Trans-prenyltransferase - African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)

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Reviewed, UniProtKB/Swiss-Prot Q65164 (TPRT_ASFB7)

Last modified January 19, 2010. Version 55. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Trans-prenyltransferase
    EC=2.5.1.-
Alternative name(s):
    Polyprenyl-diphosphate synthase
    Dimethylallyltranstransferase
    EC=2.5.1.1
    Geranyltranstransferase
    EC=2.5.1.10
    Farnesyltranstransferase
    EC=2.5.1.29

Gene names

Ordered Locus Names:	Ba71V-074
ORF Names:	B318L

Organism

African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV)

Taxonomic identifier

10498 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Asfarviridae › Asfivirus

Virus host

Ornithodoros (relapsing fever ticks) [TaxID: 6937]
Sus scrofa (Pig) [TaxID: 9823]

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Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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 activity	Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate. Geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate. Trans,trans-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate. Geranylgeranyl diphosphate + isopentenyl diphosphate = diphosphate + geranylfarnesyl diphosphate.
Cofactor	Binds 3 magnesium ions per subunit By similarity.
Pathway	Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1. Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1. Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1.
Subcellular location	Host endoplasmic reticulum. Host membrane; Single-pass membrane protein Ref.2.
Induction	Expressed late in the infection cycle.
Sequence similarities	Belongs to the FPP/GGPP synthetase family. Asfivirus trans-prenyltransferase subfamily.

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Ontologies

Keywords
Biological process	Isoprene biosynthesis
Cellular component	Host endoplasmic reticulum Host membrane Membrane
Developmental stage	Late protein
Domain	Transmembrane
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	Complete proteome Virus reference strain
Gene Ontology (GO)
Biological process	isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	host cell endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dimethylallyltranstransferase activity Inferred from electronic annotation. Source: EC farnesyltranstransferase activity Inferred from electronic annotation. Source: EC geranyltranstransferase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 318

318

Trans-prenyltransferase

PRO_0000373156

Regions

Transmembrane

1 – 21

Potential

Sites

Metal binding

129

Magnesium 1 By similarity

Metal binding

129

Magnesium 2 By similarity

Metal binding

135

Magnesium 1 By similarity

Metal binding

135

Magnesium 2 By similarity

Metal binding

257

Magnesium 3 By similarity

Binding site

Isopentenyl diphosphate By similarity

Binding site

Isopentenyl diphosphate By similarity

Binding site

122

Isopentenyl diphosphate By similarity

Binding site

140

Dimethylallyl diphosphate By similarity

Binding site

141

Isopentenyl diphosphate By similarity

Binding site

216

Dimethylallyl diphosphate By similarity

Binding site

217

Dimethylallyl diphosphate By similarity

Binding site

254

Dimethylallyl diphosphate By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q65164-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5279923BF0422CB0
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FASTA

318

35,905

        10         20         30         40         50         60 
MLHLIYISII VVLIIILISY TRKPKYFRIT APRSVALFHG IHPLNPKNYK TFSKEFETIL 

        70         80         90        100        110        120 
NNAIEDGDFK GQLTEPCSYA LRGGKYIRPI ILMEIVRACQ LQHSFGAPIY PAEAALAVEY 

       130        140        150        160        170        180 
FHVASLIIDD MPSFDNDVKR RNKDTVWARF GVAKAQMSAL ALTMQGFQNI CRQIDWIKEH 

       190        200        210        220        230        240 
CPRFPDPNQL GALLCTFVSH SLNSAGSGQL VDTPEKTIPF FKIAFIMGWV LGTGTIEDIG 

       250        260        270        280        290        300 
MIERAAHCFG HAFQLADDIK DHDTDTGWNY AKIHGKQKTF DDVAQSLQEC KKILHGKKIF 

       310 
TSIWNEIFQK VINVALGT

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11831707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"African swine fever virus trans-prenyltransferase." Alejo A., Yanez R.J., Rodriguez J.M., Vinuela E., Salas M.L. J. Biol. Chem. 272:9417-9423(1997) [PubMed: 9083080] [Abstract] Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	U18466 Genomic DNA. Translation: AAA65304.1.
RefSeq	NP_042768.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1488839.
Family and domain databases
InterPro	IPR000092. Polyprenyl_synt. IPR017446. Polyprenyl_synth-rel. IPR008949. Terpenoid_synth. [Graphical view]
Gene3D	G3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
PANTHER	PTHR12001. Polyprenyl_synt. 1 hit.
Pfam	PF00348. polyprenyl_synt. 1 hit. [Graphical view]
PROSITE	PS00723. POLYPRENYL_SYNTHET_1. False negative. PS00444. POLYPRENYL_SYNTHET_2. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

TPRT_ASFB7

Accession

Primary (citable) accession number: Q65164

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Family and domain databases

Entry information

Relevant documents