ID A0A059CJZ9_EUCGR Unreviewed; 433 AA.
AC A0A059CJZ9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=xyloglucan:xyloglucosyl transferase {ECO:0000256|ARBA:ARBA00012152};
DE EC=2.4.1.207 {ECO:0000256|ARBA:ARBA00012152};
GN ORFNames=EUGRSUZ_C00176 {ECO:0000313|EMBL:KCW78732.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW78732.1};
RN [1] {ECO:0000313|EMBL:KCW78732.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW78732.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and
CC transfers the xyloglucanyl segment on to O-4 of the non-reducing
CC terminal glucose residue of an acceptor, which can be a xyloglucan or
CC an oligosaccharide of xyloglucan.; EC=2.4.1.207;
CC Evidence={ECO:0000256|ARBA:ARBA00034022};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000256|ARBA:ARBA00004191}. Secreted, extracellular space,
CC apoplast {ECO:0000256|ARBA:ARBA00004271}.
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DR EMBL; KK198755; KCW78732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059CJZ9; -.
DR STRING; 71139.A0A059CJZ9; -.
DR EnsemblPlants; KCW78732; KCW78732; EUGRSUZ_C00176.
DR Gramene; KCW78732; KCW78732; EUGRSUZ_C00176.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR InParanoid; A0A059CJZ9; -.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016762; F:xyloglucan:xyloglucosyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0010411; P:xyloglucan metabolic process; IEA:InterPro.
DR CDD; cd02176; GH16_XET; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR044791; Beta-glucanase/XTH.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR008263; GH16_AS.
DR InterPro; IPR010713; XET_C.
DR InterPro; IPR016455; XTH.
DR PANTHER; PTHR31062; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 8-RELATED; 1.
DR PANTHER; PTHR31062:SF303; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 25-RELATED; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF06955; XET_C; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS01034; GH16_1; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 4: Predicted;
KW Apoplast {ECO:0000256|ARBA:ARBA00022523};
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 166..360
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
SQ SEQUENCE 433 AA; 48435 MW; 8EE8F75060A2001F CRC64;
MEVEPGAALT GKSVVEEELA IHQLSVNKEF WEKQRPLTVK HVAGGEQTIK LVSVWGSFVS
SRTASLHNFF AWWMWVGNVA SCPLLFENIF ILEANCPQPS CNTNRHFSLP STVFTLNSSH
WHLHLFSNYS SSSNRKQNAP NMASRSTSSL CTAALLLIMV VSWATSASAR NFYQDFDITW
GDGRAQILNN GDLLTLSLDK ASGSGFQSKN EYLFGKIDMQ LKLVPGNSAG TVTAYYLSSN
GSTWDEIDFE FLGNLSGDPY ILHTNVFSQG KGNREQQFYL WFDPTADFHT YSILWNPQRI
IFSVDGTPIR EFKNAESIGV PFPKAQPMRI FSSLWNADDW ATRGGLVKTD WTQAPFTASY
RNFNADNACV WSSGSSSCTS SSSSSDGNAW LSEELDSTSQ ERLKWVQSNY MIYNYCSDAK
RFPQGFPPEC TMS
//
