XGAT2_POPTR
ID XGAT2_POPTR Reviewed; 425 AA.
AC B9HVC2;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Xyloglucan O-acetyltransferase 2 {ECO:0000303|PubMed:30083810};
DE Short=PtrXGOAT2 {ECO:0000303|PubMed:30083810};
DE EC=2.3.1.- {ECO:0000269|PubMed:30083810};
GN Name=XGOAT2 {ECO:0000303|PubMed:30083810};
GN ORFNames=POPTR_010G095700 {ECO:0000312|EMBL:PNT15635.1};
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=30083810; DOI=10.1007/s00425-018-2972-0;
RA Zhong R., Cui D., Ye Z.H.;
RT "Xyloglucan O-acetyltransferases from Arabidopsis thaliana and Populus
RT trichocarpa catalyze acetylation of fucosylated galactose residues on
RT xyloglucan side chains.";
RL Planta 248:1159-1171(2018).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually;
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S.,
RA Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J.,
RA Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y.,
RA Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.S.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
CC -!- FUNCTION: Xyloglucan acetyltransferase that catalyzes the acetylation
CC of fucosylated Gal residues on xyloglucan side chains
CC (PubMed:30083810). Predominantly catalyze 6-O-monoacetylation of Gal
CC residues in the Fuc-Gal-Xyl trisaccharide side chains of xyloglucan
CC oligomers (PubMed:30083810). {ECO:0000269|PubMed:30083810}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.24 mM for xyloglucan oligomer {ECO:0000269|PubMed:30083810};
CC Vmax=60 pmol/min/mg enzyme with xyloglucan oligomer as substrate
CC {ECO:0000269|PubMed:30083810};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
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DR EMBL; MH568691; AXN57019.1; -; mRNA.
DR EMBL; CM009299; PNT15635.1; -; Genomic_DNA.
DR RefSeq; XP_002314730.1; XM_002314694.2.
DR SMR; B9HVC2; -.
DR STRING; 3694.POPTR_0010s10570.1; -.
DR EnsemblPlants; PNT15635; PNT15635; POPTR_010G095700v3.
DR GeneID; 7459060; -.
DR Gramene; PNT15635; PNT15635; POPTR_010G095700v3.
DR KEGG; pop:7459060; -.
DR eggNOG; ENOG502QQXW; Eukaryota.
DR HOGENOM; CLU_020953_6_0_1; -.
DR InParanoid; B9HVC2; -.
DR OMA; ERWMSEL; -.
DR Proteomes; UP000006729; Chromosome 10.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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:0016413; F:O-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:1990538; F:xylan O-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:1990937; P:xylan acetylation; IDA:UniProtKB.
DR InterPro; IPR026057; PC-Esterase.
DR InterPro; IPR029962; TBL.
DR InterPro; IPR025846; TBL_N.
DR PANTHER; PTHR32285; PTHR32285; 1.
DR Pfam; PF13839; PC-Esterase; 1.
DR Pfam; PF14416; PMR5N; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..425
FT /note="Xyloglucan O-acetyltransferase 2"
FT /id="PRO_0000453955"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..425
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 141..143
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:30083810"
FT MOTIF 393..396
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:30083810"
FT ACT_SITE 143
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 393
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 396
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 68..118
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 89..154
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 98..398
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 313..394
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 425 AA; 48943 MW; DCA8673228BF96ED CRC64;
MGSPFKDHHT LHPSLVRKLI PWTFYAMVPL VLFRVYLYPY PLHHTTTTIL TSSPVSPPPA
LLEDETSCDY TDGNWVPDRR DPLYNGSTCG TIKEGQSCIA HGRPDMGYLY WRWKPKQCKL
PRFEPNTFLQ LLRNKHLAFV GDSMARNQLE SLLCMLSSVS PPNLVYRDGE ENKFRRWYFE
SHNFSISVYW SPFLVRGVEK SNTGLNHNQL FLDHVDERWA ADMNGIDMVV LSIGHWFLHP
AVYYEGDQVL GCHYCPDLNH TEIGFYDILR KAIKTTLKAL VDRKGPNDNG FDALVTTFSP
AHFEGDWDKL GACPKTEPCK EGEKTLEGMD AEMRQVEVEE VEAAKMNSVQ LEKFRLEALD
VSKLSLMRPD GHPGPYMHPF PFAYGVAERV QNDCVHWCLP GPIDTWNEIL LEVIKKWEYA
SRREQ
