VLMR_STRVF
ID VLMR_STRVF Reviewed; 194 AA.
AC O34138;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=NADPH-flavin oxidoreductase {ECO:0000303|PubMed:9287340};
DE EC=1.5.1.38 {ECO:0000269|PubMed:9287340};
DE AltName: Full=FAD reductase (NADPH) {ECO:0000303|PubMed:9287340};
DE AltName: Full=FMN reductase (NADPH) {ECO:0000303|PubMed:9287340};
DE AltName: Full=Isobutylamine N-hydroxylase, reductase component {ECO:0000305};
GN Name=vlmR {ECO:0000303|PubMed:9287340};
OS Streptomyces viridifaciens.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=48665;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=MG456-hF10 {ECO:0000312|EMBL:AAN10239.1};
RX PubMed=9056232; DOI=10.1006/abbi.1996.9857;
RA Parry R.J., Li W.;
RT "Purification and characterization of isobutylamine N-hydroxylase from the
RT valanimycin producer Streptomyces viridifaciens MG456-hF10.";
RL Arch. Biochem. Biophys. 339:47-54(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MG456-hF10 {ECO:0000312|EMBL:AAN10239.1};
RX PubMed=8990292; DOI=10.1128/jb.179.2.409-416.1997;
RA Parry R.J., Li W., Cooper H.N.;
RT "Cloning, analysis, and overexpression of the gene encoding isobutylamine
RT N-hydroxylase from the valanimycin producer, Streptomyces viridifaciens.";
RL J. Bacteriol. 179:409-416(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBSTRATE SPECIFICITY.
RC STRAIN=MG456-hF10 {ECO:0000312|EMBL:AAC45645.1};
RX PubMed=9287340; DOI=10.1074/jbc.272.37.23303;
RA Parry R.J., Li W.;
RT "An NADPH:FAD oxidoreductase from the valanimycin producer, Streptomyces
RT viridifaciens. Cloning, analysis, and overexpression.";
RL J. Biol. Chem. 272:23303-23311(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MG456-hF10 {ECO:0000312|EMBL:AAN10239.1};
RX PubMed=10708373; DOI=10.1099/00221287-146-2-345;
RA Ma Y., Patel J., Parry R.J.;
RT "A novel valanimycin-resistance determinant (vlmF) from Streptomyces
RT viridifaciens MG456-hF10.";
RL Microbiology 146:345-352(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MG456-hF10 {ECO:0000312|EMBL:AAN10239.1};
RX PubMed=12406225; DOI=10.1046/j.1365-2958.2002.03169.x;
RA Garg R.P., Ma Y., Hoyt J.C., Parry R.J.;
RT "Molecular characterization and analysis of the biosynthetic gene cluster
RT for the azoxy antibiotic valanimycin.";
RL Mol. Microbiol. 46:505-517(2002).
CC -!- FUNCTION: Involved in the biosynthesis of the azoxy antibiotic
CC valanimycin, which has an antitumor activity. Catalyzes the reduction
CC of FAD/FMN to FADH(2)/FMNH(2) which are subsequently used for the
CC hydroxylation of isobutylamine by the isobutylamine N-hydroxylase VlmH.
CC It can reduce either FAD or flavin mononucleotide (FMN) but prefers
CC FAD. The enzyme has a strong preference for NADPH as acceptor.
CC {ECO:0000269|PubMed:9287340, ECO:0000305|PubMed:9056232}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FADH2 + NADP(+) = FAD + 2 H(+) + NADPH; Xref=Rhea:RHEA:30151,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:9287340};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FMNH2 + NADP(+) = FMN + 2 H(+) + NADPH; Xref=Rhea:RHEA:21624,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.5.1.38;
CC Evidence={ECO:0000269|PubMed:9287340};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.6 uM for FAD {ECO:0000269|PubMed:9287340};
CC KM=8.4 uM for FMN {ECO:0000269|PubMed:9287340};
CC KM=11.1 uM for riboflavin {ECO:0000269|PubMed:9287340};
CC KM=32 uM for NADPH (with 40 mM FAD) {ECO:0000269|PubMed:9287340};
CC Note=kcat is 62 sec(-1) for NADPH as substrate (with 40 mM FAD). kcat
CC is 51 sec(-1) for FAD as substrate. kcat is 45 sec(-1) for FMN as
CC substrate. kcat is 6.7 sec(-1) for riboflavin as substrate.
CC {ECO:0000269|PubMed:9287340};
CC -!- SUBUNIT: Homodimer (PubMed:9287340). It can form an isobutylamine N-
CC hydroxylase two component enzyme system formed of a flavin reductase
CC component (VlmR) and a monooxygenase component (VlmH).
CC {ECO:0000269|PubMed:9287340}.
CC -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC {ECO:0000305}.
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DR EMBL; U93606; AAC45645.1; -; Genomic_DNA.
DR EMBL; AY116644; AAN10239.1; -; Genomic_DNA.
DR AlphaFoldDB; O34138; -.
DR SMR; O34138; -.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0052873; F:FMN reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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 Antibiotic biosynthesis; FAD; Flavoprotein; FMN; NADP; Oxidoreductase.
FT CHAIN 1..194
FT /note="NADPH-flavin oxidoreductase"
FT /id="PRO_0000443527"
SQ SEQUENCE 194 AA; 21264 MW; D4442F2B04FE38F2 CRC64;
MTPSAAATGH EAADEQRLRE LRGLTRQLPT GVAVVTAQDG EVAHGATVST VSVLSQQPLR
IGVSLRRGSY LTGLIRQRRV FALNVLSSRQ SAVADWFANP ERPRGWRQFD YVRWTAHPKA
GMPVLEDALA QLHCRLTDLI PLGASDDLLV AEVLDGRGRN GRPLVNFNGR LHDVEFRGVV
RVSRDQPSAV TSLE
