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Database: UniProt
Entry: H5WHQ8_9BURK
LinkDB: H5WHQ8_9BURK
Original site: H5WHQ8_9BURK 
ID   H5WHQ8_9BURK            Unreviewed;       171 AA.
AC   H5WHQ8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
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=BurJ1DRAFT_1452 {ECO:0000313|EMBL:EHR70320.1};
OS   Burkholderiales bacterium JOSHI_001.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=864051 {ECO:0000313|EMBL:EHR70320.1, ECO:0000313|Proteomes:UP000004674};
RN   [1] {ECO:0000313|EMBL:EHR70320.1, ECO:0000313|Proteomes:UP000004674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JOSHI_001 {ECO:0000313|EMBL:EHR70320.1,
RC   ECO:0000313|Proteomes:UP000004674};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Zeytun A., Lu M., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Smith J., Lewis G.,
RA   Woyke T.;
RT   "Noncontiguous Finished sequence of Burkholderiales bacterium JOSHI_001.";
RL   Submitted (NOV-2011) 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}.
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DR   EMBL; CM001438; EHR70320.1; -; Genomic_DNA.
DR   AlphaFoldDB; H5WHQ8; -.
DR   STRING; 864051.BurJ1DRAFT_1452; -.
DR   eggNOG; COG0262; Bacteria.
DR   HOGENOM; CLU_043966_5_0_4; -.
DR   OrthoDB; 9804315at2; -.
DR   BioCyc; BBAC864051:G1H30-1443-MONOMER; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000004674; 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|PIRNR:PIRNR000194};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000194};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004674}.
FT   DOMAIN          9..170
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
SQ   SEQUENCE   171 AA;  18860 MW;  F8AD0BCCEBBF3CC6 CRC64;
     MTEAAPPPHL SLLMAVARNG VIGHQGQLPW RLPEDMAFFR RTTTGHAVVM GRRTWDSLPA
     RFRPLPQRRN IVVTRNTAWS APGAEAVPSL QAALQLAAGA PRLFVIGGAE LYAAALPLAD
     ELLLTEIDAD IEGDTHLPDF DRQAFVEVQR ERHQAAAPND FGFAFVTYRK R
//
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