bphD2; Carbon-carbon_bond_hydrolase.
DR MEROPS; S33.016; -.
DR EnsemblBacteria; ABG96326; ABG96326; RHA1_ro04540.
DR KEGG; rha:RHA1_ro04540; -.
DR PATRIC; fig|101510.16.peg.4576; -.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_020336_13_2_11; -.
DR OMA; VYILENC; -.
DR BioCyc; MetaCyc:MON-16965; -.
DR BRENDA; 3.7.1.8; 5397.
DR UniPathway; UPA00062; -.
DR Proteomes; UP000008710; Chromosome.
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 InterPro; IPR000639; Epox_hydrolase-like.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome.
FT CHAIN 1..292
FT /note="4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-
FT 1(10),2-diene-4-oate hydrolase"
FT /id="PRO_0000404510"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 44..45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 114
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 292 AA; 31889 MW; B1D871791527AD77 CRC64;
MTTTEEALTF ESTSKFAQVR PHLKLHYHEA GVGNDTTIVL LHGGGPGASS WSNFARNIPV
LAEKFHVLAV DQPGYGLSDK PTEHPQYFVH SASALKDLLD TLGVGGRVHL LGNSLGGGAA
VRFALDYPDR AGRLVLMGPG GLSVNLFAPD PTEGVKNLGK FGYQPTRENL EAFLRIMVFD
QKLITDELID ERFAAASTPE SLAAAKAMGK SFSSADFELG MLWRDAYKLR QRVLLIWGRE
DRVNPLDGAL VALKMIPRAQ LHVFGGCGHW AQLEKFDEFN RLATDFLLDG GK
