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Q65164

- TPRT_ASFB7

UniProt

Q65164 - TPRT_ASFB7

Protein

Trans-prenyltransferase

Gene

Ba71V-074

Organism
African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Trans-prenyltransferase that catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with different allylic diphosphates, such as dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylgeranyl diphosphate (GGPP), farnesyl diphosphate being the best allylic substrate.

    Catalytic activityi

    Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate.
    Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate.
    (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate.
    Geranylgeranyl diphosphate + isopentenyl diphosphate = diphosphate + geranylfarnesyl diphosphate.

    Cofactori

    Binds 3 magnesium ions per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei85 – 851Isopentenyl diphosphateBy similarity
    Binding sitei88 – 881Isopentenyl diphosphateBy similarity
    Binding sitei122 – 1221Isopentenyl diphosphateBy similarity
    Metal bindingi129 – 1291Magnesium 1By similarity
    Metal bindingi129 – 1291Magnesium 2By similarity
    Metal bindingi135 – 1351Magnesium 1By similarity
    Metal bindingi135 – 1351Magnesium 2By similarity
    Binding sitei140 – 1401Dimethylallyl diphosphateBy similarity
    Binding sitei141 – 1411Isopentenyl diphosphateBy similarity
    Binding sitei216 – 2161Dimethylallyl diphosphateBy similarity
    Binding sitei217 – 2171Dimethylallyl diphosphateBy similarity
    Binding sitei254 – 2541Dimethylallyl diphosphateBy similarity
    Metal bindingi257 – 2571Magnesium 3By similarity

    GO - Molecular functioni

    1. dimethylallyltranstransferase activity Source: UniProtKB-EC
    2. farnesyltranstransferase activity Source: UniProtKB-EC
    3. geranyltranstransferase activity Source: UniProtKB-EC
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. farnesyl diphosphate biosynthetic process Source: UniProtKB-UniPathway
    2. geranyl diphosphate biosynthetic process Source: UniProtKB-UniPathway
    3. geranylgeranyl diphosphate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Isoprene biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00259; UER00368.
    UPA00260; UER00369.
    UPA00389; UER00564.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trans-prenyltransferase (EC:2.5.1.-)
    Alternative name(s):
    (2E,6E)-farnesyl diphosphate synthase
    Dimethylallyltranstransferase (EC:2.5.1.1)
    Farnesyl diphosphate synthase
    Farnesyltranstransferase (EC:2.5.1.29)
    Geranyltranstransferase (EC:2.5.1.10)
    Polyprenyl-diphosphate synthase
    Gene namesi
    Ordered Locus Names:Ba71V-074
    ORF Names:B318L
    OrganismiAfrican swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV)
    Taxonomic identifieri10498 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAsfarviridaeAsfivirus
    Virus hostiOrnithodoros (relapsing fever ticks) [TaxID: 6937]
    Sus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000000624: Genome

    Subcellular locationi

    Host endoplasmic reticulum 1 Publication. Host membrane 1 Publication; Single-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. host cell endoplasmic reticulum Source: UniProtKB-SubCell
    2. host cell membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Host endoplasmic reticulum, Host membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 318318Trans-prenyltransferasePRO_0000373156Add
    BLAST

    Expressioni

    Inductioni

    Expressed late in the infection cycle.

    Keywords - Developmental stagei

    Late protein

    Structurei

    3D structure databases

    ProteinModelPortaliQ65164.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1 – 2121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    InterProiIPR000092. Polyprenyl_synt.
    IPR017446. Polyprenyl_synth-rel.
    IPR008949. Terpenoid_synth.
    [Graphical view]
    PANTHERiPTHR12001. PTHR12001. 1 hit.
    PfamiPF00348. polyprenyl_synt. 1 hit.
    [Graphical view]
    SUPFAMiSSF48576. SSF48576. 1 hit.
    PROSITEiPS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q65164-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLHLIYISII VVLIIILISY TRKPKYFRIT APRSVALFHG IHPLNPKNYK    50
    TFSKEFETIL NNAIEDGDFK GQLTEPCSYA LRGGKYIRPI ILMEIVRACQ 100
    LQHSFGAPIY PAEAALAVEY FHVASLIIDD MPSFDNDVKR RNKDTVWARF 150
    GVAKAQMSAL ALTMQGFQNI CRQIDWIKEH CPRFPDPNQL GALLCTFVSH 200
    SLNSAGSGQL VDTPEKTIPF FKIAFIMGWV LGTGTIEDIG MIERAAHCFG 250
    HAFQLADDIK DHDTDTGWNY AKIHGKQKTF DDVAQSLQEC KKILHGKKIF 300
    TSIWNEIFQK VINVALGT 318
    Length:318
    Mass (Da):35,905
    Last modified:November 1, 1996 - v1
    Checksum:i5279923BF0422CB0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18466 Genomic DNA. Translation: AAA65304.1.
    RefSeqiNP_042768.1. NC_001659.1.

    Genome annotation databases

    GeneIDi1488839.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18466 Genomic DNA. Translation: AAA65304.1 .
    RefSeqi NP_042768.1. NC_001659.1.

    3D structure databases

    ProteinModelPortali Q65164.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1488839.

    Enzyme and pathway databases

    UniPathwayi UPA00259 ; UER00368 .
    UPA00260 ; UER00369 .
    UPA00389 ; UER00564 .

    Family and domain databases

    Gene3Di 1.10.600.10. 1 hit.
    InterProi IPR000092. Polyprenyl_synt.
    IPR017446. Polyprenyl_synth-rel.
    IPR008949. Terpenoid_synth.
    [Graphical view ]
    PANTHERi PTHR12001. PTHR12001. 1 hit.
    Pfami PF00348. polyprenyl_synt. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48576. SSF48576. 1 hit.
    PROSITEi PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of the complete nucleotide sequence of African swine fever virus."
      Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C., Rodriguez J.F., Vinuela E.
      Virology 208:249-278(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiTPRT_ASFB7
    AccessioniPrimary (citable) accession number: Q65164
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 5, 2009
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3