ID   DYR15_ECOLX             Reviewed;         157 AA.
AC   P78218;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Dihydrofolate reductase type 15;
DE            EC=1.5.1.3;
DE   AltName: Full=Dihydrofolate reductase type XV;
GN   Name=dhfrXV; Synonyms=dfrXV;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UI14;
RA   Adrian P.V., du Plessis M., Klugman K.P., Amyes S.G.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
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; Z83311; CAB05887.1; -; Genomic_DNA.
DR   RefSeq; WP_001355915.1; NZ_SRWX01000083.1.
DR   AlphaFoldDB; P78218; -.
DR   SMR; P78218; -.
DR   KEGG; ag:CAB05887; -.
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; Trimethoprim resistance.
FT   CHAIN           1..157
FT                   /note="Dihydrofolate reductase type 15"
FT                   /id="PRO_0000186430"
FT   DOMAIN          2..156
FT                   /note="DHFR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00660"
SQ   SEQUENCE   157 AA;  17503 MW;  FF08B9F36650A83F CRC64;
     MKLSLMAAIS KNGVIGNGPD IPWSAKGEQL LFKAITYNQW LLVGRKTFES MGALPNRKYA
     VVTRSSFTSS DENVLVFPSI DEALNHLKTI TDHVIVSGGG EIYKSLIDKV DTLHISTIDI
     EPEGDVYFPE IPSSFRPVFS QDFVSNINYS YQIWQKG