DYR13_ECOLX
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 25-MAY-2022, entry version 86.
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; Proteobacteria; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; -; 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 PIRSF; PIRSF000194; DHFR; 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..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