ID   DYR13_ECOLX             Reviewed;         165 AA.
AC   Q59408;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-MAY-2023, entry version 89.
DE   RecName: Full=Dihydrofolate reductase type A13;
DE            EC=1.5.1.3;
DE   AltName: Full=Dihydrofolate reductase type XIII;
DE            Short=DHFRXIII;
GN   Name=dfrA13; Synonyms=dfr13;
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RA33.2;
RX   PubMed=10639362; DOI=10.1128/aac.44.2.355-361.2000;
RA   Adrian P.V., Thomson C.J., Klugman K.P., Amyes S.G.;
RT   "New gene cassettes for trimethoprim resistance, dfr13, and Streptomycin-
RT   spectinomycin resistance, aadA4, inserted on a class 1 integron.";
RL   Antimicrob. Agents Chemother. 44:355-361(2000).
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; Z50802; CAA90683.1; -; Genomic_DNA.
DR   PIR; S60665; S60665.
DR   RefSeq; WP_063844334.1; NG_047693.1.
DR   AlphaFoldDB; Q59408; -.
DR   SMR; Q59408; -.
DR   KEGG; ag:CAA90683; -.
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; Dihydrofolate Reductase, subunit A; 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; DIHYDROFOLATE REDUCTASE; 1.
DR   PANTHER; PTHR48069:SF3; DIHYDROFOLATE REDUCTASE; 1.
DR   Pfam; PF00186; DHFR_1; 1.
DR   PIRSF; PIRSF000194; DHFR; 1.
DR   PRINTS; PR00070; DHFR.
DR   SUPFAM; SSF53597; Dihydrofolate reductase-like; 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..165
FT                   /note="Dihydrofolate reductase type A13"
FT                   /id="PRO_0000186429"
FT   DOMAIN          7..162
FT                   /note="DHFR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00660"
SQ   SEQUENCE   165 AA;  17925 MW;  656E9E214DDFDA9D CRC64;
     MNPESVRIYL VAAMGANRVI GNGPDIPWKI PGEQKIFRRL TESKVVVMGR KTFESIGKPL
     PNRHTVVLSR QAGYSAPGCA VVSTLSHVSP STAEHGKELY VARGAEVYAL ALPHANGVFL
     SEVHQTFEGD AFFPVLNAAE FEVVSSETIQ GTITYTHSVY ARRNG
//