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   16-JUN-2009, entry version 60.
DE   RecName: Full=NAD(P)H-flavin reductase;
DE            EC=1.5.1.29;
DE            EC=1.16.1.3;
DE   AltName: Full=FMN reductase;
DE   AltName: Full=NAD(P)H:flavin oxidoreductase;
DE   AltName: Full=Aquacobalamin reductase;
DE   AltName: Full=Ferrisiderophore reductase C;
GN   Name=fre; Synonyms=ubiB; OrderedLocusNames=STM3979; ORFNames=STMD1.10;
OS   Salmonella typhimurium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   MEDLINE=21534948; 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.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-16, AND CHARACTERIZATION.
RX   MEDLINE=20353466; PubMed=10894741;
RX   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. Seems to reduces the complexed Fe(3+) iron
CC       of siderophores to Fe(2+), thus releasing it from the chelator (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: FMNH(2) + NAD(P)(+) = FMN + NAD(P)H.
CC   -!- CATALYTIC ACTIVITY: 2 cob(II)alamin + NAD(+) = 2
CC       aquacob(III)alamin + NADH.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the fre/luxG FAD/NAD(P) flavoprotein
CC       oxidoreductase family.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF233324; AAF33411.1; -; Genomic_DNA.
DR   EMBL; AE008885; AAL22823.1; -; Genomic_DNA.
DR   RefSeq; NP_462864.1; -.
DR   HSSP; P23486; 1QFJ.
DR   SMR; Q9L6L9; 2-233.
DR   GeneID; 1255505; -.
DR   GenomeReviews; AE006468_GR; STM3979.
DR   KEGG; stm:STM3979; -.
DR   NMPDR; fig|99287.1.peg.3838; -.
DR   HOGENOM; Q9L6L9; -.
DR   OMA; Q9L6L9; ETTLYWG.
DR   BioCyc; MetaCyc:MON-13237; -.
DR   BioCyc; STYP99287:STM3979-MON; -.
DR   BRENDA; 1.16.1.3; 2.
DR   BRENDA; 1.5.1.29; 2.
DR   GO; GO:0047138; F:aquacobalamin reductase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0008752; F:FMN reductase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR008333; OxRdtase_FAD-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   InterPro; IPR001221; Phe_hydroxylase.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; FAD; Flavoprotein; FMN;
KW   Ion transport; Iron; Iron transport; NAD; NADP; Oxidoreductase;
KW   Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    233       NAD(P)H-flavin reductase.
FT                                /FTId=PRO_0000068147.
FT   DOMAIN        2    119       FAD-binding FR-type.
FT   NP_BIND     111    115       Pyridine (By similarity).
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
//