ID R4PLX3_9BACT Unreviewed; 162 AA.
AC R4PLX3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=L336_0949 {ECO:0000313|EMBL:AGL62648.1};
OS Candidatus Saccharimonas aalborgensis.
OC Bacteria; Candidatus Saccharibacteria; Candidatus Saccharimonadia;
OC Candidatus Saccharimonadales; Candidatus Saccharimonadaceae; Saccharimonas.
OX NCBI_TaxID=1332188 {ECO:0000313|EMBL:AGL62648.1, ECO:0000313|Proteomes:UP000013893};
RN [1] {ECO:0000313|EMBL:AGL62648.1, ECO:0000313|Proteomes:UP000013893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM71 {ECO:0000313|EMBL:AGL62648.1};
RX PubMed=23707974; DOI=10.1038/nbt.2579;
RA Albertsen M., Hugenholtz P., Skarshewski A., Nielsen K.L., Tyson G.W.,
RA Nielsen P.H.;
RT "Genome sequences of rare, uncultured bacteria obtained by differential
RT coverage binning of multiple metagenomes.";
RL Nat. Biotechnol. 31:533-538(2013).
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; CP005957; AGL62648.1; -; Genomic_DNA.
DR AlphaFoldDB; R4PLX3; -.
DR STRING; 1332188.L336_0949; -.
DR KEGG; saal:L336_0949; -.
DR PATRIC; fig|1332188.3.peg.946; -.
DR HOGENOM; CLU_043966_5_1_0; -.
DR OrthoDB; 9804315at2; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000013893; 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:AGL62648.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013893}.
FT DOMAIN 1..161
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
SQ SEQUENCE 162 AA; 18363 MW; 1BCC677F9BDFF00D CRC64;
MKELIVAYDQ KRGIGADGDL LWQRDLPGDL AHFKQMTMGS SLVMGRTTYE SIGRPLPGRE
MIVVTHRPLD DEGIIAVHSL AEAYTRASRE RTVVIGGGQI YEQALREGSI ERIHATEVTA
TFPGATVFFP VLDAMWHETT REHHGSNEHD RYSYDFVTYE RR
//
