ID   SPRE_XENTR              Reviewed;         261 AA.
AC   B0BML7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Sepiapterin reductase;
DE            Short=SPR;
DE            EC=1.1.1.153;
GN   Name=spr;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2008) 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; BC158483; AAI58484.1; -; mRNA.
DR   RefSeq; NP_001120067.1; NM_001126595.1.
DR   AlphaFoldDB; B0BML7; -.
DR   SMR; B0BML7; -.
DR   STRING; 8364.ENSXETP00000060132; -.
DR   PaxDb; B0BML7; -.
DR   GeneID; 100145068; -.
DR   KEGG; xtr:100145068; -.
DR   CTD; 6697; -.
DR   eggNOG; KOG1204; Eukaryota.
DR   InParanoid; B0BML7; -.
DR   OrthoDB; 1089743at2759; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; 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; IEA:InterPro.
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   Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..261
FT                   /note="Sepiapterin reductase"
FT                   /id="PRO_0000327644"
FT   BINDING         16..22
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         44..45
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         71..72
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         158..159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         202..207
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   261 AA;  28359 MW;  124DB39935624B1F CRC64;
     MAATGALGSV LCVLTGASRG FGRTLAHLLC PRLLPGSTLL LVSRTEEALK GLAGELAHKY
     PGVRVRWEAA DLGTSEGVSA AVRAAGELQV GAAQKLLIIN NAGSIGDVSK MFVDFSDPKE
     VTDYMMFNVS SPLCLTASLL KTFPRRPDLQ RVVVNVSSLA ALQPFKSWAL YCSGKAARDM
     IFRVLAEEEK DVRVLNYAPG PLDTDMHVVA RTQTADPELR RFLMDRKEKG KMVDIQVSAK
     KMLDLLEADA YKSGDHIDFF D