ID   PREA_CYACA              Reviewed;         323 AA.
AC   Q9TLS1;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Prenyl transferase;
DE            EC=2.5.1.-;
GN   Name=preA;
OS   Cyanidium caldarium (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK-1;
RX   PubMed=11040290; DOI=10.1007/s002390010101;
RA   Gloeckner G., Rosenthal A., Valentin K.-U.;
RT   "The structure and gene repertoire of an ancient red algal plastid
RT   genome.";
RL   J. Mol. Evol. 51:382-390(2000).
CC   -!- FUNCTION: Possible role in synthesis of the nonaprenyl side chain of
CC       plastoquinone or in synthesis of other prenyl chains such as
CC       undekaprenyl pyrophosphate.
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; AF022186; AAF12896.1; -; Genomic_DNA.
DR   RefSeq; NP_045198.1; NC_001840.1.
DR   AlphaFoldDB; Q9TLS1; -.
DR   SMR; Q9TLS1; -.
DR   GeneID; 800126; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Isoprene biosynthesis; Magnesium; Metal-binding;
KW   Photosynthesis; Plastid; Transferase.
FT   CHAIN           1..323
FT                   /note="Prenyl transferase"
FT                   /id="PRO_0000123999"
FT   BINDING         46
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         49
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         81
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         92
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         92
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         97
FT                   /ligand="an all-trans-polyprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58914"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         174
FT                   /ligand="an all-trans-polyprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58914"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="an all-trans-polyprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58914"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="an all-trans-polyprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58914"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   323 AA;  36053 MW;  C9E7F23CBED3FC47 CRC64;
     MKVNSKTLQS VKEDLLNIEQ TLNKLIKVNN PILSAAAKHL LIVESKKIRP AIVLLVAKAI
     DKNKKIKTSQ QRLAEVTEII HTATLLHDDV VDESIIRRGT KSVNKTFGNK IAVFAGDFLF
     AQSSWYLANI NNLEVVKAIS KVITDLAEGE LQQNLTQFNT YYSIIKYLEK SFNKTASLIA
     ASCKSCCLLS DFDQSLNSKF YNYGKNLGLA FQIIDDILDI TSSSTALGKM TTSDLKLGNL
     TAPVLFALTK NSKLFKIIER EFCEKSDISE AINIIKETNA IEESFDLAYE HIEAAINSIK
     DLPTSSEKDS LIEIAYDLLN RYK