ID A0A061H2K2_9BASI Unreviewed; 288 AA.
AC A0A061H2K2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 22-FEB-2023, entry version 35.
DE RecName: Full=Dihydrofolate reductase {ECO:0000256|ARBA:ARBA00018886};
DE EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN ORFNames=PFL1_05602 {ECO:0000313|EMBL:EPQ26967.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ26967.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ26967.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ26967.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004903}.
CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC {ECO:0000256|RuleBase:RU004474}.
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DR EMBL; KE361642; EPQ26967.1; -; Genomic_DNA.
DR RefSeq; XP_007881328.1; XM_007883137.1.
DR AlphaFoldDB; A0A061H2K2; -.
DR GeneID; 19319691; -.
DR KEGG; pfp:PFL1_05602; -.
DR eggNOG; KOG1324; Eukaryota.
DR HOGENOM; CLU_043966_2_1_1; -.
DR OrthoDB; 1118873at2759; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000053664; 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 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};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053664}.
FT DOMAIN 15..286
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
FT REGION 208..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 288 AA; 31674 MW; F68641B8E932A377 CRC64;
MTSPGGSSSL SAPLRMTVIA AATMTNGLGV AGGLPWKLKG EMAYFRKATS TTSTAAVREP
GGEGQEQRNA VIMGRKTWES IPTKFRPLKD RVNIVVSRSQ TEADLGISNK DDAWLFRSIE
EAVRYLRTRT TADGAASSEA GPQVDRVFVI GGAQLYADSM ADGTPERQRL FVVDRLLITR
ILRPLYPECD AFLPEFRDAD QVQQDASIQA QAQAQAQAQA AADVDDKPQE GSLRPLDQRR
WERSSAEELQ RYLSFDPSHD GGKLGRPGDA VENEADVFYQ FQMWTRAS
//
