ID   UBIB_ECOLI     STANDARD;      PRT;   232 AA.
AC   P23486; P76768;
DT   01-NOV-1991 (Rel. 20, Created)
DT   01-NOV-1991 (Rel. 20, Last sequence update)
DT   15-JUL-1998 (Rel. 36, Last annotation update)
DE   NAD(P)H-FLAVIN REDUCTASE (EC 1.6.8.*) (FERRISIDEROPHORE REDUCTASE C).
GN   UBIB OR FRE OR FLRD OR FADI OR FSRC.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 1-20.
RX   MEDLINE; 91267929.
RA   SPYROU G., HAGGAARD-LJUNGQUIST E., KROOK M., JOERNVALL H.,
RA   NILSSON E., REICHARD P.;
RT   "Characterization of the flavin reductase gene (fre) of Escherichia
RT   coli and construction of a plasmid for overproduction of the
RT   enzyme.";
RL   J. Bacteriol. 173:3673-3679(1991).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12;
RA   DIRUSSO C.C., SHEA O.;
RL   Submitted (XXX-1991) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE; 92358234.
RA   DANIELS D.L., PLUNKETT G. III, BURLAND V.D., BLATTNER F.R.;
RT   "Analysis of the Escherichia coli genome: DNA sequence of the region
RT   from 84.5 to 86.5 minutes.";
RL   Science 257:771-778(1992).
RN   [4]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12;
RA   SAVIRANTA P.J.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   CHARACTERIZATION.
RC   STRAIN=K12;
RX   MEDLINE; 92290008.
RA   ANDREWS S.C., SHIPLEY D., KEEN J.N., FINDLAY J.B.C., HARRISON P.M.,
RA   GUEST J.R.;
RT   "The haemoglobin-like protein (HMP) of Escherichia coli has
RT   ferrisiderophore reductase activity and its C-terminal domain shares
RT   homology with ferredoxin NADP+ reductases.";
RL   FEBS Lett. 302:247-252(1992).
CC   -!- FUNCTION: CATALYZES THE REDUCTION OF SOLUBLE FLAVINS BY REDUCED
CC       PYRIDINE NUCLEOTIDES. SEEMS TO REDUCES THE COMPLEXED FE+3 IRON OF
CC       SIDEROPHORES TO FE+2, THUS RELEASING IT FROM THE CHELATOR.
CC   -!- SUBUNIT: MONOMER.
CC   -!- SIMILARITY: BELONGS TO THE FRE/LUXG FAMILY OF FAD/NAD(P)
CC       FLAVOPROTEIN OXIDOREDUCTASES.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M61182; AAA23806.1; -.
DR   EMBL; M85227; AAA23753.1; -.
DR   EMBL; M87049; AAA67641.1; -.
DR   EMBL; AE000459; AAC76847.1; -.
DR   EMBL; M74448; AAA91058.1; -.
DR   PIR; A39434; A39434.
DR   PIR; S30735; S30735.
DR   ECOGENE; EG10334; ubiB.
DR   PFAM; PF00175; oxidored_fad; 1.
KW   Oxidoreductase; FAD; Flavoprotein; NADP; Iron transport.
FT   INIT_MET      0      0
FT   NP_BIND     110    114       PYRIDINE (BY SIMILARITY).
SQ   SEQUENCE   232 AA;  26111 MW;  5F2A1AB6E2D52670 CRC64;
     TTLSCKVTSV EAITDTVYRV RIVPDAAFSF RAGQYLMVVM DERDKRPFSM ASTPDEKGFI
     ELHIGASEIN LYAKAVMDRI LKDHQIVVDI PHGEAWLRDD EERPMILIAG GTGFSYARSI
     LLTALARNPN RDITIYWGGR EEQHLYDLCE LEALSLKHPG LQVVPVVEQP EAGWRGRTGT
     VLTAVLQDHG TLAEHDIYIA GRFEMAKIAR DLFCSERNAR EDRLFGDAFA FI
//