XGAT3_POPTR
ID XGAT3_POPTR Reviewed; 397 AA.
AC A0A2K1YKA4; A0A346FH64;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 2.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Xyloglucan O-acetyltransferase 3 {ECO:0000303|PubMed:30083810};
DE Short=PtrXGOAT3 {ECO:0000303|PubMed:30083810};
DE EC=2.3.1.- {ECO:0000269|PubMed:30083810};
GN Name=XGOAT3 {ECO:0000303|PubMed:30083810};
GN ORFNames=POPTR_011G144100 {ECO:0000312|EMBL:PNT13461.2};
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=2.48 mM for xyloglucan oligomer {ECO:0000269|PubMed:30083810};
CC Vmax=23.1 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; MH568692; AXN57020.1; -; mRNA.
DR EMBL; CM009300; PNT13461.2; -; Genomic_DNA.
DR RefSeq; XP_002317022.2; XM_002316986.2.
DR SMR; A0A2K1YKA4; -.
DR STRING; 3694.POPTR_0011s14730.1; -.
DR EnsemblPlants; PNT13461; PNT13461; POPTR_011G144100v3.
DR GeneID; 7454989; -.
DR Gramene; PNT13461; PNT13461; POPTR_011G144100v3.
DR KEGG; pop:7454989; -.
DR Proteomes; UP000006729; Chromosome 11.
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..397
FT /note="Xyloglucan O-acetyltransferase 3"
FT /id="PRO_5024196589"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..397
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 121..123
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:30083810"
FT MOTIF 365..368
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:30083810"
FT ACT_SITE 123
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 365
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 368
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 48..98
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 69..134
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 78..370
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 293..366
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 397 AA; 46209 MW; E314C4F254007ECA CRC64;
MNRFFYTVGL IFLFSFFILY SPKTSDLSNN VDLHQQLLIS LQKEEERCDL FSGYWVQDLR
GSQYTNVSCS SIPESKNCFM QGRPDAGFSQ WRWKPDGCEL PRFDPGTFFE IVRGKTMAFI
GDSVARNHVE SLLCLLSSEE MPLGIYKDTE DRTRTWYFPH SNFTLMVIWT RFLVLDEERV
INGSVTGVFD LHLDKMDKNW ANKLPEIDYA ILSDAHWFFR KNYLYEKGKN IGCIFCGEPG
IKSLDIDSAL QMVIKVVLNY INNCKKCRNI LTVLRTFSPA HFADGAWDTG GSCNRTHPLG
EKEIDLASLD WKIRSIQVEE IKRVRPVARR RKKFEVLDVT KAMLMRPDGH PNSYWGNKWM
KGYNDCVHWC MPGPIDAWND FLIALLRRHA FTDFTWS
