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 14-DEC-2022, entry version 79. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; NAD(P)-binding Rossmann-fold domains; 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 //