FRED_PSEPU
ID FRED_PSEPU Reviewed; 170 AA.
AC M4YFG7;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Flavin reductase {ECO:0000303|PubMed:23524667};
DE Short=Fred {ECO:0000303|PubMed:23524667};
DE AltName: Full=FAD reductase {ECO:0000305|PubMed:23524667};
DE EC=1.5.1.37 {ECO:0000269|PubMed:23524667};
DE AltName: Full=FMN reductase {ECO:0000303|PubMed:23524667};
DE EC=1.5.1.42 {ECO:0000269|PubMed:23524667};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-29 AND 45-68,
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION, AND SUBUNIT.
RC STRAIN=ATCC 17453 / DSM 50198 / JCM 6157 / NCIMB 10007 / NRRL B-4067 /
RC Stanier 77 / Biotype A;
RX PubMed=23524667; DOI=10.1128/aem.03958-12;
RA Iwaki H., Grosse S., Bergeron H., Leisch H., Morley K., Hasegawa Y.,
RA Lau P.C.K.;
RT "Camphor pathway redux: functional recombinant expression of 2,5- and 3,6-
RT diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their
RT cognate flavin reductase catalyzing Baeyer-Villiger reactions.";
RL Appl. Environ. Microbiol. 79:3282-3293(2013).
CC -!- FUNCTION: Catalyzes the reduction of FMN, and to a lesser extent, FAD,
CC using NADH as an electron donor. Is able to provide the FMNH(2)
CC required for the Baeyer-Villiger oxidations catalyzed by 2,5-
CC diketocamphane monooxygenases and 3,6-diketocamphane monooxygenase.
CC NADPH acts as a very poor cosubstrate. {ECO:0000269|PubMed:23524667}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FMNH2 + NAD(+) = FMN + 2 H(+) + NADH; Xref=Rhea:RHEA:21620,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58210; EC=1.5.1.42;
CC Evidence={ECO:0000269|PubMed:23524667};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FADH2 + NAD(+) = FAD + 2 H(+) + NADH; Xref=Rhea:RHEA:30147,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58307; EC=1.5.1.37;
CC Evidence={ECO:0000269|PubMed:23524667};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.6 uM for FMN {ECO:0000269|PubMed:23524667};
CC KM=19 uM for FAD {ECO:0000269|PubMed:23524667};
CC KM=32 uM for NADH {ECO:0000269|PubMed:23524667};
CC Note=kcat is 283 sec(-1) for the reduction of FMN. kcat is 128 sec(-
CC 1) for the reduction of FAD.;
CC pH dependence:
CC Optimum pH is 7.5 in Tris/HCl buffer. {ECO:0000269|PubMed:23524667};
CC Temperature dependence:
CC Optimum temperature is 30-35 degrees Celsius. Has a half-life of
CC about 80 minutes at 25 degrees Celsius.
CC {ECO:0000269|PubMed:23524667};
CC -!- SUBUNIT: Homodimer. Likely forms a loose transient complex with
CC monooxygenases for which it provides FMNH(2).
CC {ECO:0000269|PubMed:23524667}.
CC -!- INDUCTION: By (+)-camphor. {ECO:0000269|PubMed:23524667}.
CC -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC {ECO:0000305}.
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DR EMBL; KC349947; AGI42835.1; -; Genomic_DNA.
DR AlphaFoldDB; M4YFG7; -.
DR SMR; M4YFG7; -.
DR BRENDA; 1.5.1.37; 5092.
DR BRENDA; 1.5.1.42; 5092.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0052874; F:FMN reductase (NADH) activity; IEA:RHEA.
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 Direct protein sequencing; FAD; Flavoprotein; FMN; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:23524667"
FT CHAIN 2..170
FT /note="Flavin reductase"
FT /id="PRO_0000444573"
FT BINDING 51
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q5SJP7"
FT BINDING 138
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q5SJP7"
FT BINDING 159..162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q5SJP7"
SQ SEQUENCE 170 AA; 18356 MW; 50A87A605C5B314C CRC64;
MTKVAAEIVR SAIDPQWFRA VLGQYPTGVC AVTAMDPDGK MSGMAVGSFT SVSLNPPLVA
FLPDRSSTSW PKIERAGKFC VNVLSDQQLG VCKRFASKDE DKFSGLVYRL SDNGSPIIEG
VVAWIDCDLH SVQEAGDHYI VIGSVRELQV ESEDSALLFY RGGYGGFAAI
