Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P43152

- HPRT_LEIDO

UniProt

P43152 - HPRT_LEIDO

Protein

Hypoxanthine-guanine phosphoribosyltransferase

Gene
N/A
Organism
Leishmania donovani
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway By similarity.By similarity

    Catalytic activityi

    IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate.
    GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate.

    Cofactori

    Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei66 – 661GMPBy similarity
    Active sitei129 – 1291Proton acceptorBy similarity
    Binding sitei157 – 1571GMPBy similarity
    Metal bindingi185 – 1851MagnesiumBy similarity
    Binding sitei185 – 1851GMP; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi125 – 1339GMPBy similarity

    GO - Molecular functioni

    1. guanine phosphoribosyltransferase activity Source: UniProtKB-EC
    2. hypoxanthine phosphoribosyltransferase activity Source: UniProtKB-EC
    3. metal ion binding Source: UniProtKB-KW
    4. nucleotide binding Source: UniProtKB-KW

    GO - Biological processi

    1. IMP salvage Source: UniProtKB-UniPathway
    2. purine ribonucleoside salvage Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Keywords - Ligandi

    Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00591; UER00648.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hypoxanthine-guanine phosphoribosyltransferase (EC:2.4.2.8)
    Short name:
    HGPRT
    Short name:
    HGPRTase
    OrganismiLeishmania donovani
    Taxonomic identifieri5661 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 211211Hypoxanthine-guanine phosphoribosyltransferasePRO_0000139593Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP43152.
    SMRiP43152. Positions 20-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    KOiK00760.

    Family and domain databases

    Gene3Di3.40.50.2020. 1 hit.
    InterProiIPR005904. Hxn_phspho_trans.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    [Graphical view]
    PfamiPF00156. Pribosyltran. 1 hit.
    [Graphical view]
    SUPFAMiSSF53271. SSF53271. 1 hit.
    TIGRFAMsiTIGR01203. HGPRTase. 1 hit.
    PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P43152-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNSAKSPSG PVGDEGRRNY PMSAHTLVTQ EQVWAATAKC AKKIAEDYRS    50
    FKLTTDNPLY LLCVLKGSFI FTADLARFLA DEGVPVKVEF ICASSYGTGV 100
    ETSGQVRMLL DVRDSVENRH ILIVEDIVDS AITLQYLMRF MLAKKPASLK 150
    TVVLLDKPSG RKVEVLVDYP VITIPHAFVI GYGMDYAESY RELRDICVLK 200
    KEYYEKPESK V 211
    Length:211
    Mass (Da):23,612
    Last modified:November 1, 1995 - v1
    Checksum:i7802A85B00CA2190
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25412 Genomic DNA. Translation: AAB00074.1.
    RefSeqiXP_003860615.1. XM_003860567.1.

    Genome annotation databases

    GeneIDi13386422.
    KEGGildo:LDBPK_210980.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25412 Genomic DNA. Translation: AAB00074.1 .
    RefSeqi XP_003860615.1. XM_003860567.1.

    3D structure databases

    ProteinModelPortali P43152.
    SMRi P43152. Positions 20-201.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 13386422.
    KEGGi ldo:LDBPK_210980.

    Phylogenomic databases

    KOi K00760.

    Enzyme and pathway databases

    UniPathwayi UPA00591 ; UER00648 .

    Family and domain databases

    Gene3Di 3.40.50.2020. 1 hit.
    InterProi IPR005904. Hxn_phspho_trans.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    [Graphical view ]
    Pfami PF00156. Pribosyltran. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53271. SSF53271. 1 hit.
    TIGRFAMsi TIGR01203. HGPRTase. 1 hit.
    PROSITEi PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of the hypoxanthine-guanine phosphoribosyltransferase from Leishmania donovani."
      Allen T.E., Hwang H.Y., Jardim A., Olafson R., Ullman B.
      Mol. Biochem. Parasitol. 73:133-143(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: MHOM/SD/62/1S.

    Entry informationi

    Entry nameiHPRT_LEIDO
    AccessioniPrimary (citable) accession number: P43152
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 66 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3