ID J0YSY1_9STRE Unreviewed; 168 AA.
AC J0YSY1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:EJG87339.1};
GN ORFNames=SPAR10_0911 {ECO:0000313|EMBL:EJG87339.1};
OS Streptococcus infantis SPAR10.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1159208 {ECO:0000313|EMBL:EJG87339.1, ECO:0000313|Proteomes:UP000010312};
RN [1] {ECO:0000313|EMBL:EJG87339.1, ECO:0000313|Proteomes:UP000010312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPAR10 {ECO:0000313|EMBL:EJG87339.1,
RC ECO:0000313|Proteomes:UP000010312};
RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., Pallavajjal A.,
RA Abolude O., Daugherty S.C., Parankush S.P., Sadzewicz L., Tallon L.J.,
RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.;
RT "Genomic Sequence of Streptococcus mitis SPAR10.";
RL Submitted (MAY-2012) 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|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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJG87339.1}.
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DR EMBL; ALCH01000004; EJG87339.1; -; Genomic_DNA.
DR RefSeq; WP_004252176.1; NZ_ALCH01000004.1.
DR AlphaFoldDB; J0YSY1; -.
DR PATRIC; fig|1159208.3.peg.849; -.
DR OrthoDB; 9804315at2; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000010312; Unassembled WGS sequence.
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}.
FT DOMAIN 4..165
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
SQ SEQUENCE 168 AA; 19730 MW; 65A70F127B0927A6 CRC64;
MTKKIVAIWA QDEKGVIGKE DRLPWHLPAE LKHFKETTLN HAILMGRVTF DGMGRRLLPG
RETLILTRNP EESIEGALVF QNVEDVLEWY HHQDKNLYIL GGKQIFQLFE PYLDEIIVTQ
IHAQVEGDTY FPEDFDLTVF ETLASKSYTR DEKNAYDFTI EYRKRKEV
//
