ID   DYR8_SHISO              Reviewed;         169 AA.
AC   P0ABQ8; Q57452;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Dihydrofolate reductase type 8;
DE            EC=1.5.1.3;
DE   AltName: Full=Dihydrofolate reductase type VIII;
DE   AltName: Full=DHFR type IIIC;
GN   Name=dhfrVIII; Synonyms=dhfrIIIc;
OS   Shigella sonnei.
OG   Plasmid pBH700.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95209332; PubMed=7695291;
RA   Barg N.L., Register S., Thomson C., Amyes S.;
RT   "Sequence identity with type VIII and association with IS176 of type
RT   IIIc dihydrofolate reductase from Shigella sonnei.";
RL   Antimicrob. Agents Chemother. 39:112-116(1995).
CC   -!- FUNCTION: Confers high-level trimethoprim resistance.
CC   -!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-
CC       dihydrofolate + NADPH.
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
CC       tetrahydrofolate from dihydrofolate: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- MISCELLANEOUS: The reaction catalyzed by this enzyme represents an
CC       essential step for de novo glycine and purine synthesis, DNA
CC       precursor synthesis, and for the conversion of dUMP to dTMP.
CC   -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC   -!- SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) domain.
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DR   EMBL; U09273; AAA79232.1; -; Genomic_DNA.
DR   HSSP; P00381; 3DFR.
DR   BRENDA; 1.5.1.3; 74546.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:EC.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; 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   InterPro; IPR012259; DHFR.
DR   InterPro; IPR001796; DHFR_reg.
DR   InterPro; IPR017925; Dihydrofolate_reductase_CS.
DR   PANTHER; PTHR11549:SF1; DHFR; 1.
DR   Pfam; PF00186; DHFR_1; 1.
DR   PRINTS; PR00070; DHFR.
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; Plasmid;
KW   Trimethoprim resistance.
FT   CHAIN         1    169       Dihydrofolate reductase type 8.
FT                                /FTId=PRO_0000186426.
FT   DOMAIN        3    169       DHFR.
SQ   SEQUENCE   169 AA;  19021 MW;  76E1ABA0C0DE30CC CRC64;
     MIELHAILAA TANGCIGKDN ALPWPPLKGD LARFKKLTMG KVVIMGRKTY ESLPVKLEGR
     TCIVMTRQAL ELPGVRDANG AIFVNNVSDA MRFAQEESVG DVAYVIGGAE IFKRLALMIT
     QIELTFVKRL YEGDTYVDLA EMVKDYEQNG MEEHDLHTYF TYRKKELTE
//