ID P93668_HORVU Unreviewed; 294 AA.
AC P93668;
DT 01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase {ECO:0000256|RuleBase:RU361120};
DE EC=2.4.1.207 {ECO:0000256|RuleBase:RU361120};
GN Name=EXT {ECO:0000313|EMBL:CAA62847.1};
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513 {ECO:0000313|EMBL:CAA62847.1};
RN [1] {ECO:0000313|EMBL:CAA62847.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:CAA62847.1};
RA Smith R.C., Matthews P.R., Schunmann P.H.D., Chandler P.M.;
RT "The regulation of leaf elongation and xyloglucan endotransglycosylase by
RT gibberellin in "Himalaya" barley (Hordeum vulgare L.).";
RL J. Exp. Bot. 47:1395-1404(1997).
CC -!- FUNCTION: Catalyzes xyloglucan endohydrolysis (XEH) and/or
CC endotransglycosylation (XET). Cleaves and religates xyloglucan
CC polymers, an essential constituent of the primary cell wall, and
CC thereby participates in cell wall construction of growing tissues.
CC {ECO:0000256|RuleBase:RU361120}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000256|RuleBase:RU361120}. Secreted, extracellular space,
CC apoplast {ECO:0000256|RuleBase:RU361120}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000256|RuleBase:RU361120}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC {ECO:0000256|RuleBase:RU361120}.
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DR EMBL; X91659; CAA62847.1; -; mRNA.
DR AlphaFoldDB; P93668; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR GlyCosmos; P93668; 1 site, No reported glycans.
DR EnsemblPlants; HORVU.MOREX.r2.4HG0299490.1; HORVU.MOREX.r2.4HG0299490.1; HORVU.MOREX.r2.4HG0299490.
DR EnsemblPlants; HORVU.MOREX.r2.4HG0299490.1.mrna1; HORVU.MOREX.r2.4HG0299490.1.mrna1; HORVU.MOREX.r2.4HG0299490.1.
DR Gramene; HORVU.MOREX.r2.4HG0299490.1; HORVU.MOREX.r2.4HG0299490.1; HORVU.MOREX.r2.4HG0299490.
DR Gramene; HORVU.MOREX.r2.4HG0299490.1.mrna1; HORVU.MOREX.r2.4HG0299490.1.mrna1; HORVU.MOREX.r2.4HG0299490.1.
DR BRENDA; 2.4.1.207; 2687.
DR ExpressionAtlas; P93668; baseline and differential.
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:SF243; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE-RELATED; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF06955; XET_C; 1.
DR PIRSF; PIRSF005604; XET; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS01034; GH16_1; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 2: Evidence at transcript level;
KW Apoplast {ECO:0000256|RuleBase:RU361120};
KW Cell wall {ECO:0000256|RuleBase:RU361120};
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU361120};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361120};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361120};
KW Secreted {ECO:0000256|RuleBase:RU361120};
KW Signal {ECO:0000256|RuleBase:RU361120};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361120}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU361120"
FT CHAIN 23..294
FT /note="Xyloglucan endotransglucosylase/hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361120"
FT /id="PRO_5005142312"
FT DOMAIN 24..221
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT ACT_SITE 107
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT ACT_SITE 111
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR005604-2"
SQ SEQUENCE 294 AA; 33594 MW; 01F7828FC8F37B25 CRC64;
MKATAGALLA VVATVLLRGI AAAPPRKPVD VPFEKNYVPT WAEDHIHYVN GGREVQLSLD
KTTGTGFQTR GSYLFGHFSM HIKLVGGDSA GTVTAFYLSS QNSEHDEIDF EFLGNRTGQP
YILQTNVFSG GKGDREQRIY LWFDPTKDYH SYSVLWNLYM IAFFVDDTPI RVFKNSKDLG
VRYPFDQPMK LYSSLWNADD WATRGGREKT DWSKAPFVAS YRGFHVDGCE ASAEAKLCAT
QGARWWDQPE FQDLDAAQYR RLAWVRKEHT IYNYCTDRER YAAMSPECKR DRDV
//
