DYR_STAHA
ID DYR_STAHA Reviewed; 166 AA.
AC Q54277;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Dihydrofolate reductase;
DE EC=1.5.1.3;
GN Name=dfrD;
OS Staphylococcus haemolyticus.
OG Plasmid pABU17.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1283;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MASS SPECTROMETRY.
RC STRAIN=MUR313;
RX PubMed=8540692; DOI=10.1128/aac.39.9.1920;
RA Dale G.E., Langen H., Page M.G., Then R.L., Stueber D.;
RT "Cloning and characterization of a novel, plasmid-encoded trimethoprim-
RT resistant dihydrofolate reductase from Staphylococcus haemolyticus
RT MUR313.";
RL Antimicrob. Agents Chemother. 39:1920-1924(1995).
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 -!- MASS SPECTROMETRY: Mass=19821.2; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8540692};
CC -!- MISCELLANEOUS: Confers trimethoprim resistance.
CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC {ECO:0000305}.
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DR EMBL; Z50141; CAA90486.1; -; Genomic_DNA.
DR AlphaFoldDB; Q54277; -.
DR SMR; Q54277; -.
DR KEGG; ag:CAA90486; -.
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 1: Evidence at protein level;
KW Antibiotic resistance; Methotrexate resistance; NADP;
KW One-carbon metabolism; Oxidoreductase; Plasmid; Trimethoprim resistance.
FT CHAIN 1..166
FT /note="Dihydrofolate reductase"
FT /id="PRO_0000186416"
FT DOMAIN 6..164
FT /note="DHFR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00660"
FT BINDING 10..12
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 11..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 19..24
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 48..51
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 67..70
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 100..105
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 166 AA; 19825 MW; 9AAD03F3ECCA9990 CRC64;
MWSFLKISLI VAMDKKRVIG KDNDIPWRIS SDWEYVKNTT KGHAIILGRK NLQSIGRALP
DRRNIILTRD KNFNFKDCEI AHSIEAAFKL CENEEEVFIF GGEQIYVMFL PYVEKMYVTK
IHHEFEGDTF FPVVNFDDWK EVSVEKGIKD EKNPYDYYFH IYERIR