ID   DYR_AEDAL               Reviewed;         186 AA.
AC   P28019;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Dihydrofolate reductase;
DE            EC=1.5.1.3;
GN   Name=DHFR;
OS   Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1915358; DOI=10.1111/j.1432-1033.1991.tb16268.x;
RA   Shotkoski F.A., Fallon A.M.;
RT   "An amplified insect dihydrofolate reductase gene contains a single
RT   intron.";
RL   Eur. J. Biochem. 201:157-160(1991).
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 (By similarity). {ECO:0000250}.
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00660};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC       tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC   -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC       {ECO:0000305}.
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DR   EMBL; X60192; CAA42748.1; -; Genomic_DNA.
DR   PIR; S17984; S17984.
DR   RefSeq; XP_019543834.1; XM_019688289.2.
DR   RefSeq; XP_019932082.1; XM_020076523.1.
DR   RefSeq; XP_019932490.1; XM_020076931.1.
DR   AlphaFoldDB; P28019; -.
DR   SMR; P28019; -.
DR   PRIDE; P28019; -.
DR   EnsemblMetazoa; AALF028131-RA; AALF028131-PA; AALF028131.
DR   GeneID; 109414458; -.
DR   GeneID; 109622266; -.
DR   KEGG; aalb:109414458; -.
DR   KEGG; aalb:109622266; -.
DR   VEuPathDB; VectorBase:AALC636_018370; -.
DR   VEuPathDB; VectorBase:AALC636_031623; -.
DR   VEuPathDB; VectorBase:AALF028131; -.
DR   VEuPathDB; VectorBase:AALFPA_045498; -.
DR   VEuPathDB; VectorBase:AALFPA_066294; -.
DR   VEuPathDB; VectorBase:AALFPA_074167; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000069940; Unplaced.
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; -; 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; PTHR48069; 1.
DR   Pfam; PF00186; DHFR_1; 1.
DR   SUPFAM; SSF53597; SSF53597; 1.
DR   PROSITE; PS00075; DHFR_1; 1.
DR   PROSITE; PS51330; DHFR_2; 1.
PE   3: Inferred from homology;
KW   NADP; One-carbon metabolism; Oxidoreductase.
FT   CHAIN           1..186
FT                   /note="Dihydrofolate reductase"
FT                   /id="PRO_0000186369"
FT   DOMAIN          3..183
FT                   /note="DHFR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00660"
FT   BINDING         9
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         15..21
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         29..34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         53..55
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         75..77
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         116..123
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   186 AA;  21447 MW;  AFCD7F469779D83C CRC64;
     MKKFSLIVAV CANGGIGIKG DLPWRLRQEL KYFSRMTKKI QDSGKRNAII MGRKTYFGVP
     ESKRPLPERL NIILTRDPSA NAYPSEVMVC TSMQEALKKL DEAPLVNEIE NVWIVGGNAV
     YKEAMQSDRC HRIYLTEIKE TFECDAFFPE ITSDFQLVKN DDDVPEDIQE ENGIQYQYRI
     YEKVPK