Q8R536 (SPRE_MERUN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sepiapterin reductase
Short name=SPR
EC=1.1.1.153

Alternative name(s):
Benzil reductase
EC=1.1.1.n7

Gene names

Name:

SPR

Organism

Meriones unguiculatus (Mongolian jird) (Mongolian gerbil)

Taxonomic identifier

10047 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Gerbillinae › Meriones

Protein attributes

Sequence length	262 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin. The enzyme also catalyzes the reduction of benzil to (S)-benzoin.
Catalytic activity	7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH. Tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH. Benzoin + NADP+ = benzil + NADPH.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the sepiapterin reductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	tetrahydrobiopterin biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	nucleotide binding Inferred from electronic annotation. Source: InterPro sepiapterin reductase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 262	262	Sepiapterin reductase		PRO_0000327642
Regions
	Nucleotide binding	15 – 21	7	NADP By similarity
	Nucleotide binding	43 – 44	2	NADP By similarity
	Nucleotide binding	70 – 71	2	NADP By similarity
	Nucleotide binding	202 – 207	6	NADP By similarity
	Region	158 – 159	2	Substrate binding By similarity
Sites
	Binding site	171	1	Substrate By similarity
	Binding site	175	1	NADP By similarity
	Binding site	200	1	Substrate; via amide nitrogen By similarity
	Binding site	258	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8R536 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 72A1A83D198CE633	FASTA	262	28,007
	10 20 30 40 50 60 MESGGLGCAV CVLTGASRGF GRALAPRLAQ LLAPGSVLLL CARSDSALRR LEEELGAQQP 70 80 90 100 110 120 GLRVVRAAAD LGTEAGLRQV LRAVRELPKP EGLQRLLLIN NAGTLGDVSK GVLNVNDPAE 130 140 150 160 170 180 VNNYWALNLT SMLCLTSGTL NAFPDSPGLS KTVVNISSLC ALQPFKGWGL YCTGKAARDM 190 200 210 220 230 240 LCQVLAAEEP SVRVLSYAPG PLDTDMQQLA RETSMDPELR NRLQRLKSEG ELVDCGTSAQ 250 260 KLLNLLQKDT FQSGAHVDFY DN

References

[1]	"The enzymes with benzil reductase activity conserved from bacteria to mammals." Maruyama R., Nishizawa M., Itoi Y., Ito S., Inoue M. J. Biotechnol. 94:157-169(2002) [PubMed: 11796169] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: MGS/Sea. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB048357 mRNA. Translation: BAB86000.1.
3D structure databases
HSSP	HSSP built from PDB template 1OAA based on UniProtKB Q64105.
ProteinModelPortal	Q8R536.
SMR	Q8R536. Positions 5-261.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG006973.
Family and domain databases
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR006393. Sepiapterin_red. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH.
TIGRFAMs	TIGR01500. Sepiapter_red. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SPRE_MERUN

Accession

Primary (citable) accession number: Q8R536

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	June 1, 2002
Last modified:	December 14, 2011
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program