SSUE_PSEPK
ID SSUE_PSEPK Reviewed; 197 AA.
AC Q88R97;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=FMN reductase (NADPH);
DE EC=1.5.1.38;
DE AltName: Full=FMN reductase;
GN Name=ssuE; OrderedLocusNames=PP_0236;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
CC -!- FUNCTION: Probably forms a two-component reduced flavin mononucleotide-
CC dependent monooxygenase by binding to SsuD. Required for growth on
CC aliphatic sulfonates or methionine but not arylsulfonates (By
CC similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the SsuE family. {ECO:0000305}.
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DR EMBL; AE015451; AAN65868.1; -; Genomic_DNA.
DR RefSeq; NP_742404.1; NC_002947.4.
DR RefSeq; WP_003255835.1; NC_002947.4.
DR AlphaFoldDB; Q88R97; -.
DR SMR; Q88R97; -.
DR STRING; 160488.PP_0236; -.
DR EnsemblBacteria; AAN65868; AAN65868; PP_0236.
DR KEGG; ppu:PP_0236; -.
DR PATRIC; fig|160488.4.peg.252; -.
DR eggNOG; COG0431; Bacteria.
DR HOGENOM; CLU_055322_3_0_6; -.
DR OMA; DVEVCHW; -.
DR PhylomeDB; Q88R97; -.
DR BioCyc; PPUT160488:G1G01-258-MON; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0052873; F:FMN reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0008752; F:FMN reductase activity; IEA:InterPro.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProt.
DR GO; GO:0046306; P:alkanesulfonate catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR InterPro; IPR020048; NADPH-dep_FMN_reduc_SsuE.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR TIGRFAMs; TIGR03567; FMN_reduc_SsuE; 1.
PE 3: Inferred from homology;
KW Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..197
FT /note="FMN reductase (NADPH)"
FT /id="PRO_0000160592"
SQ SEQUENCE 197 AA; 21571 MW; 287C427C33B667AF CRC64;
MLVVSIGGSP SLRSRSGVLL ERSRQWLQDR GVEVVTFQVR DFPAEDLLHA RFDSPHVQHF
QQLVAQADGL IVSTPVYKAS FSGALKTLLD LLPERALAHK IVLPIATGGS IAHMLAVDYA
LKPVLSALKA QETLQGIFAD DSQVAYAEGT KPAQLVQALE ERLHDSLETF HVALARRPRP
VAPGVLNERL ISARWSI