ID A0A377KQD5_9ENTE Unreviewed; 168 AA.
AC A0A377KQD5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:STP30574.1};
GN ORFNames=EA71_01738 {ECO:0000313|EMBL:RCA10984.1}, GUJ97_13055
GN {ECO:0000313|EMBL:NAA81469.1}, NCTC8129_02824
GN {ECO:0000313|EMBL:STP30574.1}, NCTC8130_01862
GN {ECO:0000313|EMBL:STP39285.1};
OS Enterococcus durans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=53345 {ECO:0000313|EMBL:STP30574.1, ECO:0000313|Proteomes:UP000254070};
RN [1] {ECO:0000313|EMBL:RCA10984.1, ECO:0000313|Proteomes:UP000252797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4EA1 {ECO:0000313|EMBL:RCA10984.1,
RC ECO:0000313|Proteomes:UP000252797};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Van Tyne D., Lebreton F., Saavedra J.T., Gilmore M.S.,
RA Manson Mcguire A., Clock S., Crupain M., Rangan U., Young S.,
RA Abouelleil A., Cao P., Chapman S.B., Griggs A., Priest M., Shea T.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus durans 4EA1.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000254070, ECO:0000313|Proteomes:UP000254113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC8129 {ECO:0000313|EMBL:STP30574.1,
RC ECO:0000313|Proteomes:UP000254070}, and NCTC8130
RC {ECO:0000313|EMBL:STP39285.1, ECO:0000313|Proteomes:UP000254113};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:NAA81469.1, ECO:0000313|Proteomes:UP000444134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A60 {ECO:0000313|EMBL:NAA81469.1,
RC ECO:0000313|Proteomes:UP000444134};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
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; WXTH01000061; NAA81469.1; -; Genomic_DNA.
DR EMBL; LEPB01000004; RCA10984.1; -; Genomic_DNA.
DR EMBL; UGIF01000002; STP30574.1; -; Genomic_DNA.
DR EMBL; UGIP01000002; STP39285.1; -; Genomic_DNA.
DR RefSeq; WP_005879475.1; NZ_WXTW01000062.1.
DR STRING; 53345.LIU_09970; -.
DR KEGG; edu:LIU_09970; -.
DR OrthoDB; 9804315at2; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000252797; Unassembled WGS sequence.
DR Proteomes; UP000254070; Unassembled WGS sequence.
DR Proteomes; UP000254113; Unassembled WGS sequence.
DR Proteomes; UP000444134; 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 1..162
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
SQ SEQUENCE 168 AA; 19641 MW; FEC802E5AAB153F0 CRC64;
MFISMWAQDR NGLIGKDGLL PWKLPNDMRF FREHTMNRIL VMGRKTYEGM GKLSLPYRKI
IVLTSQTDFK VEENAEVMHS IEELLAYAKN CSEDIYVSGG SRIFQELLPE TGIIWRTLID
ATFEGDTFIG EIDFSDFDLV EEHVGIVDEE NQYPHRFQKW QRRVAEAE
//
