PREA_CYAPA
ID PREA_CYAPA Reviewed; 323 AA.
AC P31171;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Prenyl transferase;
DE EC=2.5.1.-;
GN Name=preA;
OS Cyanophora paradoxa.
OG Plastid; Cyanelle.
OC Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX NCBI_TaxID=2762;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UTEX LB 555 / Pringsheim;
RX PubMed=1711042; DOI=10.1016/s0021-9258(18)99037-x;
RA Michalowski C.B., Loeffelhardt W., Bohnert H.J.;
RT "An ORF323 with homology to crtE, specifying prephytoene pyrophosphate
RT dehydrogenase, is encoded by cyanelle DNA in the eukaryotic alga Cyanophora
RT paradoxa.";
RL J. Biol. Chem. 266:11866-11870(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX LB 555 / Pringsheim;
RA Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J.,
RA Bryant D.A.;
RT "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa.";
RL Plant Mol. Biol. Rep. 13:327-332(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX LB 555 / Pringsheim;
RA Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M.,
RA Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M.,
RA Jakowitsch J., Bohnert H.J., Bryant D.A.;
RT "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the
RT genetic complexity of a primitive plastid.";
RL (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W.
RL (eds.);
RL Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
RC STRAIN=UTEX LB 555 / Pringsheim;
RX PubMed=2126059; DOI=10.1007/bf00271555;
RA Michalowski C.B., Pfanzagl B., Loeffelhardt W., Bohnert H.J.;
RT "The cyanelle S10 spc ribosomal protein gene operon from Cyanophora
RT paradoxa.";
RL Mol. Gen. Genet. 224:222-231(1990).
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, cyanelle.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
CC -!- CAUTION: Was originally called crtE. {ECO:0000305|PubMed:1711042}.
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DR EMBL; M37111; AAA65472.1; -; Genomic_DNA.
DR EMBL; U30821; AAA81217.1; -; Genomic_DNA.
DR EMBL; M30487; AAA63631.1; -; Genomic_DNA.
DR PIR; A40433; A40433.
DR PIR; T06874; T06874.
DR RefSeq; NP_043186.1; NC_001675.1.
DR AlphaFoldDB; P31171; -.
DR SMR; P31171; -.
DR GeneID; 801615; -.
DR GO; GO:0009842; C:cyanelle; 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 Cyanelle; Isoprene biosynthesis; Magnesium; Metal-binding; Photosynthesis;
KW Plastid; Transferase.
FT CHAIN 1..323
FT /note="Prenyl transferase"
FT /id="PRO_0000123998"
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; 35919 MW; CB4802466342B09A CRC64;
MASITNILAP VENELDLLTK NLKKLVGSGH PILSAASEHL FSASGKRPRP AIVLLISKAT
MENEIITSRH RRLAEITEII HTASLVHDDI LDESDVRRGI PTVHSDFGTK IAILAGDFLF
AQSSWYLANL ESLEVVKLIS KVITDFAEGE IRRGLNQFKV DLTLEEYLEK SFYKTASLLA
ASSKAAALLS HVDLTVANDL YNYGRHLGLA FQIVDDILDF TSSTEELGKP SCSDLKKGNL
TAPVLFALEQ NSELIPLIQR QFSEPKDFEY TLQIVEETKA IEKTRELAME HAQVAIQCLE
NLPPSSSKEA LKLITKYVLE RLY
