ID   DYR7_ECOLX              Reviewed;         157 AA.
AC   P27422;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-NOV-2008, entry version 53.
DE   RecName: Full=Dihydrofolate reductase type 7;
DE            EC=1.5.1.3;
DE   AltName: Full=Dihydrofolate reductase type VII;
GN   Name=dhfrVII;
OS   Escherichia coli.
OG   Plasmid pLMO27, Plasmid IncP-beta R751, and Plasmid pDGO100.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pLMO27; TRANSPOSON=Tn5086;
RX   PubMed=8383666;
RA   Sundstroem L., Swedberg G., Skoeld O.;
RT   "Characterization of transposon Tn5086, carrying the site-specifically
RT   inserted gene dhfrVII mediating trimethoprim resistance.";
RL   J. Bacteriol. 175:1796-1805(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=IncP-beta R751; TRANSPOSON=Tn5090;
RX   MEDLINE=94252994; PubMed=8195081;
RA   Raadstroem P., Skoeld O., Swedberg G., Flensburg J., Roy P.H.,
RA   Sundstroem L.;
RT   "Transposon Tn5090 of plasmid R751, which carries an integron, is
RT   related to Tn7, Mu, and the retroelements.";
RL   J. Bacteriol. 176:3257-3268(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VA292; PLASMID=pDGO100;
RX   PubMed=8693029; DOI=10.1006/plas.1996.0008;
RA   Burnside J.M., Groot Obbink D.J.;
RT   "Plasmid pDGO100 contains a second integron with the trimethoprim
RT   resistance gene dfrA7 as the inserted cassette.";
RL   Plasmid 35:67-70(1996).
CC   -!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-
CC       dihydrofolate + NADPH.
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
CC       tetrahydrofolate from dihydrofolate: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- MISCELLANEOUS: The reaction catalyzed by this enzyme represents an
CC       essential step for de novo glycine and purine synthesis, DNA
CC       precursor synthesis, and for the conversion of dUMP to dTMP.
CC   -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC   -!- SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) 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; X58425; CAA41326.1; -; Genomic_DNA.
DR   EMBL; U31119; AAB18756.1; -; Genomic_DNA.
DR   PIR; A47087; A47087.
DR   HSSP; P00379; 1DRA.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0031427; P:response to methotrexate; IEA:UniProtKB-KW.
DR   GO; GO:0032196; P:transposition; IEA:UniProtKB-KW.
DR   InterPro; IPR012259; DHFR.
DR   InterPro; IPR001796; DHFR_reg.
DR   PANTHER; PTHR11549:SF1; DHFR; 1.
DR   Pfam; PF00186; DHFR_1; 1.
DR   PRINTS; PR00070; DHFR.
DR   PROSITE; PS00075; DHFR_1; 1.
DR   PROSITE; PS51330; DHFR_2; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Methotrexate resistance; NADP;
KW   One-carbon metabolism; Oxidoreductase; Plasmid; Transposable element;
KW   Trimethoprim resistance.
FT   CHAIN         1    157       Dihydrofolate reductase type 7.
FT                                /FTId=PRO_0000186424.
FT   DOMAIN        2    156       DHFR.
SQ   SEQUENCE   157 AA;  17594 MW;  A7791CC9C7E029DE CRC64;
     MKISLISATS ENGVIGNGPD IPWSAKGEQL LFKALTYNQW LLVGRKTFDS MGVLPNRKYA
     VVSRKGISSS NENVLVFPSI EIALQELSKI TDHLYVSGGG QIYNSLIEKA DIIHLSTVHV
     EVEGDINFPK IPENFNLVFE QFFLSNINYT YQIWKKG
//