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Database: UniProt
Entry: A0A100IPH5_ASPNG
LinkDB: A0A100IPH5_ASPNG
Original site: A0A100IPH5_ASPNG 
ID   A0A100IPH5_ASPNG        Unreviewed;       265 AA.
AC   A0A100IPH5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   03-MAY-2023, entry version 26.
DE   RecName: Full=Dihydrofolate reductase {ECO:0000256|ARBA:ARBA00018886};
DE            EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN   ORFNames=ABL_07644 {ECO:0000313|EMBL:GAQ44983.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ44983.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
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}.
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:GAQ44983.1}.
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DR   EMBL; BCMY01000014; GAQ44983.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100IPH5; -.
DR   VEuPathDB; FungiDB:An12g04590; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1208541; -.
DR   VEuPathDB; FungiDB:ATCC64974_37640; -.
DR   VEuPathDB; FungiDB:M747DRAFT_298286; -.
DR   OMA; QYEFQMW; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000068243; 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}.
FT   DOMAIN          7..264
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
FT   REGION          15..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   265 AA;  28495 MW;  D287591324D5A58D CRC64;
     MPPTPRPLTL IVATTPIPTP ASTTESSSST TTTPIRLGIG HSGTLPWPRI KTDMSFFARV
     TSRPPVPGTT NAIIMGRKTY DSVPAHLRPL AKRISTIITR DVEGLKPRVA REVEDRKAKL
     AASAAAASST SGGNGNAVQP ATDAIVCGGL NEALQELETR YGEGKLGKVF VIGGAEIYGA
     VLAAKGGPVR IVMTNVEKKG YAEGDRGDVF ECDTFFPVDE ELFGEKEGWR RVTPEEVTEW
     VGEEVTGRWI EEGDVRVQMV GYERV
//
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