HGGT_WHEAT
ID HGGT_WHEAT Reviewed; 408 AA.
AC Q7XB13;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Homogentisate geranylgeranyltransferase {ECO:0000303|PubMed:12897790};
DE Short=HGGT {ECO:0000303|PubMed:12897790};
DE EC=2.5.1.116 {ECO:0000250|UniProtKB:Q7XB14};
DE Flags: Precursor;
GN Name=HGGT {ECO:0000303|PubMed:12897790};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000312|EMBL:AAP43912.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kernel {ECO:0000312|EMBL:AAP43912.1};
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).
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. Possesses low
CC activity with phytyl diphosphate as substrate.
CC {ECO:0000250|UniProtKB:Q7XB14}.
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:0000250|UniProtKB:Q7XB14};
CC -!- PATHWAY: Cofactor biosynthesis; tocopherol biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000250|UniProtKB:Q7XB14}; Multi-pass membrane protein
CC {ECO:0000255}.
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; AY222861; AAP43912.1; -; mRNA.
DR AlphaFoldDB; Q7XB13; -.
DR SMR; Q7XB13; -.
DR STRING; 4565.Traes_7AL_3B0FC6F2A.1; -.
DR PRIDE; Q7XB13; -.
DR EnsemblPlants; TraesCAD_scaffold_097383_01G000300.1; TraesCAD_scaffold_097383_01G000300.1; TraesCAD_scaffold_097383_01G000300.
DR EnsemblPlants; TraesCS7A02G510700.1; TraesCS7A02G510700.1; TraesCS7A02G510700.
DR EnsemblPlants; TraesPAR_scaffold_119489_01G000300.1; TraesPAR_scaffold_119489_01G000300.1; TraesPAR_scaffold_119489_01G000300.
DR EnsemblPlants; TraesROB_scaffold_024134_01G000300.1; TraesROB_scaffold_024134_01G000300.1; TraesROB_scaffold_024134_01G000300.
DR EnsemblPlants; TraesWEE_scaffold_060322_01G000100.1; TraesWEE_scaffold_060322_01G000100.1; TraesWEE_scaffold_060322_01G000100.
DR Gramene; TraesCAD_scaffold_097383_01G000300.1; TraesCAD_scaffold_097383_01G000300.1; TraesCAD_scaffold_097383_01G000300.
DR Gramene; TraesCS7A02G510700.1; TraesCS7A02G510700.1; TraesCS7A02G510700.
DR Gramene; TraesPAR_scaffold_119489_01G000300.1; TraesPAR_scaffold_119489_01G000300.1; TraesPAR_scaffold_119489_01G000300.
DR Gramene; TraesROB_scaffold_024134_01G000300.1; TraesROB_scaffold_024134_01G000300.1; TraesROB_scaffold_024134_01G000300.
DR Gramene; TraesWEE_scaffold_060322_01G000100.1; TraesWEE_scaffold_060322_01G000100.1; TraesWEE_scaffold_060322_01G000100.
DR eggNOG; ENOG502QZ7Z; Eukaryota.
DR OMA; CRPHTVI; -.
DR UniPathway; UPA00160; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q7XB13; 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 2: Evidence at transcript level;
KW Chloroplast; Membrane; Plastid; Reference proteome; Transferase;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..68
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 69..408
FT /note="Homogentisate geranylgeranyltransferase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430737"
FT TRANSMEM 122..142
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
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; 45138 MW; 21B8983BAE491A6C CRC64;
MQATTAAAAA QLLTDTRRGP RCSRARLGAT RLSWPGRFAV EAFAGRCQSS ATTVTHRFSA
ISQATSPRRK ARRQCSDDQS ALQAGCSKVN RDQHGYDVNW FEEISQEVSK KLRAFYQFCR
PHTIFGTIIG ITSVSLLPMK SIDDFTATVL KGYLEALAAA LCMNIYVVGL NQLYDIQIDK
INKPGLPLAA GEFSVATGVF LVVTFLIMSF SIGIHSGSVP LMYALVVSFL LGSAYSIEAP
LLRWKRHALL AASCILFVRA ILVQLAFFAH MQQHVLKRPL AATKSLVFAT LFMCCFSAVI
ALFKDIPDVD GDRDFGIQSL SVRLGPQRVY QLCISILLTA YLAATVVGAS STHLLQKIIT
VSGHGLLALT LWQRARHLEV ENQARVTSFY MFIWKLFYAE YFLIPFVQ
