ID   DHPR_PIG                Reviewed;         243 AA.
AC   Q8MJ30;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 83.
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; Synonyms=DHPR;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12464030; DOI=10.1046/j.1365-2052.2002.00938_6.x;
RA   Kim J.G., Nonneman D., Vallet J.L., Rohrer G.A., Christenson R.K.;
RT   "Linkage mapping of a single nucleotide polymorphism (SNP) in the porcine
RT   QDPR gene to chromosome 8.";
RL   Anim. Genet. 33:474-474(2002).
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; AF526879; AAM91996.1; -; mRNA.
DR   RefSeq; NP_999508.1; NM_214343.2.
DR   AlphaFoldDB; Q8MJ30; -.
DR   SMR; Q8MJ30; -.
DR   STRING; 9823.ENSSSCP00000024691; -.
DR   PaxDb; Q8MJ30; -.
DR   PeptideAtlas; Q8MJ30; -.
DR   PRIDE; Q8MJ30; -.
DR   GeneID; 397619; -.
DR   KEGG; ssc:397619; -.
DR   CTD; 5860; -.
DR   eggNOG; KOG4022; Eukaryota.
DR   InParanoid; Q8MJ30; -.
DR   OrthoDB; 1585354at2759; -.
DR   BRENDA; 1.5.1.34; 6170.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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; Phosphoprotein; Reference proteome;
KW   Tetrahydrobiopterin biosynthesis.
FT   CHAIN           1..243
FT                   /note="Dihydropteridine reductase"
FT                   /id="PRO_0000054638"
FT   ACT_SITE        149
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         13..37
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         72
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BVI4"
FT   MOD_RES         78
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BVI4"
FT   MOD_RES         95
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BVI4"
FT   MOD_RES         101
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BVI4"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11348"
SQ   SEQUENCE   243 AA;  25758 MW;  53A6634FE7D015CC CRC64;
     MAAAAAGEAR RVLVYGGRGA LGSRCVQAFR ARNWWVASID VVENEEASAN VVVKMTDSFT
     EQADQVTAEV GKLLGTEKVD AILCVAGGWA GGNAKSKSLF KNCDLMWKQS MWTSTISSHL
     ATKHLKEGGL LTLAGAKAAL DGTPGMIGYG MAKGAVHQLC QSLAGKDSGM PSGAAAIAVL
     PVTLDTPLNR KSMPHADFSS WTPLEFLVET FHDWIIEKNR PSSGSLIQVV TTQGKTELTP
     AYF