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 29-OCT-2014, entry version 59. 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) (Mongolian gerbil). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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. CC The enzyme also catalyzes the reduction of benzil to (S)-benzoin. CC -!- CATALYTIC ACTIVITY: L-erythro-7,8-dihydrobiopterin + NADP(+) = CC sepiapterin + NADPH. CC -!- CATALYTIC ACTIVITY: L-erythro-tetrahydrobiopterin + 2 NADP(+) = 6- CC pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH. CC -!- CATALYTIC ACTIVITY: (S)-benzoin + NADP(+) = benzil + NADPH. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the sepiapterin reductase family. CC {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 ProteinModelPortal; Q8R536; -. DR SMR; Q8R536; 5-261. DR HOVERGEN; HBG006973; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0004757; F:sepiapterin reductase activity; ISS:UniProtKB. DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006393; Sepiapterin_red. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR TIGRFAMs; TIGR01500; sepiapter_red; 1. PE 2: Evidence at transcript level; KW Acetylation; Cytoplasm; NADP; Oxidoreductase; Phosphoprotein. FT CHAIN 1 262 Sepiapterin reductase. FT /FTId=PRO_0000327642. FT NP_BIND 15 21 NADP. {ECO:0000250}. FT NP_BIND 43 44 NADP. {ECO:0000250}. FT NP_BIND 70 71 NADP. {ECO:0000250}. FT NP_BIND 202 207 NADP. {ECO:0000250}. FT REGION 158 159 Substrate binding. {ECO:0000250}. FT BINDING 171 171 Substrate. {ECO:0000250}. FT BINDING 175 175 NADP. {ECO:0000250}. FT BINDING 200 200 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 258 258 Substrate. {ECO:0000250}. FT MOD_RES 1 1 N-acetylmethionine. {ECO:0000250}. FT MOD_RES 46 46 Phosphoserine. {ECO:0000250}. FT MOD_RES 196 196 Phosphoserine. {ECO:0000250}. FT MOD_RES 214 214 Phosphoserine. {ECO:0000250}. 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 //