Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Sepiapterin reductase

Gene

Spr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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.

Kineticsi

  1. KM=12.6 µM for sepiapterin1 Publication
  2. KM=2.8 µM for NADPH1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei171SubstrateBy similarity1
    Binding sitei175NADPBy similarity1
    Binding sitei200Substrate; via amide nitrogenBy similarity1
    Binding sitei258SubstrateBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi15 – 21NADPBy similarity7
    Nucleotide bindingi43 – 44NADPBy similarity2
    Nucleotide bindingi70 – 71NADPBy similarity2
    Nucleotide bindingi202 – 207NADPBy similarity6

    GO - Molecular functioni

    • sepiapterin reductase activity Source: UniProtKB

    GO - Biological processi

    • response to organic substance Source: RGD
    • tetrahydrobiopterin biosynthetic process Source: RGD

    Keywordsi

    Molecular functionOxidoreductase
    LigandNADP

    Enzyme and pathway databases

    ReactomeiR-RNO-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
    R-RNO-203615 eNOS activation
    SABIO-RKiP18297

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sepiapterin reductase (EC:1.1.1.153)
    Short name:
    SPR
    Gene namesi
    Name:Spr
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Chromosome 4

    Organism-specific databases

    RGDi3753 Spr

    Subcellular locationi

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi29A → V: Reduces affinity for NADP and for sepiapterin 4-fold. 1 Publication1
    Mutagenesisi46S → A: Abolishes phosphorylation by CaMK2. No effect on kinetic parameters; when associated with A-196 and A-214. 1 Publication1
    Mutagenesisi158S → D: Reduces activity 4-fold. Loss of activity; when associated with V-171. 1 Publication1
    Mutagenesisi171Y → V: Reduces activity 4-fold. Loss of activity; when associated with V-171. 1 Publication1
    Mutagenesisi175K → I: Reduces activity 4-fold. 1 Publication1
    Mutagenesisi196S → A: Abolishes phosphorylation by CaMK2. No effect on kinetic parameters; when associated with A-46 and A-214. 1 Publication1
    Mutagenesisi214S → A: Abolishes phosphorylation by CaMK2. No effect on kinetic parameters; when associated with A-46 and A-196. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000721511 – 262Sepiapterin reductaseAdd BLAST262

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei1N-acetylmethionine1 Publication1
    Modified residuei33PhosphoserineCombined sources1
    Modified residuei46Phosphoserine; by CaMK2; in vitro1 Publication1
    Modified residuei196Phosphoserine; by CaMK2; in vitro1 Publication1
    Modified residuei214Phosphoserine; by CaMK2; in vitro1 Publication1

    Post-translational modificationi

    In vitro phosphorylation of Ser-46, Ser-196 and Ser-214 by CaMK2 does not change kinetic parameters.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP18297
    PRIDEiP18297

    PTM databases

    iPTMnetiP18297
    PhosphoSitePlusiP18297

    Expressioni

    Gene expression databases

    BgeeiENSRNOG00000015455
    ExpressionAtlasiP18297 baseline and differential
    GenevisibleiP18297 RN

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000020749

    Structurei

    3D structure databases

    ProteinModelPortaliP18297
    SMRiP18297
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni158 – 159Substrate bindingBy similarity2

    Sequence similaritiesi

    Belongs to the sepiapterin reductase family.Curated

    Phylogenomic databases

    eggNOGiKOG1204 Eukaryota
    ENOG4111PZG LUCA
    GeneTreeiENSGT00440000033609
    HOVERGENiHBG006973
    InParanoidiP18297
    KOiK00072
    OMAiLVDCKVS
    OrthoDBiEOG091G0N30
    PhylomeDBiP18297
    TreeFamiTF326358

    Family and domain databases

    InterProiView protein in InterPro
    IPR036291 NAD(P)-bd_dom_sf
    IPR002347 SDR_fam
    IPR006393 Sepiapterin_red
    PfamiView protein in Pfam
    PF00106 adh_short, 1 hit
    PRINTSiPR00081 GDHRDH
    SUPFAMiSSF51735 SSF51735, 1 hit
    TIGRFAMsiTIGR01500 sepiapter_red, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P18297-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEGGRLGCAV CVLTGASRGF GRALAPQLAG LLSPGSVLLL SARSDSMLRQ
    60 70 80 90 100
    LKEELCTQQP GLQVVLAAAD LGTESGVQQL LSAVRELPRP ERLQRLLLIN
    110 120 130 140 150
    NAGTLGDVSK GFLNINDLAE VNNYWALNLT SMLCLTTGTL NAFSNSPGLS
    160 170 180 190 200
    KTVVNISSLC ALQPFKGWGL YCAGKAARDM LYQVLAVEEP SVRVLSYAPG
    210 220 230 240 250
    PLDTNMQQLA RETSMDPELR SRLQKLNSEG ELVDCGTSAQ KLLSLLQRDT
    260
    FQSGAHVDFY DI
    Length:262
    Mass (Da):28,128
    Last modified:November 1, 1990 - v1
    Checksum:iEC992564A0334C61
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M36410 mRNA Translation: AAA42130.1
    PIRiA36024
    RefSeqiNP_062054.1, NM_019181.1
    UniGeneiRn.6658

    Genome annotation databases

    EnsembliENSRNOT00000020749; ENSRNOP00000020749; ENSRNOG00000015455
    GeneIDi29270
    KEGGirno:29270
    UCSCiRGD:3753 rat

    Similar proteinsi

    Entry informationi

    Entry nameiSPRE_RAT
    AccessioniPrimary (citable) accession number: P18297
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: May 23, 2018
    This is version 135 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health