PLQA_SYNY3
ID PLQA_SYNY3 Reviewed; 292 AA.
AC Q55500;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=4-hydroxybenzoate solanesyltransferase {ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000303|PubMed:22166075};
DE EC=2.5.1.39 {ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000305|PubMed:22166075};
DE AltName: Full=4-HB polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01635};
GN Name=plqA {ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000303|PubMed:22166075};
GN OrderedLocusNames=slr0926 {ECO:0000312|EMBL:BAA10850.1};
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22166075; DOI=10.1042/bj20111796;
RA Sadre R., Pfaff C., Buchkremer S.;
RT "Plastoquinone-9 biosynthesis in cyanobacteria differs from that in plants
RT and involves a novel 4-hydroxybenzoate solanesyltransferase.";
RL Biochem. J. 442:621-629(2012).
CC -!- FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with
CC an all-trans polyprenyl group. Mediates the second step in the final
CC reaction sequence of plastoquinone-9 (PQ-9) biosynthesis, which is the
CC condensation of the polyisoprenoid side chain with PHB, generating the
CC first membrane-bound Q intermediate 4-hydroxy-3-solanesylbenzoate.
CC {ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000269|PubMed:22166075}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + all-trans-nonaprenyl diphosphate = 4-
CC hydroxy-3-all-trans-nonaprenylbenzoate + diphosphate;
CC Xref=Rhea:RHEA:17709, ChEBI:CHEBI:17879, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58391, ChEBI:CHEBI:84502; EC=2.5.1.39;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01635,
CC ECO:0000269|PubMed:22166075};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01635,
CC ECO:0000269|PubMed:22166075};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.3 uM for 4-hydroxybenzoate {ECO:0000269|PubMed:22166075};
CC KM=11.8 uM for geranylgeranyl diphosphate
CC {ECO:0000269|PubMed:22166075};
CC KM=18.1 uM for farnesyl diphosphate {ECO:0000269|PubMed:22166075};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01635, ECO:0000269|PubMed:22166075}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01635}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01635}.
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DR EMBL; BA000022; BAA10850.1; -; Genomic_DNA.
DR PIR; S76003; S76003.
DR AlphaFoldDB; Q55500; -.
DR SMR; Q55500; -.
DR STRING; 1148.1001363; -.
DR PaxDb; Q55500; -.
DR EnsemblBacteria; BAA10850; BAA10850; BAA10850.
DR KEGG; syn:slr0926; -.
DR eggNOG; COG0382; Bacteria.
DR InParanoid; Q55500; -.
DR OMA; MVVYPYG; -.
DR PhylomeDB; Q55500; -.
DR BioCyc; MetaCyc:MON-17095; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002083; F:4-hydroxybenzoate decaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047293; F:4-hydroxybenzoate nonaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IBA:GO_Central.
DR GO; GO:0010236; P:plastoquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR HAMAP; MF_01635; UbiA; 1.
DR InterPro; IPR006370; HB_polyprenyltransferase-like.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
DR TIGRFAMs; TIGR01474; ubiA_proteo; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Magnesium; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..292
FT /note="4-hydroxybenzoate solanesyltransferase"
FT /id="PRO_0000432822"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
SQ SEQUENCE 292 AA; 31646 MW; E6B02BF58D5DE0BF CRC64;
MVAQTPSSPP LWLTIIYLLR WHKPAGRLIL MIPALWAVCL AAQGLPPLPL LGTIALGTLA
TSGLGCVVND LWDRDIDPQV ERTKQRPLAA RALSVQVGIG VALVALLCAA GLAFYLTPLS
FWLCVAAVPV IVAYPGAKRV FPVPQLVLSI AWGFAVLISW SAVTGDLTDA TWVLWGATVF
WTLGFDTVYA MADREDDRRI GVNSSALFFG QYVGEAVGIF FALTIGCLFY LGMILMLNPL
YWLSLAIAIV GWVIQYIQLS APTPEPKLYG QIFGQNVIIG FVLLAGMLLG WL
