ID   Q2Q3Z8_SALSE            Unreviewed;       157 AA.
AC   Q2Q3Z8;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=dihydrofolate reductase {ECO:0000256|ARBA:ARBA00012856};
DE            EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN   Name=dfrA14 {ECO:0000313|EMBL:ABB77558.1};
OS   Salmonella senftenberg.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=28150 {ECO:0000313|EMBL:ABB77558.1};
RN   [1] {ECO:0000313|EMBL:ABB77558.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=N246 {ECO:0000313|EMBL:ABB77558.1};
RA   Vo A., van Duijkeren E., Fluit A., Gaastra W.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABB77558.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=N246 {ECO:0000313|EMBL:ABB77558.1};
RX   PubMed=16911867; DOI=10.1016/j.ijantimicag.2006.05.027;
RA   Vo A.T., van Duijkeren E., Fluit A.C., Wannet W.J., Verbruggen A.J.,
RA   Maas H.M., Gaastra W.;
RT   "Antibiotic resistance, integrons and Salmonella genomic island 1 among
RT   non-typhoidal Salmonella serovars in The Netherlands.";
RL   Int. J. Antimicrob. Agents 28:172-179(2006).
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. {ECO:0000256|ARBA:ARBA00025067}.
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC       tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004903}.
CC   -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC       {ECO:0000256|ARBA:ARBA00009539, ECO:0000256|RuleBase:RU004474}.
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DR   EMBL; DQ228133; ABB77558.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2Q3Z8; -.
DR   SMR; Q2Q3Z8; -.
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: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   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   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          2..156
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
SQ   SEQUENCE   157 AA;  17542 MW;  6803C643BBBDCFBF CRC64;
     MKVSLMAAKA KNGVIGCGPD IPWSAKGEQL LFKALTYNQW LLVGRKTFES MGALPNRKYA
     VVTRSGWTSN DDNVVVFQSI EEAMDRLAEF TGHVIVSGGG EIYRETLPMA STLHLSTIDI
     EPEGDVFFPS IPNTFEVVFE QHFTSNINYC YQIWKKG
//