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Database: UniProt
Entry: A0A1Q2D8S5_9ENTE
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ID   A0A1Q2D8S5_9ENTE        Unreviewed;       165 AA.
AC   A0A1Q2D8S5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=BW732_11220 {ECO:0000313|EMBL:AQP54720.1};
OS   Vagococcus penaei.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX   NCBI_TaxID=633807 {ECO:0000313|EMBL:AQP54720.1, ECO:0000313|Proteomes:UP000188246};
RN   [1] {ECO:0000313|EMBL:AQP54720.1, ECO:0000313|Proteomes:UP000188246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD276 {ECO:0000313|EMBL:AQP54720.1,
RC   ECO:0000313|Proteomes:UP000188246};
RX   PubMed=19897618; DOI=10.1099/ijs.0.012872-0;
RA   Jaffres E., Prevost H., Rossero A., Joffraud J.J., Dousset X.;
RT   "Vagococcus penaei sp. nov., isolated from spoilage microbiota of cooked
RT   shrimp (Penaeus vannamei).";
RL   Int. J. Syst. Evol. Microbiol. 60:2159-2164(2010).
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; CP019609; AQP54720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2D8S5; -.
DR   STRING; 633807.BW732_11220; -.
DR   KEGG; vpi:BW732_11220; -.
DR   OrthoDB; 9804315at2; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000188246; 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|ARBA:ARBA00022563,
KW   ECO:0000256|PIRNR:PIRNR000194};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000194};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188246}.
FT   DOMAIN          1..161
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
SQ   SEQUENCE   165 AA;  18987 MW;  3A23430B3946BB56 CRC64;
     MIAAIWAQDM NGLIGNNEVL PWYLPDDLQF FKQMTENNAI VMGRKTFEGM GKRLLPNRET
     IVLTSDKNYD GNGAIVMNSV EEVLEFANEF EGITFITGGG EIYKTFLPHL DVLYRTLIKA
     EFEGDTYFPY LDWDEWHIVS TSAGTVDDKN LYAHDFETYQ RHVNN
//
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