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-MAY-2022, entry version 112.
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; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pLMO27; TRANSPOSON=Tn5086;
RX   PubMed=8383666; DOI=10.1128/jb.175.6.1796-1805.1993;
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   PubMed=8195081; DOI=10.1128/jb.176.11.3257-3268.1994;
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 related
RT   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   -!- FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential
CC       reaction for de novo glycine and purine synthesis, and for DNA
CC       precursor synthesis (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate +
CC         H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00660};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC       tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC       {ECO:0000305}.
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DR   EMBL; X58425; CAA41326.1; -; Genomic_DNA.
DR   EMBL; U31119; AAB18756.1; -; Genomic_DNA.
DR   PIR; A47087; A47087.
DR   RefSeq; WP_000703418.1; NZ_WSWW01000037.1.
DR   RefSeq; YP_006953993.1; NC_019091.1.
DR   AlphaFoldDB; P27422; -.
DR   SMR; P27422; -.
DR   KEGG; ag:CAA41326; -.
DR   OMA; EECFVIG; -.
DR   UniPathway; UPA00077; UER00158.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; 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:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00209; DHFR; 1.
DR   Gene3D; 3.40.430.10; -; 1.
DR   InterPro; IPR012259; DHFR.
DR   InterPro; IPR024072; DHFR-like_dom_sf.
DR   InterPro; IPR017925; DHFR_CS.
DR   InterPro; IPR001796; DHFR_dom.
DR   PANTHER; PTHR48069; PTHR48069; 1.
DR   Pfam; PF00186; DHFR_1; 1.
DR   SUPFAM; SSF53597; SSF53597; 1.
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
FT                   /note="Dihydrofolate reductase type 7"
FT                   /id="PRO_0000186424"
FT   DOMAIN          2..156
FT                   /note="DHFR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00660"
SQ   SEQUENCE   157 AA;  17594 MW;  A7791CC9C7E029DE CRC64;
     MKISLISATS ENGVIGNGPD IPWSAKGEQL LFKALTYNQW LLVGRKTFDS MGVLPNRKYA
     VVSRKGISSS NENVLVFPSI EIALQELSKI TDHLYVSGGG QIYNSLIEKA DIIHLSTVHV
     EVEGDINFPK IPENFNLVFE QFFLSNINYT YQIWKKG