ID   NFNB_ENTCL     STANDARD;      PRT;   217 AA.
AC   Q01234;
DT   01-JUL-1993 (Rel. 26, Created)
DT   01-JUL-1993 (Rel. 26, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Oxygen-insensitive NAD(P)H nitroreductase (EC 1.-.-.-).
GN   Name=nfnB; Synonyms=nfsI;
OS   Enterobacter cloacae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 43560 / 96-3;
RX   MEDLINE=91154203; PubMed=1999406;
RA   Bryant C., Hubbard L., McElroy W.D.;
RT   "Cloning, nucleotide sequence, and expression of the nitroreductase
RT   gene from Enterobacter cloacae.";
RL   J. Biol. Chem. 266:4126-4130(1991).
RN   [2]
RP   CHARACTERIZATION.
RX   MEDLINE=91154202; PubMed=1999405;
RA   Bryant C., Deluca M.;
RT   "Purification and characterization of an oxygen-insensitive NAD(P)H
RT   nitroreductase from Enterobacter cloacae.";
RL   J. Biol. Chem. 266:4119-4125(1991).
CC   -!- FUNCTION: Reduction of a variety of nitroaromatic compounds using
CC       NADH (and to lesser extent NADPH) as source of reducing
CC       equivalents; two electrons are transferred.
CC   -!- COFACTOR: FMN.
CC   -!- PATHWAY: The nitroreductase might be involved in the quinone
CC       metabolism. It shows functional similarity to mammalian quinone
CC       reductases.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the nitroreductase family.
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 as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; M63808; AAA62801.1; -.
DR   PIR; A38686; A38686.
DR   PDB; 1KQB; X-ray; A/B/C/D=1-217.
DR   PDB; 1KQC; X-ray; A/B/C/D=1-217.
DR   PDB; 1KQD; X-ray; A/B/C/D=1-217.
DR   PDB; 1NEC; X-ray; A/B/C/D=2-217.
DR   InterPro; IPR000415; Nitroreductase.
DR   Pfam; PF00881; Nitroreductase; 1.
KW   3D-structure; Flavoprotein; FMN; NAD; NADP; Oxidoreductase.
FT   NP_BIND     153    158       NAD or NADP (By similarity).
FT   HELIX         3      9
FT   STRAND       12     12
FT   STRAND       16     16
FT   TURN         18     19
FT   HELIX        24     36
FT   HELIX        40     42
FT   STRAND       46     51
FT   HELIX        54     60
FT   HELIX        61     63
FT   HELIX        66     71
FT   HELIX        72     77
FT   STRAND       80     87
FT   HELIX        92    104
FT   TURN        105    106
FT   HELIX       111    129
FT   TURN        130    132
FT   HELIX       135    156
FT   TURN        157    158
FT   STRAND      160    161
FT   STRAND      164    164
FT   HELIX       169    175
FT   TURN        176    177
FT   HELIX       178    181
FT   TURN        182    182
FT   STRAND      183    192
FT   STRAND      194    194
FT   TURN        196    197
FT   HELIX       199    201
FT   TURN        202    202
FT   HELIX       210    213
FT   STRAND      214    217
SQ   SEQUENCE   217 AA;  23950 MW;  C42AA3DB184D5D9B CRC64;
     MDIISVALKR HSTKAFDASK KLTAEEAEKI KTLLQYSPSS TNSQPWHFIV ASTEEGKARV
     AKSAAGTYVF NERKMLDASH VVVFCAKTAM DDAWLERVVD QEEADGRFNT PEAKAANHKG
     RTYFADMHRV DLKDDDQWMA KQVYLNVGNF LLGVGAMGLD AVPIEGFDAA ILDEEFGLKE
     KGFTSLVVVP VGHHSVEDFN ATLPKSRLPL STIVTEC
//