XGAT4_POPTR
ID XGAT4_POPTR Reviewed; 420 AA.
AC A0A2K1X4I9;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Xyloglucan O-acetyltransferase 4 {ECO:0000303|PubMed:30083810};
DE Short=PtrXGOAT4 {ECO:0000303|PubMed:30083810};
DE EC=2.3.1.- {ECO:0000269|PubMed:30083810};
GN Name=XGOAT4 {ECO:0000303|PubMed:30083810};
GN ORFNames=POPTR_017G073700 {ECO:0000312|EMBL:PNS95700.1};
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=4.15 mM for xyloglucan oligomer {ECO:0000269|PubMed:30083810};
CC Vmax=106.4 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; MH568693; AXN57021.1; -; mRNA.
DR EMBL; CM009306; PNS95700.1; -; Genomic_DNA.
DR SMR; A0A2K1X4I9; -.
DR STRING; 3694.POPTR_0017s11000.1; -.
DR EnsemblPlants; PNS95700; PNS95700; POPTR_017G073700v3.
DR Gramene; PNS95700; PNS95700; POPTR_017G073700v3.
DR OMA; GCAMEKF; -.
DR Proteomes; UP000006729; Chromosome 17.
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..420
FT /note="Xyloglucan O-acetyltransferase 4"
FT /id="PRO_0000453956"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 31..51
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..420
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 151..153
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:30083810"
FT MOTIF 395..398
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:30083810"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 395
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 398
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 78..128
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 99..164
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 108..400
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 323..396
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 420 AA; 48615 MW; 53CACF630F082E9B CRC64;
MTMHEKMKLP SCSCSAFKCG KKDRWLNMER PIPFLLIGLT TILSVFILYT LNPLKFVIEH
NIDQKLLLIK PHKEEDKCDL FNGNWVPDFE GSIYTNSSCA TIPTSKNCFR NGRKDQDFLN
WRWKPERCDL PRFDATAYLD IVRGKTLAFI GDSVARNHIE SLLCLLSQKE VPVDAYLDSE
DRNRIWHFPV HNFTLKMLWT KFLVHGEERV INGSSSGIFD LYLDKVDENW ARDLHSLDYV
VISDAHWFFR QVYLHRGSNV VACVYCNEAN VTDRGVAFAL RMAFRAAFSQ INHCNKCKGI
VTLLRTFSPS HFENGFWNTG GSCNRTSPYN DQKINFGAYE WEIRSMQVEE IERAEKRGKK
GKSFGVLDVT MAMLMRPDGH PGAFWGNQWM KGYNDCVHWC LPGPIDVWND LLLAVLRRLD
