ID   SPRE_BOVIN              Reviewed;         267 AA.
AC   Q17QK8; A7YKV0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Sepiapterin reductase;
DE            Short=SPR;
DE            EC=1.1.1.153;
GN   Name=SPR;
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 [MRNA].
RA   Pung Y.F., Cai H.;
RT   "Cloning and sequencing of cDNA encoding bovine sepiapterin reductase
RT   isoform 2.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the final one or two reductions in tetra-
CC       hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-erythro-7,8-dihydrobiopterin + NADP(+) = H(+) + NADPH +
CC         sepiapterin; Xref=Rhea:RHEA:18953, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16095, ChEBI:CHEBI:43029, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.153;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = 6-
CC         pyruvoyl-5,6,7,8-tetrahydropterin + 2 H(+) + 2 NADPH;
CC         Xref=Rhea:RHEA:32627, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:59560, ChEBI:CHEBI:136564;
CC         EC=1.1.1.153;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sepiapterin reductase family. {ECO:0000305}.
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DR   EMBL; DQ978331; ABI79460.1; -; mRNA.
DR   EMBL; BC118299; AAI18300.1; -; mRNA.
DR   RefSeq; NP_001069471.1; NM_001076003.1.
DR   AlphaFoldDB; Q17QK8; -.
DR   SMR; Q17QK8; -.
DR   STRING; 9913.ENSBTAP00000029280; -.
DR   PaxDb; Q17QK8; -.
DR   PRIDE; Q17QK8; -.
DR   GeneID; 533836; -.
DR   KEGG; bta:533836; -.
DR   CTD; 6697; -.
DR   eggNOG; KOG1204; Eukaryota.
DR   HOGENOM; CLU_010194_2_11_1; -.
DR   InParanoid; Q17QK8; -.
DR   OrthoDB; 1089743at2759; -.
DR   TreeFam; TF326358; -.
DR   BRENDA; 1.1.1.153; 908.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004757; F:sepiapterin reductase activity; ISS:UniProtKB.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   InterPro; IPR006393; Sepiapterin_red.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01500; sepiapter_red; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; NADP; Oxidoreductase; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..267
FT                   /note="Sepiapterin reductase"
FT                   /id="PRO_0000327641"
FT   BINDING         20..26
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         48..49
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         75..76
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         163..164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         207..212
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P18297"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18297"
FT   MOD_RES         201
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18297"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35270"
FT   CONFLICT        236
FT                   /note="E -> Q (in Ref. 1; ABI79460)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   267 AA;  28939 MW;  4F2B7089A40F8C52 CRC64;
     MEGSVGKVGG LGRTLCVLTG ASRGFGRTLA QVLAPLMSPR SVLVLSARND EALRQLETEL
     GAEWPGLRIV RVPADLGAET GLQQLVGALC DLPRPEGLQR VLLINNAGTL GDVSKRWVDL
     TDPTEVNNYW TLNLTSTLCL TSSILQAFPD SPGLSRTVVN ISSICALQPF KGWGLYCAGK
     AARNMMFQVL AAEEPSVRVL SYGPGPLDTD MQQLARETSV DPDLRKSLQE LKRKGELVDC
     KISAQKLLSL LQNDKFESGA HIDFYDE