PGT1_LITER
ID PGT1_LITER Reviewed; 307 AA.
AC Q8W405;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=4-hydroxybenzoate geranyltransferase 1;
DE EC=2.5.1.93;
DE AltName: Full=PHB geranyltransferase 1;
DE Short=LePGT1;
GN Name=PGT-1;
OS Lithospermum erythrorhizon (Purple gromwell) (Lithospermum officinale var.
OS erythrorhizon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Boraginales; Boraginaceae; Boraginoideae; Lithospermeae;
OC Lithospermum.
OX NCBI_TaxID=34254;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=11744717; DOI=10.1074/jbc.m106387200;
RA Yazaki K., Kunihisa M., Fujisaki T., Sato F.;
RT "Geranyl diphosphate:4-hydroxybenzoate geranyltransferase from Lithospermum
RT erythrorhizon. Cloning and characterization of a key enzyme in shikonin
RT biosynthesis.";
RL J. Biol. Chem. 277:6240-6246(2002).
RN [2]
RP SUBCELLULAR LOCATION.
RX DOI=10.1016/S0031-9422(00)95147-1;
RA Yamaga Y., Nakanishi K., Fukui H., Tabata M.;
RT "Intracellular localization of p-hydroxybenzoate geranyltransferase, a key
RT enzyme involved in shikonin biosynthesis.";
RL Phytochemistry 32:633-636(1993).
RN [3]
RP INDUCTION BY METHYL JASMONATE, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=9640665; DOI=10.1007/s004250050337;
RA Muehlenweg A., Melzer M., Li S.M., Heide L.;
RT "4-Hydroxybenzoate 3-geranyltransferase from Lithospermum erythrorhizon:
RT purification of a plant membrane-bound prenyltransferase.";
RL Planta 205:407-413(1998).
RN [4]
RP FUNCTION, MUTAGENESIS OF ARG-76; ASN-83; ASP-84; ASP-87; ASP-91; ARG-96;
RP LYS-152; ARG-153; GLN-207; ASP-208; ASP-211; ASP-212; SER-219 AND LYS-229,
RP AND 3D-STRUCTURE MODELING.
RX PubMed=19392660; DOI=10.1042/bj20081968;
RA Ohara K., Muroya A., Fukushima N., Yazaki K.;
RT "Functional characterization of LePGT1, a membrane-bound prenyltransferase
RT involved in the geranylation of p-hydroxybenzoic acid.";
RL Biochem. J. 421:231-241(2009).
CC -!- FUNCTION: Prenyltransferase involved in the biosynthesis of shikonin, a
CC naphthoquinone secondary metabolite. Could accept only geranyl
CC diphosphate and not dimethylallyl diphosphate, farnesyl diphosphate, or
CC geranylgeranyl diphosphate as substrate. {ECO:0000269|PubMed:11744717,
CC ECO:0000269|PubMed:19392660}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + 4-hydroxybenzoate = 3-geranyl-4-
CC hydroxybenzoate + diphosphate; Xref=Rhea:RHEA:27854,
CC ChEBI:CHEBI:17879, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:60878; EC=2.5.1.93;
CC Evidence={ECO:0000269|PubMed:11744717, ECO:0000269|PubMed:9640665};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9640665};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.3 uM for 4-hydroxybenzoate {ECO:0000269|PubMed:11744717};
CC KM=5.1 uM for geranyl diphosphate {ECO:0000269|PubMed:11744717};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed only in roots.
CC {ECO:0000269|PubMed:11744717}.
CC -!- INDUCTION: Up-regulated in the dark and by methyl jasmonate or
CC oligogalacturonide. Down-regulated in the light and by ammonium or 2,4-
CC dichlorophenoxyacetic acid (2,4-D). {ECO:0000269|PubMed:11744717,
CC ECO:0000269|PubMed:9640665}.
CC -!- DOMAIN: The N-terminus (1-130) is determinant for the chain length
CC specificity. Region I (76-96) and region III (201-229) are involved in
CC the recognition of both substrates in a coordinated manner.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB055078; BAB84122.1; -; mRNA.
DR AlphaFoldDB; Q8W405; -.
DR SMR; Q8W405; -.
DR KEGG; ag:BAB84122; -.
DR BRENDA; 2.5.1.93; 3048.
DR SABIO-RK; Q8W405; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0102930; F:4-hydroxybenzoate geranyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004337; F:geranyltranstransferase activity; IMP:CACAO.
DR GO; GO:0002094; F:polyprenyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
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 Endoplasmic reticulum; Magnesium; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..307
FT /note="4-hydroxybenzoate geranyltransferase 1"
FT /id="PRO_0000409380"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 76
FT /note="R->A: Reduces activity 99%, decreases affinity for
FT 4-hydroxybenzoate 4-fold and increases affinity for geranyl
FT diphosphate 4-fold."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 83
FT /note="N->A: Reduces activity 99% and decreases affinity
FT for 4-hydroxybenzoate 21.5-fold."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 83
FT /note="N->D: Reduces activity 93% and no effect on affinity
FT for 4-hydroxybenzoate."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 84
FT /note="D->A: Reduces activity 98%."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 84
FT /note="D->E: Reduces activity 85% and decreases affinity
FT for 4-hydroxybenzoate 3.5-fold and for geranyl diphosphate
FT 6.5-fold."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 84
FT /note="D->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 87
FT /note="D->A,E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 91
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 96
FT /note="R->A,K: Reduces activity 99%."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 152
FT /note="K->A: Reduces activity 99%."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 153
FT /note="R->A: Reduces activity 18%."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 207
FT /note="Q->A: Reduces activity 97%."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 208
FT /note="D->A,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 208
FT /note="D->E: Reduces activity 99%."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 211
FT /note="D->A: Reduces activity 98%."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 212
FT /note="D->A: Reduces activity 99%."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 212
FT /note="D->E: Reduces activity 97%."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 219
FT /note="S->A: Reduces activity 85% and decreases affinity
FT for geranyl diphosphate 5-fold."
FT /evidence="ECO:0000269|PubMed:19392660"
FT MUTAGEN 229
FT /note="K->A: Reduces activity 87% and decreases affinity
FT for geranyl diphosphate 3-fold."
FT /evidence="ECO:0000269|PubMed:19392660"
SQ SEQUENCE 307 AA; 34319 MW; B4AFB0803F050C30 CRC64;
MVSSKQTQLK KGKQPSWIEM YLPKEVRPYA HLARLDKPIG SWLLAWPAFW SVALAADLES
LPKMLAIFGW WAVWIRGAGC TINDYFDRNF DKKVERTKSR PLASGAVSPA QGLWWLAFQL
FIGLGVLYQF NVLTLALAIV HVPFVFAYPL MKRITYWPQA FLGVMISWGA LLGSSALKGS
VVPSIAYPLY ISSFFWTLVY DTIYAHQDKV DDAKAGIKST ALRFGDATKM WISWFGVGCI
AALVIGGLIL NIGLPYYVFV AIATGQLVWQ IFTVDLLSPL DCGKKFVSNQ WFGAIIFTGI
LLGRLFP
