XTH_WHEAT
ID XTH_WHEAT Reviewed; 293 AA.
AC Q41542;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase;
DE EC=2.4.1.207;
DE Flags: Precursor;
GN Name=XTH; Synonyms=EXT;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8244968; DOI=10.1016/s0021-9258(19)74400-7;
RA Okazawa K., Sato Y., Nakagawa T., Asada K., Kato I., Tomita E.,
RA Nishitani K.;
RT "Molecular cloning and cDNA sequencing of endoxyloglucan transferase, a
RT novel class of glycosyltransferase that mediates molecular grafting between
RT matrix polysaccharides in plant cell walls.";
RL J. Biol. Chem. 268:25364-25368(1993).
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 (By
CC similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC extracellular space, apoplast {ECO:0000305}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 1
CC subfamily. {ECO:0000305}.
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DR EMBL; D16457; BAA03924.1; -; mRNA.
DR PIR; E49539; E49539.
DR AlphaFoldDB; Q41542; -.
DR SMR; Q41542; -.
DR STRING; 4565.Traes_4DS_6B94D4FA6.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PRIDE; Q41542; -.
DR eggNOG; ENOG502QQUC; Eukaryota.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q41542; baseline.
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:0030247; F:polysaccharide binding; ISS:UniProtKB.
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 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; PTHR31062; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF06955; XET_C; 1.
DR PIRSF; PIRSF005604; XET; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS01034; GH16_1; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 2: Evidence at transcript level;
KW Apoplast; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..293
FT /note="Probable xyloglucan endotransglucosylase/hydrolase"
FT /id="PRO_0000011841"
FT DOMAIN 23..220
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 110
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 110
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 123..125
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 133..135
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 199..200
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 204
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 279
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 108
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 228..237
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 274..287
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 293 AA; 33422 MW; FF21C732308DB446 CRC64;
MKATAGALLA VVAAVLLRGV AAAPRKPVDV PFDKNYVPTW AQDHIHYVNG GREVQLSLDK
TTGTGFQTRG SYLFGHFSMH IKLVGGDSAG TVTAFYLSSQ NSEHDEIDFE FLGNRTGQPY
ILQTNVFSGG KGDREQRIYL WFDPTKDYHS YSVLWNLYMI AFFVDDTPIR VFKNSKDLGV
RYPFDQPMKL YSSLWNADDW ATRGGREKTD WSKAPFVASY RGFHVDGCEA SAEAKFCATQ
GARWWDQPEF QDLDAAQYRR LAWVRKEHTI YNYCTDHDRY AAMAPECKRD RDV
