DYR_BPT4
ID DYR_BPT4 Reviewed; 193 AA.
AC P04382;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Dihydrofolate reductase;
DE EC=1.5.1.3;
GN Name=frd;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6327673; DOI=10.1016/s0021-9258(20)82135-8;
RA Purohit S., Mathews C.K.;
RT "Nucleotide sequence reveals overlap between T4 phage genes encoding
RT dihydrofolate reductase and thymidylate synthase.";
RL J. Biol. Chem. 259:6261-6266(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 123-193.
RC STRAIN=ALC4;
RX PubMed=3698096; DOI=10.1016/0092-8674(86)90379-x;
RA Chu F.K., Maley G.F., West D.K., Belfort M., Maley F.;
RT "Characterization of the intron in the phage T4 thymidylate synthase gene
RT and evidence for its self-excision from the primary transcript.";
RL Cell 45:157-166(1986).
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 -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC {ECO:0000305}.
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DR EMBL; K01804; AAA32491.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42577.1; -; Genomic_DNA.
DR EMBL; M12742; AAC12815.1; -; Genomic_DNA.
DR PIR; A00396; RDBPT4.
DR RefSeq; NP_049850.1; NC_000866.4.
DR PDB; 1JUV; X-ray; 1.70 A; A=1-193.
DR PDBsum; 1JUV; -.
DR SMR; P04382; -.
DR GeneID; 1258671; -.
DR KEGG; vg:1258671; -.
DR UniPathway; UPA00077; UER00158.
DR EvolutionaryTrace; P04382; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0004146; F:dihydrofolate reductase activity; IDA:CACAO.
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 Gene3D; 3.40.430.10; -; 1.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR017925; DHFR_CS.
DR InterPro; IPR001796; DHFR_dom.
DR Pfam; PF00186; DHFR_1; 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 3D-structure; Antibiotic resistance; Methotrexate resistance; NADP;
KW One-carbon metabolism; Oxidoreductase; Reference proteome;
KW Trimethoprim resistance.
FT CHAIN 1..193
FT /note="Dihydrofolate reductase"
FT /id="PRO_0000186434"
FT DOMAIN 1..193
FT /note="DHFR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00660"
FT BINDING 7
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 22..27
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 52..55
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 73..77
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT STRAND 2..12
FT /evidence="ECO:0007829|PDB:1JUV"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:1JUV"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:1JUV"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1JUV"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:1JUV"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1JUV"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1JUV"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:1JUV"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1JUV"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1JUV"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1JUV"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:1JUV"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1JUV"
FT STRAND 141..152
FT /evidence="ECO:0007829|PDB:1JUV"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:1JUV"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:1JUV"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:1JUV"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:1JUV"
SQ SEQUENCE 193 AA; 21713 MW; 64E033916E628178 CRC64;
MIKLVFRYSP TKTVDGFNEL AFGLGDGLPW GRVKKDLQNF KARTEGTIMI MGAKTFQSLP
TLLPGRSHIV VCDLARDYPV TKDGDLAHFY ITWEQYITYI SGGEIQVSSP NAPFETMLDQ
NSKVSVIGGP ALLYAALPYA DEVVVSRIVK RHRVNSTVQL DASFLDDISK REMVETHWYK
IDEVTTLTES VYK
