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 28-NOV-2012, entry version 54. 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 MEDLINE=21655309; 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 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the sepiapterin reductase family. 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 HSSP; Q64105; 1OAA. DR ProteinModelPortal; Q8R536; -. DR SMR; Q8R536; 5-261. DR HOVERGEN; HBG006973; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. 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; NAD(P)-bd; 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 Cytoplasm; NADP; Oxidoreductase. FT CHAIN 1 262 Sepiapterin reductase. FT /FTId=PRO_0000327642. FT NP_BIND 15 21 NADP (By similarity). FT NP_BIND 43 44 NADP (By similarity). FT NP_BIND 70 71 NADP (By similarity). FT NP_BIND 202 207 NADP (By similarity). FT REGION 158 159 Substrate binding (By similarity). FT BINDING 171 171 Substrate (By similarity). FT BINDING 175 175 NADP (By similarity). FT BINDING 200 200 Substrate; via amide nitrogen (By FT similarity). FT BINDING 258 258 Substrate (By similarity). 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 //