ID   L5KJI5_PTEAL            Unreviewed;       186 AA.
AC   L5KJI5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Dihydrofolate reductase {ECO:0000256|ARBA:ARBA00018886};
DE            EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN   ORFNames=PAL_GLEAN10024944 {ECO:0000313|EMBL:ELK11482.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK11482.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(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; KB030673; ELK11482.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5KJI5; -.
DR   STRING; 9402.L5KJI5; -.
DR   eggNOG; KOG1324; Eukaryota.
DR   InParanoid; L5KJI5; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000010552; 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:0031427; P:response to methotrexate; 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:SF6; 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   Methotrexate resistance {ECO:0000256|ARBA:ARBA00022609};
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:UP000010552}.
FT   DOMAIN          4..184
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
SQ   SEQUENCE   186 AA;  21442 MW;  BCD3B2167B1FD23C CRC64;
     MVRSLNCIVA VSQNMGIGKN GDLPWPPLRN EFKYFQRMTT TSSEGKRNLV IMGRKTWFSI
     PKKNRPLKDR INLVLSRELK EPPKGAHFLA KSLDDALKLI EQPELRSKVD MVWIVGGSSV
     YKEAMSKPGH IKLFVTKIMQ EFESDTFFPE IDLGKYKLLP EYPGVLSDVQ EEKGIKYKFE
     VYEKND
//