ID   HSAB_MYCTO              Reviewed;         187 AA.
AC   P9WND8; L0TG39; P96849; Q7D598;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Flavin-dependent monooxygenase, reductase subunit HsaB;
DE            EC=1.5.1.36;
DE   AltName: Full=3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4-hydroxylase, reductase subunit;
DE   AltName: Full=Flavin:NADH reductase;
GN   Name=hsaB; OrderedLocusNames=MT3672;
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 reduction of free flavins (FMN or FAD) by NADH.
CC       Subsequently, the reduced flavins diffuse to the HsaA oxygenase subunit
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a reduced flavin + NAD(+) = an oxidized flavin + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:31303, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:60531, ChEBI:CHEBI:62787; EC=1.5.1.36;
CC   -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC   -!- SUBUNIT: HsaAB monooxygenase consists of an oxygenase component HsaA
CC       and a reductase component HsaB. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase 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; AAK48031.1; -; Genomic_DNA.
DR   PIR; E70605; E70605.
DR   RefSeq; WP_003900713.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WND8; -.
DR   SMR; P9WND8; -.
DR   EnsemblBacteria; AAK48031; AAK48031; MT3672.
DR   KEGG; mtc:MT3672; -.
DR   PATRIC; fig|83331.31.peg.3954; -.
DR   HOGENOM; CLU_059021_1_0_11; -.
DR   UniPathway; UPA00062; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0036382; F:flavin reductase (NADH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0010181; F:FMN binding; 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; 2.30.110.10; -; 1.
DR   InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   Pfam; PF01613; Flavin_Reduct; 1.
DR   SMART; SM00903; Flavin_Reduct; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; FAD; Flavoprotein; FMN;
KW   Lipid degradation; Lipid metabolism; NAD; Oxidoreductase;
KW   Steroid metabolism.
FT   CHAIN           1..187
FT                   /note="Flavin-dependent monooxygenase, reductase subunit
FT                   HsaB"
FT                   /id="PRO_0000427144"
FT   BINDING         32..36
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         38..39
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         53..55
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..60
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         85..86
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         152..155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   187 AA;  20539 MW;  4FF7CCE26F797BD1 CRC64;
     MSAQIDPRTF RSVLGQFCTG ITVITTVHDD VPVGFACQSF AALSLEPPLV LFCPTKVSRS
     WQAIEASGRF CVNVLTEKQK DVSARFGSKE PDKFAGIDWR PSELGSPIIE GSLAYIDCTV
     ASVHDGGDHF VVFGAVESLS EVPAVKPRPL LFYRGDYTGI EPEKTTPAHW RDDLEAFLIT
     TTQDTWL