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Database: UniProt
Entry: B0BL08_ECOLX
LinkDB: B0BL08_ECOLX
Original site: B0BL08_ECOLX 
ID   B0BL08_ECOLX            Unreviewed;       157 AA.
AC   B0BL08;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=dihydrofolate reductase {ECO:0000256|ARBA:ARBA00012856};
DE            EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN   Name=dfrA17 {ECO:0000313|EMBL:CAP69686.1};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:CAP69686.1};
RN   [1] {ECO:0000313|EMBL:CAP69686.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=854 {ECO:0000313|EMBL:CAP69686.1};
RX   PubMed=18550679; DOI=10.1093/jac/dkn233;
RA   Kadlec K., Schwarz S.;
RT   "Analysis and distribution of class 1 and class 2 integrons and associated
RT   gene cassettes among Escherichia coli isolates from swine, horses, cats and
RT   dogs collected in the BfT-GermVet monitoring study.";
RL   J. Antimicrob. Chemother. 62:469-473(2008).
RN   [2] {ECO:0000313|EMBL:CAP69686.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=854 {ECO:0000313|EMBL:CAP69686.1};
RA   Schwarz S.P.;
RL   Submitted (JAN-2008) 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. {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; AM932673; CAP69686.1; -; Genomic_DNA.
DR   RefSeq; WP_063844367.1; NG_047711.1.
DR   AlphaFoldDB; B0BL08; -.
DR   SMR; B0BL08; -.
DR   BindingDB; B0BL08; -.
DR   DrugCentral; B0BL08; -.
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;  17532 MW;  2C80D7CB0CF90519 CRC64;
     MKISLISAVS ESGVIGSGPD IPWSVKGEQL LFKALTYNQW LLVGRKTFDS MGVLPNRKYA
     VVSKNGISSS NENVLVFPSI ENALKELSKV TDHVYVSGGG QIYNSLIEKA DIIHLSTVHV
     EVEGDIKFPI MPENFNLVFE QFFMSNINYT YQIWKKG
//
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