HSTC_ARATH
ID HSTC_ARATH Reviewed; 386 AA.
AC Q1ACB3; Q9LHM7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Homogentisate solanesyltransferase, chloroplastic;
DE Short=AtHST;
DE EC=2.5.1.117;
DE AltName: Full=Homogentisate phytyltransferase 2;
DE Short=AtHPT2;
DE AltName: Full=Vitamin E pathway gene 2-2 protein;
DE Short=AtVTE2-2;
DE Flags: Precursor;
GN Name=HST; Synonyms=HPT2, VTE2-2; OrderedLocusNames=At3g11945;
GN ORFNames=MEC18;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=16408209; DOI=10.1007/s00425-005-0180-1;
RA Venkatesh T.V., Karunanandaa B., Free D.L., Rottnek J.M., Baszis S.R.,
RA Valentin H.E.;
RT "Identification and characterization of an Arabidopsis homogentisate
RT phytyltransferase paralog.";
RL Planta 223:1134-1144(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF 148-VAL-GLY-149, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=17569077; DOI=10.1007/s00425-007-0564-5;
RA Tian L., DellaPenna D., Dixon R.A.;
RT "The pds2 mutation is a lesion in the Arabidopsis homogentisate
RT solanesyltransferase gene involved in plastoquinone biosynthesis.";
RL Planta 226:1067-1073(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16989822; DOI=10.1016/j.febslet.2006.09.002;
RA Sadre R., Gruber J., Frentzen M.;
RT "Characterization of homogentisate prenyltransferases involved in
RT plastoquinone-9 and tocochromanol biosynthesis.";
RL FEBS Lett. 580:5357-5362(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=20400515; DOI=10.1074/jbc.m110.117929;
RA Sadre R., Frentzen M., Saeed M., Hawkes T.;
RT "Catalytic reactions of the homogentisate prenyl transferase involved in
RT plastoquinone-9 biosynthesis.";
RL J. Biol. Chem. 285:18191-18198(2010).
CC -!- FUNCTION: Involved in the synthesis of plastoquinone-9. Can use both
CC homogentisic acid and 2,5-dihydroxyphenylacetic acid gamma-lactone as
CC prenyl acceptors, and solanesyl diphosphate > farnesyl diphosphate >
CC geranylgeranyl diphosphate >> phytyl diphosphate as prenyl donors. Do
CC not catalyze the decardoxylation of homogentisate uncoupled from
CC prenylation. {ECO:0000269|PubMed:16408209, ECO:0000269|PubMed:16989822,
CC ECO:0000269|PubMed:20400515}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-nonaprenyl diphosphate + H(+) + homogentisate = 2-
CC methyl-6-all-trans-nonaprenylbenzene-1,4-diol + CO2 + diphosphate;
CC Xref=Rhea:RHEA:37995, ChEBI:CHEBI:15378, ChEBI:CHEBI:16169,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:58391,
CC ChEBI:CHEBI:75402; EC=2.5.1.117;
CC Evidence={ECO:0000269|PubMed:16989822, ECO:0000269|PubMed:20400515};
CC -!- ACTIVITY REGULATION: Inhibited by haloxydine (3,5-dichloro-2,6-
CC difluoro-4-haloxypyridine). {ECO:0000269|PubMed:20400515}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:17569077}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17569077}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q1ACB3-1; Sequence=Displayed;
CC -!- MISCELLANEOUS: Seeds overexpressing HST accumulate increased levels of
CC tocopherol. {ECO:0000305|PubMed:16408209}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was initially thought to have a homogentisate
CC phytyltransferase activity and to be involved in tocopherol
CC biosynthesis. {ECO:0000305|PubMed:16408209}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB03104.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ231060; ABB70127.1; -; mRNA.
DR EMBL; AP002040; BAB03104.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75125.1; -; Genomic_DNA.
DR RefSeq; NP_001078138.1; NM_001084669.2. [Q1ACB3-1]
DR AlphaFoldDB; Q1ACB3; -.
DR SMR; Q1ACB3; -.
DR STRING; 3702.AT3G11945.2; -.
DR SwissPalm; Q1ACB3; -.
DR PRIDE; Q1ACB3; -.
DR ProteomicsDB; 230218; -. [Q1ACB3-1]
DR EnsemblPlants; AT3G11945.1; AT3G11945.1; AT3G11945. [Q1ACB3-1]
DR GeneID; 5007993; -.
DR Gramene; AT3G11945.1; AT3G11945.1; AT3G11945. [Q1ACB3-1]
DR KEGG; ath:AT3G11945; -.
DR Araport; AT3G11945; -.
DR eggNOG; ENOG502QUHT; Eukaryota.
DR HOGENOM; CLU_048963_2_0_1; -.
DR InParanoid; Q1ACB3; -.
DR OMA; LERANYT; -.
DR PhylomeDB; Q1ACB3; -.
DR BRENDA; 2.5.1.115; 399.
DR BRENDA; 2.5.1.117; 399.
DR PRO; PR:Q1ACB3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q1ACB3; baseline and differential.
DR Genevisible; Q1ACB3; AT.
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:0102661; F:homogentisate solanyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:InterPro.
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 Alternative splicing; Chloroplast; Membrane; Plastid; Reference proteome;
KW Transferase; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..69
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 70..386
FT /note="Homogentisate solanesyltransferase, chloroplastic"
FT /id="PRO_0000409869"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 148..149
FT /note="Missing: In pds2; albino phenotype."
FT /evidence="ECO:0000269|PubMed:17569077"
SQ SEQUENCE 386 AA; 42841 MW; 54D13052FE67F277 CRC64;
MELSISQSPR VRFSSLAPRF LAASHHHRPS VHLAGKFISL PRDVRFTSLS TSRMRSKFVS
TNYRKISIRA CSQVGAAESD DPVLDRIARF QNACWRFLRP HTIRGTALGS TALVTRALIE
NTHLIKWSLV LKALSGLLAL ICGNGYIVGI NQIYDIGIDK VNKPYLPIAA GDLSVQSAWL
LVIFFAIAGL LVVGFNFGPF ITSLYSLGLF LGTIYSVPPL RMKRFPVAAF LIIATVRGFL
LNFGVYHATR AALGLPFQWS APVAFITSFV TLFALVIAIT KDLPDVEGDR KFQISTLATK
LGVRNIAFLG SGLLLVNYVS AISLAFYMPQ VFRGSLMIPA HVILASGLIF QTWVLEKANY
TKEAISGYYR FIWNLFYAEY LLFPFL
