FRE_SALTY
ID FRE_SALTY Reviewed; 233 AA.
AC Q9L6L9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=NAD(P)H-flavin reductase;
DE EC=1.5.1.41 {ECO:0000269|PubMed:10894741};
DE AltName: Full=FMN reductase;
DE AltName: Full=Ferrisiderophore reductase C;
DE AltName: Full=NAD(P)H:flavin oxidoreductase;
DE AltName: Full=Riboflavin reductase [NAD(P)H];
GN Name=fre; Synonyms=ubiB; OrderedLocusNames=STM3979; ORFNames=STMD1.10;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP PROTEIN SEQUENCE OF 2-16, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10894741; DOI=10.1128/jb.182.15.4304-4309.2000;
RA Fonseca M.V., Escalante-Semerena J.C.;
RT "Reduction of Cob(III)alamin to Cob(II)alamin in Salmonella enterica
RT serovar typhimurium LT2.";
RL J. Bacteriol. 182:4304-4309(2000).
CC -!- FUNCTION: Catalyzes the reduction of soluble flavins by reduced
CC pyridine nucleotides. {ECO:0000269|PubMed:10894741}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + reduced riboflavin = 2 H(+) + NADPH + riboflavin;
CC Xref=Rhea:RHEA:19377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17607,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57986, ChEBI:CHEBI:58349; EC=1.5.1.41;
CC Evidence={ECO:0000269|PubMed:10894741};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + reduced riboflavin = 2 H(+) + NADH + riboflavin;
CC Xref=Rhea:RHEA:31455, ChEBI:CHEBI:15378, ChEBI:CHEBI:17607,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57986; EC=1.5.1.41;
CC Evidence={ECO:0000269|PubMed:10894741};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P0AEN1}.
CC -!- SIMILARITY: Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AF233324; AAF33411.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22823.1; -; Genomic_DNA.
DR RefSeq; NP_462864.1; NC_003197.2.
DR RefSeq; WP_000209831.1; NC_003197.2.
DR AlphaFoldDB; Q9L6L9; -.
DR SMR; Q9L6L9; -.
DR STRING; 99287.STM3979; -.
DR PaxDb; Q9L6L9; -.
DR PRIDE; Q9L6L9; -.
DR EnsemblBacteria; AAL22823; AAL22823; STM3979.
DR GeneID; 1255505; -.
DR KEGG; stm:STM3979; -.
DR PATRIC; fig|99287.12.peg.4198; -.
DR HOGENOM; CLU_003827_7_4_6; -.
DR OMA; PCRHEGE; -.
DR PhylomeDB; Q9L6L9; -.
DR BioCyc; MetaCyc:MON-13237; -.
DR BioCyc; SENT99287:STM3979-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0052875; F:riboflavin reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; FMN; Ion transport; Iron;
KW Iron transport; NAD; NADP; Oxidoreductase; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..233
FT /note="NAD(P)H-flavin reductase"
FT /id="PRO_0000068147"
FT DOMAIN 2..119
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 111..115
FT /ligand="pyridine"
FT /ligand_id="ChEBI:CHEBI:16227"
FT /evidence="ECO:0000250"
SQ SEQUENCE 233 AA; 26351 MW; 200AE5691041B715 CRC64;
MTTLSCKVTS VEAITDTVYR VRLVPDAAFS FRAGQYLMVV MDERDKRPFS MASTPDEKGF
IELHIGASEL NLYAMAVMDR ILKDREIVVD IPHGDAWLRD DEERPLILIA GGTGFSYVRS
ILLTALARNP ARDVTIYWGG REEKHLYDLS ELEALSVNHP NLRIEPVVEQ PEEGWRGRTG
TVLTAVLQDY GTLAGHDIYI AGRFEMAKIA RDLFCHERNA REDRLFGDAF AFI
