GXM1_ARATH
ID GXM1_ARATH Reviewed; 282 AA.
AC Q6NMK1; O80540;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Glucuronoxylan 4-O-methyltransferase 1;
DE EC=2.1.1.112;
GN Name=GXM1; OrderedLocusNames=At1g09610; ORFNames=F14J9.26 F14J9.29;
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, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23045523; DOI=10.1093/pcp/pcs138;
RA Lee C., Teng Q., Zhong R., Yuan Y., Haghighat M., Ye Z.H.;
RT "Three Arabidopsis DUF579 domain-containing GXM proteins are
RT methyltransferases catalyzing 4-O-methylation of glucuronic acid on
RT xylan.";
RL Plant Cell Physiol. 53:1934-1949(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Shinn P., Chen H., Cheuk R., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=21288268; DOI=10.1111/j.1365-313x.2010.04475.x;
RA Jensen J.K., Kim H., Cocuron J.C., Orler R., Ralph J., Wilkerson C.G.;
RT "The DUF579 domain containing proteins IRX15 and IRX15-L affect xylan
RT synthesis in Arabidopsis.";
RL Plant J. 66:387-400(2011).
RN [7]
RP DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=21251108; DOI=10.1111/j.1365-313x.2011.04501.x;
RA Brown D., Wightman R., Zhang Z., Gomez L.D., Atanassov I., Bukowski J.P.,
RA Tryfona T., McQueen-Mason S.J., Dupree P., Turner S.;
RT "Arabidopsis genes IRREGULAR XYLEM (IRX15) and IRX15L encode DUF579-
RT containing proteins that are essential for normal xylan deposition in the
RT secondary cell wall.";
RL Plant J. 66:401-413(2011).
CC -!- FUNCTION: Methyltransferase catalyzing 4-O-methylation of glucuronic
CC acid side chains on xylan. {ECO:0000269|PubMed:23045523}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glucuronoxylan D-glucuronate + n S-adenosyl-L-methionine =
CC glucuronoxylan 4-O-methyl-D-glucuronate + n H(+) + n S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:20413, Rhea:RHEA-COMP:14499, Rhea:RHEA-
CC COMP:14500, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:140335, ChEBI:CHEBI:140336; EC=2.1.1.112;
CC Evidence={ECO:0000269|PubMed:23045523};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:23045523}; Single-pass membrane protein
CC {ECO:0000269|PubMed:23045523}.
CC -!- TISSUE SPECIFICITY: Expressed in rosette leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:21288268, ECO:0000269|PubMed:23045523}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during secondary cell wall
CC deposition. {ECO:0000269|PubMed:21251108}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due to redundancy with GXM2
CC and GXM3. {ECO:0000269|PubMed:21251108, ECO:0000269|PubMed:23045523}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC33218.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g09600 has been split into 2 genes: At1g09600 and At1g09610.; Evidence={ECO:0000305};
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DR EMBL; JX914594; AFU91592.1; -; mRNA.
DR EMBL; AC003970; AAC33218.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28468.1; -; Genomic_DNA.
DR EMBL; BT010727; AAR20784.1; -; mRNA.
DR EMBL; BT011658; AAS47664.1; -; mRNA.
DR RefSeq; NP_172432.1; NM_100833.2.
DR AlphaFoldDB; Q6NMK1; -.
DR STRING; 3702.AT1G09610.1; -.
DR PaxDb; Q6NMK1; -.
DR PRIDE; Q6NMK1; -.
DR ProteomicsDB; 247277; -.
DR EnsemblPlants; AT1G09610.1; AT1G09610.1; AT1G09610.
DR GeneID; 837488; -.
DR Gramene; AT1G09610.1; AT1G09610.1; AT1G09610.
DR KEGG; ath:AT1G09610; -.
DR Araport; AT1G09610; -.
DR TAIR; locus:2012350; AT1G09610.
DR eggNOG; ENOG502QST5; Eukaryota.
DR HOGENOM; CLU_053427_0_0_1; -.
DR InParanoid; Q6NMK1; -.
DR OMA; DESWIEQ; -.
DR OrthoDB; 1130631at2759; -.
DR PhylomeDB; Q6NMK1; -.
DR PRO; PR:Q6NMK1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NMK1; baseline and differential.
DR Genevisible; Q6NMK1; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030775; F:glucuronoxylan 4-O-methyltransferase activity; IDA:TAIR.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IBA:GO_Central.
DR GO; GO:0045492; P:xylan biosynthetic process; IBA:GO_Central.
DR GO; GO:0045491; P:xylan metabolic process; IMP:TAIR.
DR InterPro; IPR006514; IRX15/IRX15L/IGXM.
DR InterPro; IPR021148; Polysacc_synth_dom.
DR PANTHER; PTHR31444; PTHR31444; 1.
DR Pfam; PF04669; Polysacc_synt_4; 1.
DR TIGRFAMs; TIGR01627; A_thal_3515; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Membrane; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..282
FT /note="Glucuronoxylan 4-O-methyltransferase 1"
FT /id="PRO_0000420837"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 282 AA; 31883 MW; B9147789976A421C CRC64;
MRPKANQNHK LKVLLVFLLA TLILIFIVRS TLTSSQEHQT PQETRSTRCS GACNKLPRSL
AQALIHYSTS VITPQQTLKE IAVSSRVLGK KSPCNFLVFG LGHDSLMWSS LNYGGRTVFL
EEDEAWIKQI KRRFPMLESY HVTYDSKVNQ ADNLIEVGKG PECTAIGDPR YSMCQLALKG
LPAEIYETGW DLIMVDAPTG YYDEAPGRMT AIYTAGMMAR NRKQGGETDV FVHDVNREIE
DKFSKAFLCE GYMKKQEGRL RHFIIPSYRD GSESESNRPF CP
