ID   HSAC_MYCTO              Reviewed;         300 AA.
AC   P9WNW6; L0TFW3; P96850; Q7D597;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Iron-dependent extradiol dioxygenase;
DE            EC=1.13.11.25;
GN   Name=hsaC; Synonyms=bphC; OrderedLocusNames=MT3673;
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 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). {ECO:0000250}.
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, but may form a homooctamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK48032.1; -; Genomic_DNA.
DR   PIR; F70605; F70605.
DR   RefSeq; WP_003419378.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNW6; -.
DR   SMR; P9WNW6; -.
DR   PRIDE; P9WNW6; -.
DR   EnsemblBacteria; AAK48032; AAK48032; MT3673.
DR   KEGG; mtc:MT3673; -.
DR   PATRIC; fig|83331.31.peg.3955; -.
DR   HOGENOM; CLU_052361_2_0_11; -.
DR   UniPathway; UPA00296; -.
DR   Proteomes; UP000001020; 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: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   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   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Cholesterol metabolism; Dioxygenase;
KW   Iron; Lipid degradation; Lipid metabolism; Metal-binding; Oxidoreductase;
KW   Repeat; Steroid metabolism; Sterol metabolism.
FT   CHAIN           1..300
FT                   /note="Iron-dependent extradiol dioxygenase"
FT                   /id="PRO_0000427055"
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;  33582 MW;  2AA94528D119ACB0 CRC64;
     MSIRSLGYLR IEATDMAAWR EYGLKVLGMV EGKGAPEGAL YLRMDDFPAR LVVVPGEHDR
     LLEAGWECAN AEGLQEIRNR LDLEGTPYKE ATAAELADRR VDEMIRFADP SGNCLEVFHG
     TALEHRRVVS PYGHRFVTGE QGMGHVVLST RDDAEALHFY RDVLGFRLRD SMRLPPQMVG
     RPADGPPAWL RFFGCNPRHH SLAFLPMPTS SGIVHLMVEV EQADDVGLCL DRALRRKVPM
     SATLGRHVND LMLSFYMKTP GGFDIEFGCE GRQVDDRDWI ARESTAVSLW GHDFTVGARG