HSTC_CHLRE
ID HSTC_CHLRE Reviewed; 370 AA.
AC A1JHN0; A8J261;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Homogentisate solanesyltransferase, chloroplastic;
DE Short=CrHST;
DE EC=2.5.1.117;
DE AltName: Full=Homogentisate prenyltransferase;
DE Flags: Precursor;
GN Name=HST; Synonyms=VTE2-2;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC STRAIN=21gr / CC-1690;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 71-370.
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP 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: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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16989822};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16989822};
CC -!- ACTIVITY REGULATION: Inhibited by haloxydine (3,5-dichloro-2,6-
CC difluoro-4-haloxypyridine). {ECO:0000269|PubMed:20400515}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40.5 uM for homogentisate (in the presence of 200 uM farnesyl
CC diphosphate) {ECO:0000269|PubMed:16989822,
CC ECO:0000269|PubMed:20400515};
CC KM=25 uM for farnesyl diphosphate (in the presence of 100 uM
CC homogentisate) {ECO:0000269|PubMed:16989822,
CC ECO:0000269|PubMed:20400515};
CC Vmax=84 pmol/min/mg enzyme {ECO:0000269|PubMed:16989822,
CC ECO:0000269|PubMed:20400515};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:16989822,
CC ECO:0000269|PubMed:20400515};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AM285678; CAL01105.1; -; mRNA.
DR EMBL; DS496133; EDP01599.1; -; Genomic_DNA.
DR AlphaFoldDB; A1JHN0; -.
DR STRING; 3055.EDP01599; -.
DR PaxDb; A1JHN0; -.
DR EnsemblPlants; PNW82555; PNW82555; CHLRE_06g283750v5.
DR GeneID; 5720967; -.
DR Gramene; PNW82555; PNW82555; CHLRE_06g283750v5.
DR eggNOG; ENOG502QUHT; Eukaryota.
DR HOGENOM; CLU_048963_2_0_1; -.
DR OMA; LERANYT; -.
DR OrthoDB; 1231215at2759; -.
DR BRENDA; 2.5.1.117; 1318.
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 Chloroplast; Membrane; Plastid; Transferase; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..370
FT /note="Homogentisate solanesyltransferase, chloroplastic"
FT /id="PRO_0000430139"
FT TRANSMEM 117..137
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 39347 MW; 17F6A31BAF076EF8 CRC64;
MDLCSSTGRG ACLSPASTSR PCPAPVHLRG RRLAFSPAQP AGRRHLPVLS SAAVPAPLPN
GGNDESFAQK LANFPNAFWK FLRPHTIRGT ILGTTAVTAK VLMENPGCID WALLPKALLG
LVALLCGNGY IVGINQIYDV DIDVVNKPFL PVASGELSPA LAWGLCLSLA AAGAGIVAAN
FGNLITSLYT FGLFLGTVYS VPPLRLKQYA VPAFMIIATV RGFLLNFGVY SATRAALGLP
FEWSPAVSFI TVFVTLFATV IAITKDLPDV EGDQANNIST FATRMGVRNV ALLAIGLLMA
NYLGAIALAL TYSTAFNVPL MAGAHAILAA TLALRTLKLH AASYSREAVA SFYRWIWNLF
YAEYALLPFL
