HGGT_SYNY3
ID HGGT_SYNY3 Reviewed; 308 AA.
AC P73726;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Homogentisate phytyltransferase {ECO:0000303|PubMed:11706191};
DE Short=HPT {ECO:0000305};
DE EC=2.5.1.115 {ECO:0000269|PubMed:12011362};
GN OrderedLocusNames=slr1736 {ECO:0000312|EMBL:BAA17774.1};
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11418103; DOI=10.1016/s0014-5793(01)02508-x;
RA Schledz M., Seidler A., Beyer P., Neuhaus G.;
RT "A novel phytyltransferase from Synechocystis sp. PCC 6803 involved in
RT tocopherol biosynthesis.";
RL FEBS Lett. 499:15-20(2001).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11706191; DOI=10.1104/pp.010421;
RA Collakova E., DellaPenna D.;
RT "Isolation and functional analysis of homogentisate phytyltransferase from
RT Synechocystis sp. PCC 6803 and Arabidopsis.";
RL Plant Physiol. 127:1113-1124(2001).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=12011362; DOI=10.1104/pp.010747;
RA Savidge B., Weiss J.D., Wong Y.H.H., Lassner M.W., Mitsky T.A.,
RA Shewmaker C.K., Post-Beittenmiller D., Valentin H.E.;
RT "Isolation and characterization of homogentisate phytyltransferase genes
RT from Synechocystis sp. PCC 6803 and Arabidopsis.";
RL Plant Physiol. 129:321-332(2002).
CC -!- FUNCTION: Involved in the synthesis of tocopherol (vitamin E)
CC (PubMed:11418103, PubMed:11706191, PubMed:12011362). Catalyzes the
CC condensation of homogentisate and phytyl diphosphate to form
CC dimethylphytylhydrquinone (PubMed:12011362).
CC {ECO:0000269|PubMed:11418103, ECO:0000269|PubMed:11706191,
CC ECO:0000269|PubMed:12011362}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + homogentisate + phytyl diphosphate = 2-methyl-6-phytyl-
CC 1,4-benzene-1,4-diol + CO2 + diphosphate; Xref=Rhea:RHEA:37975,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16169, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:75434, ChEBI:CHEBI:75920;
CC EC=2.5.1.115; Evidence={ECO:0000269|PubMed:12011362};
CC -!- PATHWAY: Cofactor biosynthesis; tocopherol biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Impaired in biosynthesis of alpha-tocopherol.
CC {ECO:0000269|PubMed:11418103, ECO:0000269|PubMed:11706191,
CC ECO:0000269|PubMed:12011362}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BA000022; BAA17774.1; -; Genomic_DNA.
DR PIR; S74813; S74813.
DR AlphaFoldDB; P73726; -.
DR SMR; P73726; -.
DR STRING; 1148.1652856; -.
DR SwissLipids; SLP:000001496; -.
DR PaxDb; P73726; -.
DR EnsemblBacteria; BAA17774; BAA17774; BAA17774.
DR KEGG; syn:slr1736; -.
DR eggNOG; COG0382; Bacteria.
DR InParanoid; P73726; -.
DR OMA; FYQFIWK; -.
DR PhylomeDB; P73726; -.
DR BioCyc; MetaCyc:MON-13902; -.
DR BRENDA; 2.5.1.115; 382.
DR BRENDA; 2.5.1.116; 382.
DR UniPathway; UPA00160; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010176; F:homogentisate phytyltransferase activity; IEA:RHEA.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IMP:CACAO.
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 Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..308
FT /note="Homogentisate phytyltransferase"
FT /id="PRO_0000430739"
FT TRANSMEM 13..33
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..241
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..263
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
SQ SEQUENCE 308 AA; 34410 MW; D91B3366EEFE4C16 CRC64;
MATIQAFWRF SRPHTIIGTT LSVWAVYLLT ILGDGNSVNS PASLDLVFGA WLACLLGNVY
IVGLNQLWDV DIDRINKPNL PLANGDFSIA QGRWIVGLCG VASLAIAWGL GLWLGLTVGI
SLIIGTAYSV PPVRLKRFSL LAALCILTVR GIVVNLGLFL FFRIGLGYPP TLITPIWVLT
LFILVFTVAI AIFKDVPDME GDRQFKIQTL TLQIGKQNVF RGTLILLTGC YLAMAIWGLW
AAMPLNTAFL IVSHLCLLAL LWWRSRDVHL ESKTEIASFY QFIWKLFFLE YLLYPLALWL
PNFSNTIF
