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Protein

Sepiapterin reductase

Gene

Spr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.

Catalytic activityi

L-erythro-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH.
L-erythro-tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei171Substrate1
Binding sitei175NADP1
Binding sitei200Substrate; via amide nitrogen1
Binding sitei222Substrate1
Binding sitei258Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi15 – 21NADP7
Nucleotide bindingi43 – 44NADP2
Nucleotide bindingi70 – 71NADP2
Nucleotide bindingi202 – 207NADP6

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • sepiapterin reductase activity Source: UniProtKB

GO - Biological processi

  • cell morphogenesis involved in neuron differentiation Source: MGI
  • dopamine metabolic process Source: MGI
  • L-phenylalanine metabolic process Source: MGI
  • nitric oxide biosynthetic process Source: MGI
  • norepinephrine metabolic process Source: MGI
  • pteridine metabolic process Source: MGI
  • regulation of multicellular organism growth Source: MGI
  • serotonin metabolic process Source: MGI
  • tetrahydrobiopterin biosynthetic process Source: InterPro
  • tetrahydrobiopterin metabolic process Source: MGI
  • voluntary musculoskeletal movement Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.153. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Sepiapterin reductase (EC:1.1.1.153)
Short name:
SPR
Gene namesi
Name:Spr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:103078. Spr.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000721501 – 261Sepiapterin reductaseAdd BLAST261

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei33PhosphoserineBy similarity1
Modified residuei46PhosphoserineBy similarity1
Modified residuei196PhosphoserineBy similarity1
Modified residuei214PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ64105.
MaxQBiQ64105.
PaxDbiQ64105.
PeptideAtlasiQ64105.
PRIDEiQ64105.

2D gel databases

REPRODUCTION-2DPAGEQ64105.

PTM databases

iPTMnetiQ64105.
PhosphoSitePlusiQ64105.
SwissPalmiQ64105.

Expressioni

Gene expression databases

CleanExiMM_SPR.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

MINTiMINT-1869513.
STRINGi10090.ENSMUSP00000048111.

Structurei

Secondary structure

1261
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 15Combined sources9
Helixi19 – 29Combined sources11
Beta strandi37 – 43Combined sources7
Helixi45 – 58Combined sources14
Beta strandi62 – 68Combined sources7
Helixi74 – 86Combined sources13
Beta strandi95 – 100Combined sources6
Helixi112 – 114Combined sources3
Helixi118 – 128Combined sources11
Helixi130 – 141Combined sources12
Beta strandi150 – 156Combined sources7
Helixi159 – 161Combined sources3
Helixi169 – 188Combined sources20
Beta strandi192 – 198Combined sources7
Beta strandi201 – 204Combined sources4
Helixi205 – 213Combined sources9
Helixi217 – 228Combined sources12
Helixi235 – 248Combined sources14
Beta strandi255 – 258Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NASX-ray2.10A3-261[»]
1OAAX-ray1.25A3-261[»]
1SEPX-ray1.95A1-261[»]
ProteinModelPortaliQ64105.
SMRiQ64105.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64105.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni158 – 159Substrate binding2

Sequence similaritiesi

Belongs to the sepiapterin reductase family.Curated

Phylogenomic databases

eggNOGiKOG1204. Eukaryota.
ENOG4111PZG. LUCA.
HOVERGENiHBG006973.
InParanoidiQ64105.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
IPR006393. Sepiapterin_red.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01500. sepiapter_red. 1 hit.

Sequencei

Sequence statusi: Complete.

Q64105-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEADGLGCAV CVLTGASRGF GRALAPQLAR LLSPGSVMLV SARSESMLRQ
60 70 80 90 100
LKEELGAQQP DLKVVLAAAD LGTEAGVQRL LSAVRELPRP EGLQRLLLIN
110 120 130 140 150
NAATLGDVSK GFLNVNDLAE VNNYWALNLT SMLCLTSGTL NAFQDSPGLS
160 170 180 190 200
KTVVNISSLC ALQPYKGWGL YCAGKAARDM LYQVLAAEEP SVRVLSYAPG
210 220 230 240 250
PLDNDMQQLA RETSKDPELR SKLQKLKSDG ALVDCGTSAQ KLLGLLQKDT
260
FQSGAHVDFY D
Length:261
Mass (Da):27,883
Last modified:November 1, 1997 - v1
Checksum:i102294E439CB8AEC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4D → G in AAC69364 (PubMed:10209270).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S77493 mRNA. Translation: AAB33611.1.
U78077, U78076 Genomic DNA. Translation: AAC69364.1.
S71375 mRNA. No translation available.
PIRiS52110.
UniGeneiMm.28393.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S77493 mRNA. Translation: AAB33611.1.
U78077, U78076 Genomic DNA. Translation: AAC69364.1.
S71375 mRNA. No translation available.
PIRiS52110.
UniGeneiMm.28393.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NASX-ray2.10A3-261[»]
1OAAX-ray1.25A3-261[»]
1SEPX-ray1.95A1-261[»]
ProteinModelPortaliQ64105.
SMRiQ64105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1869513.
STRINGi10090.ENSMUSP00000048111.

PTM databases

iPTMnetiQ64105.
PhosphoSitePlusiQ64105.
SwissPalmiQ64105.

2D gel databases

REPRODUCTION-2DPAGEQ64105.

Proteomic databases

EPDiQ64105.
MaxQBiQ64105.
PaxDbiQ64105.
PeptideAtlasiQ64105.
PRIDEiQ64105.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:103078. Spr.

Phylogenomic databases

eggNOGiKOG1204. Eukaryota.
ENOG4111PZG. LUCA.
HOVERGENiHBG006973.
InParanoidiQ64105.

Enzyme and pathway databases

BRENDAi1.1.1.153. 3474.

Miscellaneous databases

ChiTaRSiSpr. mouse.
EvolutionaryTraceiQ64105.
PROiQ64105.
SOURCEiSearch...

Gene expression databases

CleanExiMM_SPR.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
IPR006393. Sepiapterin_red.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01500. sepiapter_red. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSPRE_MOUSE
AccessioniPrimary (citable) accession number: Q64105
Secondary accession number(s): Q63996
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.