ID Q8DZ08_STRA5 Unreviewed; 164 AA.
AC Q8DZ08;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Dihydrofolate reductase {ECO:0000256|ARBA:ARBA00012856, ECO:0000256|PIRNR:PIRNR000194};
DE EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856, ECO:0000256|PIRNR:PIRNR000194};
GN Name=folA {ECO:0000313|EMBL:AAN00185.1};
GN OrderedLocusNames=SAG1314 {ECO:0000313|EMBL:AAN00185.1};
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435 {ECO:0000313|EMBL:AAN00185.1, ECO:0000313|Proteomes:UP000000821};
RN [1] {ECO:0000313|EMBL:AAN00185.1, ECO:0000313|Proteomes:UP000000821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R {ECO:0000313|Proteomes:UP000000821};
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin S., Kolonay J.F., Umayam L.A., Madupu R., Lewis M.R.,
RA Radune D., Fedorova N.B., Scanlan D., Khouri H., Mulligan S., Carty H.A.,
RA Cline R.T., Gill J., Scarselli M., Mora M., Iacobini E.T., Brettoni C.,
RA Galli G., Mariani M., Vegni F., Maione D., Rinaudo D., Rappuoli R.,
RA Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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|PIRNR:PIRNR000194}.
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;
CC Evidence={ECO:0000256|PIRNR:PIRNR000194};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004903, ECO:0000256|PIRNR:PIRNR000194}.
CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC {ECO:0000256|ARBA:ARBA00009539, ECO:0000256|PIRNR:PIRNR000194,
CC ECO:0000256|RuleBase:RU004474}.
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DR EMBL; AE009948; AAN00185.1; -; Genomic_DNA.
DR RefSeq; NP_688312.1; NC_004116.1.
DR RefSeq; WP_000166043.1; NC_004116.1.
DR AlphaFoldDB; Q8DZ08; -.
DR STRING; 208435.SAG1314; -.
DR GeneID; 66886179; -.
DR KEGG; sag:SAG1314; -.
DR PATRIC; fig|208435.3.peg.1322; -.
DR HOGENOM; CLU_043966_5_2_9; -.
DR OrthoDB; 9804315at2; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000000821; Chromosome.
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 PIRSF; PIRSF000194; DHFR; 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, ECO:0000256|PIRNR:PIRNR000194};
KW One-carbon metabolism {ECO:0000256|PIRNR:PIRNR000194};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000194};
KW Reference proteome {ECO:0000313|Proteomes:UP000000821}.
FT DOMAIN 4..164
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
SQ SEQUENCE 164 AA; 18943 MW; 06BD1D9B85DA724A CRC64;
MTKQIIAIWA EDEDHLIGVN GGLPWRLPKE LHHFKETTMG QALLMGRKTF DGMNRRVLPG
RETIILTKDE QFQADGVTVL NSVEQVIKWF QEHNKTLFIV GGASIYKAFL PYCEAIIKTK
VHGKFKGDTY FPDVNLSEFK VISRDYFEKD EQNAHAFTVT YFEK
//
