ID   SPRE_XENLA              Reviewed;         263 AA.
AC   Q7ZY31;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Sepiapterin reductase;
DE            Short=SPR;
DE            EC=1.1.1.153;
GN   Name=spr;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) 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; BC043999; AAH43999.1; -; mRNA.
DR   RefSeq; NP_001080581.1; NM_001087112.1.
DR   AlphaFoldDB; Q7ZY31; -.
DR   SMR; Q7ZY31; -.
DR   MaxQB; Q7ZY31; -.
DR   DNASU; 380273; -.
DR   GeneID; 380273; -.
DR   KEGG; xla:380273; -.
DR   CTD; 380273; -.
DR   OrthoDB; 1089743at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 380273; Expressed in kidney and 20 other tissues.
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..263
FT                   /note="Sepiapterin reductase"
FT                   /id="PRO_0000327643"
FT   BINDING         18..24
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         46..47
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         73..74
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         160..161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         204..209
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   263 AA;  28706 MW;  5B20B26508DAADDD CRC64;
     MTAARAGALG SVLCVLTGAS RGFGRTLAHE LCPRVLPGST LLLVSRTEEA LKGLAEELGH
     EFPGVRVRWA AADLSTTEGV SATVRAAREL QAGTAHRLLI INNAGSIGDV SKMFVDFSAP
     EEVTEYMKFN VSSPLCLTAS LLKTFPRRPD LQRLVVNVSS LAALQPYKSW VLYCSGKAAR
     DMMFRVLAEE EDDVRVLSYA PGPLDTDMHE VACTQTADPE LRRAIMDRKE KGNMVDIRVS
     ANKMLDLLEA DAYKSGDHID FYD