ID   SPRE_MERUN              Reviewed;         262 AA.
AC   Q8R536;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Sepiapterin reductase;
DE            Short=SPR;
DE            EC=1.1.1.153;
DE   AltName: Full=Benzil reductase ((S)-benzoin forming);
DE            EC=1.1.1.320;
GN   Name=SPR;
OS   Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Gerbillinae; Meriones.
OX   NCBI_TaxID=10047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=MGS/Sea; TISSUE=Liver;
RX   PubMed=11796169; DOI=10.1016/s0168-1656(01)00426-6;
RA   Maruyama R., Nishizawa M., Itoi Y., Ito S., Inoue M.;
RT   "The enzymes with benzil reductase activity conserved from bacteria to
RT   mammals.";
RL   J. Biotechnol. 94:157-169(2002).
CC   -!- FUNCTION: Catalyzes the final one or two reductions in tetra-
CC       hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin. The
CC       enzyme also catalyzes the reduction of benzil to (S)-benzoin.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-benzoin + NADP(+) = benzil + H(+) + NADPH;
CC         Xref=Rhea:RHEA:25968, ChEBI:CHEBI:15378, ChEBI:CHEBI:51507,
CC         ChEBI:CHEBI:51510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.320;
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; AB048357; BAB86000.1; -; mRNA.
DR   AlphaFoldDB; Q8R536; -.
DR   SMR; Q8R536; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0102306; F:benzil reductase [(S)-benzoin-forming] activity; IEA:UniProtKB-EC.
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   Acetylation; Cytoplasm; NADP; Oxidoreductase; Phosphoprotein.
FT   CHAIN           1..262
FT                   /note="Sepiapterin reductase"
FT                   /id="PRO_0000327642"
FT   BINDING         15..21
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         43..44
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         70..71
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"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P18297"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18297"
FT   MOD_RES         196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18297"
FT   MOD_RES         214
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35270"
SQ   SEQUENCE   262 AA;  28007 MW;  72A1A83D198CE633 CRC64;
     MESGGLGCAV CVLTGASRGF GRALAPRLAQ LLAPGSVLLL CARSDSALRR LEEELGAQQP
     GLRVVRAAAD LGTEAGLRQV LRAVRELPKP EGLQRLLLIN NAGTLGDVSK GVLNVNDPAE
     VNNYWALNLT SMLCLTSGTL NAFPDSPGLS KTVVNISSLC ALQPFKGWGL YCTGKAARDM
     LCQVLAAEEP SVRVLSYAPG PLDTDMQQLA RETSMDPELR NRLQRLKSEG ELVDCGTSAQ
     KLLNLLQKDT FQSGAHVDFY DN