BQMT_SYNY3
ID BQMT_SYNY3 Reviewed; 318 AA.
AC P74388;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=2-methyl-6-phytyl-1,4-hydroquinone methyltransferase {ECO:0000303|PubMed:11821038};
DE EC=2.1.1.295 {ECO:0000269|PubMed:11821038};
DE AltName: Full=2-methyl-6-phytylbenzoquinone/2-methyl-6-solanyl-1,4-benzoquinone methyltransferase {ECO:0000303|PubMed:11821038};
DE Short=MPBQ/MSBQ methyltransferase {ECO:0000305|PubMed:11821038};
DE Flags: Precursor;
GN OrderedLocusNames=sll0418 {ECO:0000312|EMBL:BAA18485.1};
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 CATALYTIC ACTIVITY.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=11821038; DOI=10.1016/s0014-5793(01)03223-9;
RA Shintani D.K., Cheng Z., DellaPenna D.;
RT "The role of 2-methyl-6-phytylbenzoquinone methyltransferase in determining
RT tocopherol composition in Synechocystis sp. PCC6803.";
RL FEBS Lett. 511:1-5(2002).
CC -!- FUNCTION: Involved in a key methylation step in both tocopherol
CC (vitamin E) and plastoquinone synthesis. Catalyzes the conversion of 2-
CC methyl-6-phytyl-1,4-hydroquinol (MPBQ) to 2,3-dimethyl-6-phytyl-1,4-
CC hydroquinol (DMPQ, a substrate for tocopherol cyclase), and 2-methyl-6-
CC solanyl-1,4-benzoquinol (MSBQ) to plastoquinol.
CC {ECO:0000269|PubMed:11821038}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methyl-6-phytyl-1,4-benzene-1,4-diol + S-adenosyl-L-
CC methionine = 2,3-dimethyl-6-phytylbenzene-1,4-diol + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:37979, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:75920,
CC ChEBI:CHEBI:75921; EC=2.1.1.295;
CC Evidence={ECO:0000269|PubMed:11821038};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol + S-adenosyl-
CC L-methionine = H(+) + plastoquinol-9 + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:37999, ChEBI:CHEBI:15378, ChEBI:CHEBI:28026,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:75402;
CC EC=2.1.1.295; Evidence={ECO:0000269|PubMed:11821038};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-geranylgeranyl-2-methylbenzene-1,4-diol + S-adenosyl-L-
CC methionine = 6-geranylgeranyl-2,3-dimethylbenzene-1,4-diol + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:38007, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:75411,
CC ChEBI:CHEBI:75412; EC=2.1.1.295;
CC Evidence={ECO:0000269|PubMed:11821038};
CC -!- PATHWAY: Cofactor biosynthesis; tocopherol biosynthesis.
CC {ECO:0000303|PubMed:11821038}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. gTMT family. {ECO:0000255|PROSITE-ProRule:PRU00914}.
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DR EMBL; BA000022; BAA18485.1; -; Genomic_DNA.
DR PIR; S76226; S76226.
DR AlphaFoldDB; P74388; -.
DR SMR; P74388; -.
DR IntAct; P74388; 13.
DR STRING; 1148.1653572; -.
DR PaxDb; P74388; -.
DR EnsemblBacteria; BAA18485; BAA18485; BAA18485.
DR KEGG; syn:sll0418; -.
DR eggNOG; COG2226; Bacteria.
DR InParanoid; P74388; -.
DR OMA; LLDQWSH; -.
DR PhylomeDB; P74388; -.
DR BioCyc; MetaCyc:MON-13899; -.
DR UniPathway; UPA00160; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0102550; F:2-methyl-6-geranylgeranyl-1,4-benzoquinol methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0051741; F:2-methyl-6-phytyl-1,4-benzoquinone methyltransferase activity; IMP:CACAO.
DR GO; GO:0051742; F:2-methyl-6-solanyl-1,4-benzoquinone methyltransferase activity; IEA:RHEA.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR025774; MTs_g-TMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51581; SAM_GTMT; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine; Signal;
KW Transferase.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..318
FT /note="2-methyl-6-phytyl-1,4-hydroquinone
FT methyltransferase"
FT /id="PRO_0000431257"
FT REGION 97..106
FT /note="SAM motif I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00914"
FT REGION 157..165
FT /note="SAM motif II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00914"
FT REGION 184..193
FT /note="SAM motif III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00914"
SQ SEQUENCE 318 AA; 34947 MW; 3E788118B3C0EFF0 CRC64;
MPEYLLLPAG LISLSLAIAA GLYLLTARGY QSSDSVANAY DQWTEDGILE YYWGDHIHLG
HYGDPPVAKD FIQSKIDFVH AMAQWGGLDT LPPGTTVLDV GCGIGGSSRI LAKDYGFNVT
GITISPQQVK RATELTPPDV TAKFAVDDAM ALSFPDGSFD VVWSVEAGPH MPDKAVFAKE
LLRVVKPGGI LVVADWNQRD DRQVPLNFWE KPVMRQLLDQ WSHPAFASIE GFAENLEATG
LVEGQVTTAD WTVPTLPAWL DTIWQGIIRP QGWLQYGIRG FIKSVREVPT ILLMRLAFGV
GLCRFGMFKA VRKNATQA
