XGAT1_POPTR
ID XGAT1_POPTR Reviewed; 429 AA.
AC B9HJR7;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Xyloglucan O-acetyltransferase 1 {ECO:0000303|PubMed:30083810};
DE Short=PtrXGOAT1 {ECO:0000303|PubMed:30083810};
DE EC=2.3.1.- {ECO:0000269|PubMed:30083810};
GN Name=XGOAT1 {ECO:0000303|PubMed:30083810};
GN ORFNames=POPTR_008G146100 {ECO:0000312|EMBL:PNT24667.1};
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=9.95 mM for xyloglucan oligomer {ECO:0000269|PubMed:30083810};
CC Vmax=73.5 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; MH568690; AXN57018.1; -; mRNA.
DR EMBL; CM009297; PNT24667.1; -; Genomic_DNA.
DR RefSeq; XP_002312510.1; XM_002312474.2.
DR SMR; B9HJR7; -.
DR STRING; 3694.POPTR_0008s14540.1; -.
DR EnsemblPlants; PNT24667; PNT24667; POPTR_008G146100v3.
DR EnsemblPlants; PNT24669; PNT24669; POPTR_008G146100v3.
DR EnsemblPlants; PNT24670; PNT24670; POPTR_008G146100v3.
DR GeneID; 7457851; -.
DR Gramene; PNT24667; PNT24667; POPTR_008G146100v3.
DR Gramene; PNT24669; PNT24669; POPTR_008G146100v3.
DR Gramene; PNT24670; PNT24670; POPTR_008G146100v3.
DR KEGG; pop:7457851; -.
DR eggNOG; ENOG502QQXW; Eukaryota.
DR HOGENOM; CLU_020953_6_0_1; -.
DR InParanoid; B9HJR7; -.
DR OMA; WMDAEMR; -.
DR Proteomes; UP000006729; Chromosome 8.
DR ExpressionAtlas; B9HJR7; baseline and differential.
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..429
FT /note="Xyloglucan O-acetyltransferase 1"
FT /id="PRO_0000453954"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..429
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 145..147
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:30083810"
FT MOTIF 397..400
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:30083810"
FT ACT_SITE 147
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 397
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 400
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 72..122
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 93..158
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 102..402
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 317..398
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 429 AA; 49207 MW; 43A3C45A1EAD7CFD CRC64;
MGSPFKDHHH HHHPFSLAKK LIPWTFYAMI PLVLFRLYFY PYPLHNITTP ILTSSSSSVS
SSTPFVAEET SCDYTTGKWV RDKRGPLYNG SACGTIKEGQ NCIAHGRPDM GYLYWRWKPK
HCKLPRFEPN TFLQLLRNKH LAFVGDSMAR NQLESLLCML SSASAPNLVY RDGDDNKFRR
WYFESHNINI SVYWSPFLVK GVEKSNTGPN HNQLYLDHVD ERWAADMNGI DMIVLSIGHW
FLHPAVYYEG DQVLGCHYCP GLNHTEIGFY DVLRKAIKTT LKALIDRKGA NSNGINAFVT
TFSPAHFEGD WDKLGACPKT KPYKEGDKAL EGMDADMRQI EVEEVEAAKM NSTQLEKFRL
EALDVTSLSL MRPDGHPGPY MHPFPFANGV TERVQNDCVH WCLPGPIDTW NEILLEVIKK
WDYESRREE
