HSAB_RHOJR
ID HSAB_RHOJR Reviewed; 195 AA.
AC Q0S808;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=RHA1_ro04542;
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
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 [2]
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 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, ECO:0000269|PubMed:17264217}.
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}.
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DR EMBL; CP000431; ABG96328.1; -; Genomic_DNA.
DR RefSeq; WP_005244804.1; NC_008268.1.
DR AlphaFoldDB; Q0S808; -.
DR SMR; Q0S808; -.
DR STRING; 101510.RHA1_ro04542; -.
DR EnsemblBacteria; ABG96328; ABG96328; RHA1_ro04542.
DR GeneID; 66784015; -.
DR KEGG; rha:RHA1_ro04542; -.
DR eggNOG; COG1853; Bacteria.
DR HOGENOM; CLU_059021_1_0_11; -.
DR OMA; WFDRGYH; -.
DR BioCyc; MetaCyc:MON-16962; -.
DR UniPathway; UPA00062; -.
DR Proteomes; UP000008710; 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 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; FAD; Flavoprotein; FMN;
KW Lipid degradation; Lipid metabolism; NAD; Oxidoreductase;
KW Reference proteome; Steroid metabolism.
FT CHAIN 1..195
FT /note="Flavin-dependent monooxygenase, reductase subunit
FT HsaB"
FT /id="PRO_0000404506"
FT BINDING 42..46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 48..49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 63..65
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 69..70
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 95..96
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 160..163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 195 AA; 21233 MW; B7ABFDC15005724F CRC64;
MSEVTGDGAV AAEAIDPRRF RTVLGQFCTG VTIITTIDDG VPVGFACQSF AALSLEPPLV
LFCPTKTSRS WAAIERSGIF CVNVLAEEQQ STCARFGSRD PDKFAGIDWT ESPLGSPILT
GSLAHIDCSL ESVHDGGDHW VAFGRVSSLS EIREERPLLF YRGQYTGIEP DKTVPAPWRD
DLEAFLTTSS EDTWL
