ID TPRT_ASFB7 Reviewed; 318 AA. AC Q65164; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 101. DE RecName: Full=Trans-prenyltransferase; DE EC=2.5.1.-; DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase; DE AltName: Full=Dimethylallyltranstransferase; DE EC=2.5.1.1; DE AltName: Full=Farnesyl diphosphate synthase; DE AltName: Full=Farnesyltranstransferase; DE EC=2.5.1.29; DE AltName: Full=Geranyltranstransferase; DE EC=2.5.1.10; DE AltName: Full=Polyprenyl-diphosphate synthase; GN OrderedLocusNames=Ba71V-074; ORFNames=B318L; OS African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) OS (ASFV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Asfuvirales; Asfarviridae; Asfivirus; African swine fever virus. OX NCBI_TaxID=10498; OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks). OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11831707; DOI=10.1006/viro.1995.1149; RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C., RA Rodriguez J.F., Vinuela E.; RT "Analysis of the complete nucleotide sequence of African swine fever RT virus."; RL Virology 208:249-278(1995). RN [2] RP CHARACTERIZATION, AND SUBCELLULAR LOCATION. RX PubMed=9083080; DOI=10.1074/jbc.272.14.9417; RA Alejo A., Yanez R.J., Rodriguez J.M., Vinuela E., Salas M.L.; RT "African swine fever virus trans-prenyltransferase."; RL J. Biol. Chem. 272:9417-9423(1997). RN [3] RP INDUCTION. RX PubMed=32075923; DOI=10.1128/jvi.00119-20; RA Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J., RA Dixon L., Werner F.; RT "The African Swine Fever Virus Transcriptome."; RL J. Virol. 94:0-0(2020). CC -!- FUNCTION: Trans-prenyltransferase that catalyzes the sequential CC condensation of isopentenyl diphosphate (IPP) with different allylic CC diphosphates, such as dimethylallyl diphosphate (DMAPP), geranyl CC diphosphate (GPP), farnesyl diphosphate (FPP) and geranylgeranyl CC diphosphate (GGPP), farnesyl diphosphate being the best allylic CC substrate. CC -!- CATALYTIC ACTIVITY: CC Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)- CC geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, CC ChEBI:CHEBI:128769; EC=2.5.1.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)- CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, CC ChEBI:CHEBI:175763; EC=2.5.1.10; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl CC diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + CC diphosphate; Xref=Rhea:RHEA:25694, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57907, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250}; CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; CC farnesyl diphosphate from geranyl diphosphate and isopentenyl CC diphosphate: step 1/1. CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl CC diphosphate: step 1/1. CC -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate CC biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and CC isopentenyl diphosphate: step 1/1. CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum CC {ECO:0000269|PubMed:9083080}. Host membrane CC {ECO:0000269|PubMed:9083080}; Single-pass membrane protein CC {ECO:0000269|PubMed:9083080}. CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle. CC {ECO:0000269|PubMed:32075923}. CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. Asfivirus trans- CC prenyltransferase subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U18466; AAA65304.1; -; Genomic_DNA. DR RefSeq; NP_042768.1; NC_001659.2. DR PDB; 8HDL; X-ray; 3.20 A; A=31-318. DR PDBsum; 8HDL; -. DR SMR; Q65164; -. DR GeneID; 22220304; -. DR KEGG; vg:22220304; -. DR UniPathway; UPA00259; UER00368. DR UniPathway; UPA00260; UER00369. DR UniPathway; UPA00389; UER00564. DR Proteomes; UP000000624; Segment. DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:UniProtKB-EC. DR GO; GO:0044687; F:geranylfarnesyl diphosphate synthase activity; IEA:RHEA. DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf. DR InterPro; IPR000092; Polyprenyl_synt. DR PANTHER; PTHR43281; FARNESYL DIPHOSPHATE SYNTHASE; 1. DR PANTHER; PTHR43281:SF1; FARNESYL DIPHOSPHATE SYNTHASE; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Host endoplasmic reticulum; Host membrane; KW Isoprene biosynthesis; Late protein; Magnesium; Membrane; Metal-binding; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..318 FT /note="Trans-prenyltransferase" FT /id="PRO_0000373156" FT TRANSMEM 1..21 FT /note="Helical" FT /evidence="ECO:0000255" FT BINDING 85 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 88 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 122 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 129 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 129 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 135 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 135 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 140 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 141 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:P14324" FT BINDING 216 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 217 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT BINDING 254 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" SQ SEQUENCE 318 AA; 35905 MW; 5279923BF0422CB0 CRC64; MLHLIYISII VVLIIILISY TRKPKYFRIT APRSVALFHG IHPLNPKNYK TFSKEFETIL NNAIEDGDFK GQLTEPCSYA LRGGKYIRPI ILMEIVRACQ LQHSFGAPIY PAEAALAVEY FHVASLIIDD MPSFDNDVKR RNKDTVWARF GVAKAQMSAL ALTMQGFQNI CRQIDWIKEH CPRFPDPNQL GALLCTFVSH SLNSAGSGQL VDTPEKTIPF FKIAFIMGWV LGTGTIEDIG MIERAAHCFG HAFQLADDIK DHDTDTGWNY AKIHGKQKTF DDVAQSLQEC KKILHGKKIF TSIWNEIFQK VINVALGT //