ID   DHPR_BOVIN              Reviewed;         242 AA.
AC   Q3T0Z7;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Dihydropteridine reductase;
DE            EC=1.5.1.34 {ECO:0000250|UniProtKB:P09417};
DE   AltName: Full=HDHPR;
DE   AltName: Full=Quinoid dihydropteridine reductase;
GN   Name=QDPR;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of quinonoid dihydrobiopterin into
CC       tetrahydrobiopterin. {ECO:0000250|UniProtKB:P09417}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6,7,8-tetrahydropteridine + NAD(+) = 6,7-dihydropteridine +
CC         H(+) + NADH; Xref=Rhea:RHEA:17869, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28889, ChEBI:CHEBI:30156, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.5.1.34;
CC         Evidence={ECO:0000250|UniProtKB:P09417};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17871;
CC         Evidence={ECO:0000250|UniProtKB:P09417};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6,7,8-tetrahydropteridine + NADP(+) = 6,7-dihydropteridine +
CC         H(+) + NADPH; Xref=Rhea:RHEA:17865, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28889, ChEBI:CHEBI:30156, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.5.1.34;
CC         Evidence={ECO:0000250|UniProtKB:P09417};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17867;
CC         Evidence={ECO:0000250|UniProtKB:P09417};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11348}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; BC102193; AAI02194.1; -; mRNA.
DR   RefSeq; NP_001069960.1; NM_001076492.2.
DR   AlphaFoldDB; Q3T0Z7; -.
DR   SMR; Q3T0Z7; -.
DR   STRING; 9913.ENSBTAP00000049659; -.
DR   PaxDb; Q3T0Z7; -.
DR   PeptideAtlas; Q3T0Z7; -.
DR   PRIDE; Q3T0Z7; -.
DR   Ensembl; ENSBTAT00000055681; ENSBTAP00000049659; ENSBTAG00000040333.
DR   GeneID; 618084; -.
DR   KEGG; bta:618084; -.
DR   CTD; 5860; -.
DR   VEuPathDB; HostDB:ENSBTAG00000040333; -.
DR   VGNC; VGNC:33596; QDPR.
DR   eggNOG; KOG4022; Eukaryota.
DR   GeneTree; ENSGT00390000000470; -.
DR   HOGENOM; CLU_010194_22_0_1; -.
DR   InParanoid; Q3T0Z7; -.
DR   OMA; DWWVASI; -.
DR   OrthoDB; 1585354at2759; -.
DR   TreeFam; TF105932; -.
DR   Proteomes; UP000009136; Chromosome 6.
DR   Bgee; ENSBTAG00000040333; Expressed in corpus epididymis and 104 other tissues.
DR   ExpressionAtlas; Q3T0Z7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004155; F:6,7-dihydropteridine reductase activity; ISS:UniProtKB.
DR   GO; GO:0070404; F:NADH binding; IBA:GO_Central.
DR   GO; GO:0070402; F:NADPH binding; IBA:GO_Central.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   NADP; Oxidoreductase; Reference proteome; Tetrahydrobiopterin biosynthesis.
FT   CHAIN           1..242
FT                   /note="Dihydropteridine reductase"
FT                   /id="PRO_0000284384"
FT   ACT_SITE        148
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         12..36
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         71
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BVI4"
FT   MOD_RES         77
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BVI4"
FT   MOD_RES         94
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BVI4"
FT   MOD_RES         100
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BVI4"
SQ   SEQUENCE   242 AA;  25504 MW;  C200631990475C7E CRC64;
     MAAAAGEARR VLVYGGRGAL GSRCVQAFRA RNWWVASIDV QENEEASANV VVKMTDSFTE
     QADQVTAEVG KLLGTEKVDA ILCVAGGWAG GNAKSKSLFK NCDLMWKQSV WTSTISSHLA
     TKHLKEGGLL TLAGARAALD GTPGMIGYGM AKAAVHQLCQ SLAGKSSGLP PGAAAVALLP
     VTLDTPVNRK SMPEADFSSW TPLEFLVETF HDWITEKNRP SSGSLIQVVT TEGKTELTAA
     SP