HSAA_MYCTO
ID HSAA_MYCTO Reviewed; 394 AA.
AC P9WJA0; L0TCY6; P96852; Q7D595;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Flavin-dependent monooxygenase, oxygenase subunit HsaA {ECO:0000250|UniProtKB:P9WJA1};
DE EC=1.14.14.12 {ECO:0000250|UniProtKB:P9WJA1};
DE AltName: Full=3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4-hydroxylase, oxygenase subunit {ECO:0000250|UniProtKB:P9WJA1};
DE AltName: Full=3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase {ECO:0000250|UniProtKB:P9WJA1};
GN Name=hsaA {ECO:0000250|UniProtKB:P9WJA1}; OrderedLocusNames=MT3675;
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 o-hydroxylation of 3-hydroxy-9,10-secoandrosta-
CC 1,3,5(10)-triene-9,17-dione (3-HSA) to 3,4-dihydroxy-9,10-secoandrosta-
CC 1,3,5(10)-triene-9,17-dione (3,4-DHSA) in the catabolism of
CC cholesterol. {ECO:0000250|UniProtKB:P9WJA1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione +
CC FMNH2 + O2 = 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-
CC dione + FMN + H(+) + H2O; Xref=Rhea:RHEA:31731, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15896,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:63245;
CC EC=1.14.14.12; Evidence={ECO:0000250|UniProtKB:P9WJA1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31732;
CC Evidence={ECO:0000250|UniProtKB:P9WJA1};
CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC {ECO:0000250|UniProtKB:P9WJA1}.
CC -!- SUBUNIT: Homotetramer under anaerobic conditions. HsaAB monooxygenase
CC consists of an oxygenase component HsaA and a reductase component HsaB.
CC {ECO:0000250|UniProtKB:P9WJA1}.
CC -!- SIMILARITY: Belongs to the HpaH/HsaA monooxygenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000516; AAK48034.1; -; Genomic_DNA.
DR PIR; H70605; H70605.
DR RefSeq; WP_003900101.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WJA0; -.
DR SMR; P9WJA0; -.
DR EnsemblBacteria; AAK48034; AAK48034; MT3675.
DR KEGG; mtc:MT3675; -.
DR PATRIC; fig|83331.31.peg.3957; -.
DR HOGENOM; CLU_018204_2_0_11; -.
DR UniPathway; UPA00062; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0036383; F:3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; FAD; Flavoprotein; FMN;
KW Lipid degradation; Lipid metabolism; Monooxygenase; Oxidoreductase;
KW Steroid metabolism.
FT CHAIN 1..394
FT /note="Flavin-dependent monooxygenase, oxygenase subunit
FT HsaA"
FT /id="PRO_0000427866"
FT BINDING 84
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 118..120
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 141..143
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 346..347
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 368..369
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
SQ SEQUENCE 394 AA; 43143 MW; F3103435D8EB1485 CRC64;
MTSIQQRDAQ SVLAAIDNLL PEIRDRAQAT EDLRRLPDET VKALDDVGFF TLLQPQQWGG
LQCDPALFFE ATRRLASVCG STGWVSSIVG VHNWHLALFD QRAQEEVWGE DPSTRISSSY
APMGAGVVVD GGYLVNGSWN WSSGCDHASW TFVGGPVIKD GRPVDFGSFL IPRSEYEIKD
VWYVVGLRGT GSNTLVVKDV FVPRHRFLSY KAMNDHTAGG LATNSAPVYK MPWGTMHPTT
ISAPIVGMAY GAYAAHVEHQ GKRVRAAFAG EKAKDDPFAK VRIAEAASDI DAAWRQLIGN
VSDEYALLAA GKEIPFELRA RARRDQVRAT GRSIASIDRL FEASGATALS NEAPIQRFWR
DAHAGRVHAA NDPERAYVIF GNHEFGLPPG DTMV
