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Database: UniProt
Entry: A0A199XR01_9FLAO
LinkDB: A0A199XR01_9FLAO
Original site: A0A199XR01_9FLAO 
ID   A0A199XR01_9FLAO        Unreviewed;       161 AA.
AC   A0A199XR01;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=dfrA {ECO:0000313|EMBL:OAZ04075.1};
GN   ORFNames=FLB_17670 {ECO:0000313|EMBL:OAZ04075.1};
OS   Flavobacterium succinicans.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=29536 {ECO:0000313|EMBL:OAZ04075.1, ECO:0000313|Proteomes:UP000093807};
RN   [1] {ECO:0000313|EMBL:OAZ04075.1, ECO:0000313|Proteomes:UP000093807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD5b {ECO:0000313|EMBL:OAZ04075.1,
RC   ECO:0000313|Proteomes:UP000093807};
RA   Poehlein A., Daniel R., Simeonova D.D.;
RT   "Draft genome sequence of Flavobacterium succinicans strain DD5b.";
RL   Submitted (JUN-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAZ04075.1}.
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DR   EMBL; JMTM01000046; OAZ04075.1; -; Genomic_DNA.
DR   RefSeq; WP_064715558.1; NZ_JMTM01000046.1.
DR   AlphaFoldDB; A0A199XR01; -.
DR   PATRIC; fig|29536.5.peg.1850; -.
DR   OrthoDB; 9804315at2; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000093807; 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; 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|ARBA:ARBA00022563,
KW   ECO:0000256|PIRNR:PIRNR000194};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000194,
KW   ECO:0000313|EMBL:OAZ04075.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093807}.
FT   DOMAIN          1..159
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
SQ   SEQUENCE   161 AA;  18635 MW;  C2490638B56A36E8 CRC64;
     MITLIAAVAD NRALGKNNDL LWHLPNDFKR FKAITSGHYI VMGRKTFESF PKPLPNRIHV
     IITRQKNYQP EGCIVVDSIE KAFEACSTTD NIYVIGGGEI YNLAMPYADL LDITRVHHEF
     EADTFFPEID PKKWQLSKSE KHLKDEKHLY DYSFETYSPI K
//
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