Search by BoMiProt ID - Bomi9019

Primary Information

BoMiProt ID Bomi9019
Protein Name Sepiapterin reductase
Organism Bos taurus
Uniprot IDQ17QK8
Milk FractionExosomes
Ref Sequence ID NP_001069471.1
Aminoacid Length 267
Molecular Weight 28939
FASTA Sequence Download
Gene Name SPR
Gene ID 533836
Protein Existence Status Reviewed

Secondary Information

Protein Function Sepiapterin reductase, a homodimer composed of two subunits, plays an important role in the biosynthesis of tetrahydrobiopterin. 
Biochemical Properties This protein has 261 amino acids of each monomer fold into a single domain with an α/β‐structure. A seven‐stranded anti‐parallel oriented β‐sheet in the centre of the molecule is sandwiched by two arrays of three α‐helices. Six of these strands could form a classic nicotinamide‐binding motif composed of βαβ units. The association of two monomers into the active homodimeric SPR leads to the formation of a four‐helix bundle (helices αE and αF of each monomer).
PTMs N-acetylation at Meth,Phosphorylation at Ser
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Additional Comments  Sepiapterin reductase exhibits a wide distribution in different tissues and is associated with many diseases, including brain dysfunction, chronic pain, cardiovascular disease and cancer.
Bibliography 1.Wu Y, Chen P, Sun L, Yuan S, Cheng Z, Lu L, Du H, Zhan M. Sepiapterin reductase: Characteristics and role in diseases. J Cell Mol Med. 2020 Sep;24(17):9495-9506. doi: 10.1111/jcmm.15608. Epub 2020 Jul 30. PMID: 32734666; PMCID: PMC7520308. 2.Auerbach G, Herrmann A, Gütlich M, et al. The 1.25 Å crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters. EMBO J. 1997;16:7219‐7230. 3.Supangat S, Seo KH, Choi YK, et al. Structure of chlorobium tepidum sepiapterin reductase complex reveals the novel substrate binding mode for stereospecific production of L‐threo‐tetrahydrobiopterin. J Biol Chem. 2006;281:2245‐2256.