HSAB_MYCTU
ID HSAB_MYCTU Reviewed; 187 AA.
AC P9WND9; 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 39.
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=Rv3567c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17635188; DOI=10.1111/j.1365-2958.2007.05827.x;
RA Kendall S.L., Withers M., Soffair C.N., Moreland N.J., Gurcha S.,
RA Sidders B., Frita R., Ten Bokum A., Besra G.S., Lott J.S., Stoker N.G.;
RT "A highly conserved transcriptional repressor controls a large regulon
RT involved in lipid degradation in Mycobacterium smegmatis and Mycobacterium
RT tuberculosis.";
RL Mol. Microbiol. 65:684-699(2007).
RN [3]
RP FUNCTION AS A COMPONENT OF THE FLAVIN-DEPENDENT MONOOXYGENASE, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20448045; DOI=10.1074/jbc.m109.099028;
RA Dresen C., Lin L.Y., D'Angelo I., Tocheva E.I., Strynadka N., Eltis L.D.;
RT "A flavin-dependent monooxygenase from Mycobacterium tuberculosis involved
RT in cholesterol catabolism.";
RL J. Biol. Chem. 285:22264-22275(2010).
CC -!- FUNCTION: Catalyzes the reduction of free flavins (FMN or FAD) by NADH.
CC Subsequently, the reduced flavins diffuse to the HsaA oxygenase
CC subunit. {ECO:0000269|PubMed:20448045}.
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.
CC -!- INDUCTION: Induced by KstR. {ECO:0000269|PubMed:17635188}.
CC -!- MISCELLANEOUS: Cholesterol metabolism contributes to the survival of
CC M.tuberculosis in the host by helping the bacterial multiplication
CC during earlier stages of infection and to the dissemination of the
CC pathogen in the host.
CC -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46390.1; -; Genomic_DNA.
DR PIR; E70605; E70605.
DR RefSeq; NP_218084.1; NC_000962.3.
DR RefSeq; WP_003900713.1; NZ_NVQJ01000014.1.
DR AlphaFoldDB; P9WND9; -.
DR SMR; P9WND9; -.
DR STRING; 83332.Rv3567c; -.
DR PaxDb; P9WND9; -.
DR DNASU; 887525; -.
DR GeneID; 887525; -.
DR KEGG; mtu:Rv3567c; -.
DR TubercuList; Rv3567c; -.
DR eggNOG; COG1853; Bacteria.
DR OMA; WFDRGYH; -.
DR PhylomeDB; P9WND9; -.
DR BioCyc; MetaCyc:G185E-7845-MON; -.
DR UniPathway; UPA00062; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0036382; F:flavin reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016646; F:oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor; IDA:MTBBASE.
DR GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006707; P:cholesterol catabolic process; IDA:MTBBASE.
DR GO; GO:0006694; P:steroid biosynthetic process; IDA:UniProtKB.
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..187
FT /note="Flavin-dependent monooxygenase, reductase subunit
FT HsaB"
FT /id="PRO_0000404505"
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
