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Database: UniProt
Entry: V5RX86_9BACT
LinkDB: V5RX86_9BACT
Original site: V5RX86_9BACT 
ID   V5RX86_9BACT            Unreviewed;       163 AA.
AC   V5RX86;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
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   ORFNames=RAAC3_TM7C00001G0728 {ECO:0000313|EMBL:AHB42570.1};
OS   Candidatus Saccharibacteria bacterium RAAC3_TM7_1.
OC   Bacteria; Candidatus Saccharibacteria.
OX   NCBI_TaxID=1394711 {ECO:0000313|EMBL:AHB42570.1, ECO:0000313|Proteomes:UP000018523};
RN   [1] {ECO:0000313|EMBL:AHB42570.1, ECO:0000313|Proteomes:UP000018523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAAC3_TM7_1 {ECO:0000313|EMBL:AHB42570.1,
RC   ECO:0000313|Proteomes:UP000018523};
RA   Kantor R.S., Wrighton K.C., Handley K.M., Sharon I., Hug L.A.,
RA   Castelle C.J., Thomas B.C., Banfield J.F.;
RT   "Small genomes and sparse metabolisms of sediment-associated bacteria from
RT   four candidate phyla.";
RL   Submitted (NOV-2013) 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}.
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DR   EMBL; CP006915; AHB42570.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5RX86; -.
DR   STRING; 1394711.RAAC3_TM7C00001G0728; -.
DR   KEGG; sbe:RAAC3_TM7C01G0728; -.
DR   PATRIC; fig|1394711.4.peg.657; -.
DR   HOGENOM; CLU_043966_5_2_0; -.
DR   BioCyc; CSAC1394711:G132K-728-MONOMER; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000018523; 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; 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; PS51330; DHFR_2; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|PIRNR:PIRNR000194};
KW   One-carbon metabolism {ECO:0000256|PIRNR:PIRNR000194};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000194};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018523}.
FT   DOMAIN          1..159
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
SQ   SEQUENCE   163 AA;  18237 MW;  E15057243412CDEC CRC64;
     MKAIVVAMDK NNGIGAENDL LWLRDLPADL AHFKKLTIGG SVIMGSNTFK SIGRPLTDRE
     NIVVSRTPTG VEGVLTANSL ASAYELARYP VFVIGGGQIY AQAIDDVDRL YVTYVDAEFP
     QATVFFPQIS CDDWQEIERD HHEADEKNKY SYDFVKYERI QGV
//
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