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Database: UniProt
Entry: G8UQ25_TANFA
LinkDB: G8UQ25_TANFA
Original site: G8UQ25_TANFA 
ID   G8UQ25_TANFA            Unreviewed;       163 AA.
AC   G8UQ25;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
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:AEW19886.1};
GN   OrderedLocusNames=BFO_0996 {ECO:0000313|EMBL:AEW19886.1};
OS   Tannerella forsythia (strain ATCC 43037 / JCM 10827 / CCUG 21028 A / KCTC
OS   5666 / FDC 338) (Bacteroides forsythus).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Tannerella.
OX   NCBI_TaxID=203275 {ECO:0000313|EMBL:AEW19886.1, ECO:0000313|Proteomes:UP000005436};
RN   [1] {ECO:0000313|Proteomes:UP000005436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43037 / JCM 10827 / CCUG 33226 / KCTC 5666 / FDC 338
RC   {ECO:0000313|Proteomes:UP000005436};
RA   Dewhirst F., Tanner A., Izard J., Brinkac L., Durkin A.S., Hostetler J.,
RA   Shetty J., Torralba M., Gill S., Nelson K.;
RT   "Complete sequence of Tannerella forsythia ATCC 43037.";
RL   Submitted (DEC-2011) 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; CP003191; AEW19886.1; -; Genomic_DNA.
DR   RefSeq; WP_014224415.1; NC_016610.1.
DR   AlphaFoldDB; G8UQ25; -.
DR   STRING; 203275.BFO_0996; -.
DR   GeneID; 34758268; -.
DR   KEGG; tfo:BFO_0996; -.
DR   PATRIC; fig|203275.8.peg.894; -.
DR   eggNOG; COG0262; Bacteria.
DR   HOGENOM; CLU_043966_5_2_10; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000005436; 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   ECO:0000313|EMBL:AEW19886.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005436}.
FT   DOMAIN          1..161
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
SQ   SEQUENCE   163 AA;  18714 MW;  F3CCBE9A7C1FD468 CRC64;
     MISIIVATDQ RGAIGKDNSL LWRLPNDMKH FRELTVGHTV VMGRRTFESL PHGALPNRRN
     MVLTTEWGAH FNNCLVYNTL WGALMDTEEE EEVFVIGGGN VYKQALEVAD KLYLTLVHHT
     FPEADTFFPP VDPKVWEEVS RTDVPTDEKN PYPHSFLTYV RKK
//
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