HGGT_HORVU
ID HGGT_HORVU Reviewed; 408 AA.
AC Q7XB14;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Homogentisate geranylgeranyltransferase {ECO:0000303|PubMed:12897790};
DE Short=HGGT {ECO:0000303|PubMed:12897790};
DE EC=2.5.1.116 {ECO:0000269|PubMed:21223386};
DE Flags: Precursor;
GN Name=HGGT {ECO:0000303|PubMed:12897790};
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513 {ECO:0000312|EMBL:AAP43911.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12897790; DOI=10.1038/nbt853;
RA Cahoon E.B., Hall S.E., Ripp K.G., Ganzke T.S., Hitz W.D., Coughlan S.J.;
RT "Metabolic redesign of vitamin E biosynthesis in plants for tocotrienol
RT production and increased antioxidant content.";
RL Nat. Biotechnol. 21:1082-1087(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21223386; DOI=10.1111/j.1365-313x.2010.04417.x;
RA Yang W., Cahoon R.E., Hunter S.C., Zhang C., Han J., Borgschulte T.,
RA Cahoon E.B.;
RT "Vitamin E biosynthesis: functional characterization of the monocot
RT homogentisate geranylgeranyl transferase.";
RL Plant J. 65:206-217(2011).
CC -!- FUNCTION: Involved in the synthesis of tocotrienol (vitamin E).
CC Catalyzes the condensation of homogentisate and geranylgeranyl
CC diphosphate to form 2-methyl-6-geranylgeranylbenzoquinol
CC (PubMed:12897790, PubMed:21223386). Possesses low activity with phytyl
CC diphosphate as substrate (PubMed:21223386).
CC {ECO:0000269|PubMed:12897790, ECO:0000269|PubMed:21223386}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + H(+) + homogentisate
CC = 6-geranylgeranyl-2-methylbenzene-1,4-diol + CO2 + diphosphate;
CC Xref=Rhea:RHEA:38003, ChEBI:CHEBI:15378, ChEBI:CHEBI:16169,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:75411; EC=2.5.1.116;
CC Evidence={ECO:0000269|PubMed:21223386};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 uM for geranylgeranyl diphosphate
CC {ECO:0000269|PubMed:21223386};
CC KM=0.4 uM for phytyl diphosphate {ECO:0000269|PubMed:21223386};
CC Vmax=0.43 pmol/min/mg enzyme toward geranylgeranyl diphosphate
CC {ECO:0000269|PubMed:21223386};
CC Vmax=0.06 pmol/min/mg enzyme toward phytyl diphosphate
CC {ECO:0000269|PubMed:21223386};
CC -!- PATHWAY: Cofactor biosynthesis; tocopherol biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:21223386}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds. {ECO:0000269|PubMed:12897790}.
CC -!- MISCELLANEOUS: Seeds of most monocots are enriched in tocotrienols and
CC contain only small amounts of tocopherols.
CC {ECO:0000303|PubMed:12897790}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY222860; AAP43911.1; -; mRNA.
DR AlphaFoldDB; Q7XB14; -.
DR SMR; Q7XB14; -.
DR EnsemblPlants; HORVU.MOREX.r2.7HG0616750.1; HORVU.MOREX.r2.7HG0616750.1; HORVU.MOREX.r2.7HG0616750.
DR EnsemblPlants; HORVU.MOREX.r2.7HG0616750.1.mrna1; HORVU.MOREX.r2.7HG0616750.1.mrna1; HORVU.MOREX.r2.7HG0616750.1.
DR Gramene; HORVU.MOREX.r2.7HG0616750.1; HORVU.MOREX.r2.7HG0616750.1; HORVU.MOREX.r2.7HG0616750.
DR Gramene; HORVU.MOREX.r2.7HG0616750.1.mrna1; HORVU.MOREX.r2.7HG0616750.1.mrna1; HORVU.MOREX.r2.7HG0616750.1.
DR OMA; LAMACLH; -.
DR BioCyc; MetaCyc:MON-18465; -.
DR BRENDA; 2.5.1.116; 2687.
DR SABIO-RK; Q7XB14; -.
DR UniPathway; UPA00160; -.
DR ExpressionAtlas; Q7XB14; baseline and differential.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102551; F:homogentisate geranylgeranyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:InterPro.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd13960; PT_UbiA_HPT1; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR044502; AtHST-like.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR Pfam; PF01040; UbiA; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Transferase; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..408
FT /note="Homogentisate geranylgeranyltransferase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430738"
FT TRANSMEM 122..142
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
SQ SEQUENCE 408 AA; 45092 MW; 3079CC1FF1E3A8FB CRC64;
MQAVTAAAAA GQLLTDTRRG PRCRARLGTT RLSWTGRFAV EAFAGQCQSS ATTVMHKFSA
ISQAARPRRN TKRQCSDDYP ALQAGCSEVN WDQNGSNANR LEEIRGDVLK KLRSFYEFCR
PHTIFGTIIG ITSVSLLPMK SIDDFTVTVL RGYLEALTAA LCMNIYVVGL NQLYDIQIDK
INKPGLPLAS GEFSVATGVF LVLAFLIMSF SIGIRSGSAP LMCALIVSFL LGSAYSIEAP
FLRWKRHALL AASCILFVRA ILVQLAFFAH MQQHVLKRPL AATKSLVFAT LFMCCFSAVI
ALFKDIPDVD GDRDFGIQSL SVRLGPQRVY QLCISILLTA YGAATLVGAS STNLFQKIIT
VSGHGLLALT LWQRAQHFEV ENQARVTSFY MFIWKLFYAE YFLIPFVQ
