DYR22_ECOLX
ID DYR22_ECOLX Reviewed; 78 AA.
AC P00384;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Dihydrofolate reductase type 2;
DE EC=1.5.1.3;
DE AltName: Full=Dihydrofolate reductase type II;
OS Escherichia coli.
OG Plasmid IncW R388.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6261228; DOI=10.1093/nar/9.3.697;
RA Zolg J.W., Haenggi U.J.;
RT "Characterization of a R plasmid-associated, trimethoprim-resistant
RT dihydrofolate reductase and determination of the nucleotide sequence of the
RT reductase gene.";
RL Nucleic Acids Res. 9:697-710(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7022127; DOI=10.1007/bf00428733;
RA Swift G., McCarthy B.J., Heffron F.;
RT "DNA sequence of a plasmid-encoded dihydrofolate reductase.";
RL Mol. Gen. Genet. 181:441-447(1981).
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;
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- DOMAIN: The active site is situated at the inner surface of a pore
CC formed by the four subunits. {ECO:0000250}.
CC -!- MISCELLANEOUS: Type II plasmid-specified enzyme is practically
CC insensitive to trimethoprim and methotrexate.
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DR EMBL; V00252; CAA23503.1; -; Genomic_DNA.
DR EMBL; J01773; AAA72145.1; -; Genomic_DNA.
DR PIR; A00398; RDECD8.
DR RefSeq; WP_015060228.1; NG_051851.1.
DR RefSeq; YP_009182144.1; NC_028464.1.
DR AlphaFoldDB; P00384; -.
DR SMR; P00384; -.
DR KEGG; ag:AAA72145; -.
DR UniPathway; UPA00077; UER00158.
DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC.
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:0009410; P:response to xenobiotic stimulus; IEA:InterPro.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.30.30.60; -; 1.
DR InterPro; IPR009159; Dhfr_type_II.
DR InterPro; IPR008990; Elect_transpt_acc-like_dom_sf.
DR InterPro; IPR023408; MscS_dom_sf.
DR Pfam; PF06442; DHFR_2; 1.
DR PIRSF; PIRSF000199; Dhfr_type_II; 1.
DR SUPFAM; SSF50090; SSF50090; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Methotrexate resistance; NADP;
KW One-carbon metabolism; Oxidoreductase; Plasmid; Trimethoprim resistance.
FT CHAIN 1..78
FT /note="Dihydrofolate reductase type 2"
FT /id="PRO_0000186436"
FT BINDING 32
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 66..69
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 78 AA; 8195 MW; EE9B686CBE5BCB93 CRC64;
MGQSSDEANA PVAGQFALPL SATFGLGDRV RKKSGAAWQG QVVGWYCTKL TPEGYAVESE
SHPGSVQIYP VAALERVA
