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Database: UniProt
Entry: A0A1V4CHG8_9BURK
LinkDB: A0A1V4CHG8_9BURK
Original site: A0A1V4CHG8_9BURK 
ID   A0A1V4CHG8_9BURK        Unreviewed;       170 AA.
AC   A0A1V4CHG8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=BC358_04120 {ECO:0000313|EMBL:OPF64059.1};
OS   Hydrogenophaga sp. H7.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1882399 {ECO:0000313|EMBL:OPF64059.1, ECO:0000313|Proteomes:UP000189907};
RN   [1] {ECO:0000313|Proteomes:UP000189907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H7 {ECO:0000313|Proteomes:UP000189907};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-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|ARBA:ARBA00025067,
CC       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}.
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:OPF64059.1}.
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DR   EMBL; MCIC01000012; OPF64059.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4CHG8; -.
DR   STRING; 1882399.BC358_04120; -.
DR   OrthoDB; 9804315at2; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000189907; 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|ARBA:ARBA00022563,
KW   ECO:0000256|PIRNR:PIRNR000194};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000194};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189907}.
FT   DOMAIN          9..167
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
SQ   SEQUENCE   170 AA;  18252 MW;  DADEEF2EAB93AFF8 CRC64;
     MPETTAPASL HLIYARAANG VIGKDNRLPW HLPEDMAHFK RSTLGCPVIM GRKTWDSLPP
     KFRPLPGRLN IVVTRDTAFV AEGASVAHSL EAARGLCPAG STAWVIGGAQ IYAQALPLAS
     EVVVTEIAQD FEGDAFAPVL GGDWREVARE EQVSASGLPF AFVTYRRADA
//
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