MSUE_PSEPK
ID MSUE_PSEPK Reviewed; 186 AA.
AC Q88J85;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=FMN reductase (NADPH);
DE EC=1.5.1.38;
DE AltName: Full=FMN reductase;
GN Name=msuE; OrderedLocusNames=PP_2764;
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 -!- 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; AAN68372.1; -; Genomic_DNA.
DR RefSeq; NP_744908.2; NC_002947.4.
DR RefSeq; WP_004576525.1; NC_002947.4.
DR PDB; 4C76; X-ray; 1.96 A; A/B=1-184.
DR PDBsum; 4C76; -.
DR AlphaFoldDB; Q88J85; -.
DR SMR; Q88J85; -.
DR STRING; 160488.PP_2764; -.
DR PRIDE; Q88J85; -.
DR EnsemblBacteria; AAN68372; AAN68372; PP_2764.
DR KEGG; ppu:PP_2764; -.
DR PATRIC; fig|160488.4.peg.2931; -.
DR eggNOG; COG0431; Bacteria.
DR HOGENOM; CLU_055322_3_3_6; -.
DR OMA; YAMRPLF; -.
DR PhylomeDB; Q88J85; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0052873; F:FMN reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProt.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR InterPro; IPR019912; FMN_Rdtase_MsuE-like.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR TIGRFAMs; TIGR03566; FMN_reduc_MsuE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..186
FT /note="FMN reductase (NADPH)"
FT /id="PRO_0000160595"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:4C76"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:4C76"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:4C76"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:4C76"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:4C76"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4C76"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:4C76"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4C76"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:4C76"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:4C76"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:4C76"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:4C76"
FT TURN 103..108
FT /evidence="ECO:0007829|PDB:4C76"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:4C76"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:4C76"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:4C76"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:4C76"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:4C76"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:4C76"
FT HELIX 161..177
FT /evidence="ECO:0007829|PDB:4C76"
SQ SEQUENCE 186 AA; 20420 MW; A6FB6FE6FB6BFFF8 CRC64;
MNARVIRVVV VSGSLRAPSR THGLLQALVE RLPAVLPKLE VHWVRIAELS ASLAGSLERD
SASADLQPHL QAIEQADLLL VGSPVYRASY TGLFKHLFDL VDHQSLKGVP VVLAATGGSE
RHALMIDHQL RPLFAFFQAH TLPYGLYASV ESFDDQRLAD PAQFERIERV LDTVGAFFHI
PVARAA
