ID   HSAC_RHOJR              Reviewed;         300 AA.
AC   Q9KWQ5;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Iron-dependent extradiol dioxygenase;
DE            EC=1.13.11.25;
GN   Name=hsaC; Synonyms=bphC5; OrderedLocusNames=RHA1_ro04541;
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, AND DISRUPTION PHENOTYPE.
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 meta-cleavage of 3,4-dihydroxy-9,10-
CC       seconandrost-1,3,5(10)-triene-9,17-dione (3,4-DHSA) to produce 4,5-
CC       9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid
CC       (4,9-DSHA). Also involved in biphenyl and polychlorinated biphenyls
CC       (PCBs) degradation. {ECO:0000269|PubMed:16233225,
CC       ECO:0000269|PubMed:17264217}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione +
CC         O2 = (1E,2Z)-3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-
CC         dien-4-oate + H(+); Xref=Rhea:RHEA:21352, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15896, ChEBI:CHEBI:63690;
CC         EC=1.13.11.25;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow on cholesterol at a
CC       rate that is 60% that of the wild-type and develop a pink color
CC       consistent with the accumulation and nonenzymatic oxidation of a
CC       catechol. {ECO:0000269|PubMed:17264217}.
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000431; ABG96327.1; -; Genomic_DNA.
DR   EMBL; AB030672; BAA98137.1; -; Genomic_DNA.
DR   RefSeq; WP_011596919.1; NC_008268.1.
DR   AlphaFoldDB; Q9KWQ5; -.
DR   SMR; Q9KWQ5; -.
DR   STRING; 101510.RHA1_ro04541; -.
DR   EnsemblBacteria; ABG96327; ABG96327; RHA1_ro04541.
DR   KEGG; rha:RHA1_ro04541; -.
DR   PATRIC; fig|101510.16.peg.4577; -.
DR   eggNOG; COG0346; Bacteria.
DR   HOGENOM; CLU_052361_2_0_11; -.
DR   OMA; KMSATLG; -.
DR   BioCyc; MetaCyc:MON-16964; -.
DR   UniPathway; UPA00296; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0047071; F:3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IDA:UniProtKB.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0070723; P:response to cholesterol; IEP:UniProtKB.
DR   Gene3D; 3.10.180.10; -; 2.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR037523; VOC.
DR   InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; SSF54593; 2.
DR   PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR   PROSITE; PS51819; VOC; 2.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Cholesterol metabolism; Dioxygenase;
KW   Iron; Lipid degradation; Lipid metabolism; Metal-binding; Oxidoreductase;
KW   Reference proteome; Repeat; Steroid metabolism; Sterol metabolism.
FT   CHAIN           1..300
FT                   /note="Iron-dependent extradiol dioxygenase"
FT                   /id="PRO_0000404508"
FT   DOMAIN          5..120
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          142..270
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         145
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   300 AA;  33515 MW;  6F46E2DDCC986C2D CRC64;
     MSIRSLAYMR IEATDMSAWR EYGLKVLGMV EGKGSDPDAL YLRMDDFPAR LVIFPGEHDR
     LSVSGWETAN AAELQEVRDN LSAAGVAFKE GTAEQLQDRR VDELITFEDP SGNTLEAFHG
     AALEHRRVVS PYGHKFVTGE QGLGHVVLST TDDEASLRFY RDVLGFRLRD SMRLPPQLVG
     RPADGKPAWL RFFGCNPRHH SLAFLPMPTP SGIVHLMIEV ENSDDVGLCL DRALRKKVKM
     SATLGRHVND LMLSFYMKTP GGFDIEFGCE GRQVEDESWI ARESTAVSLW GHDFSVGMQP