XTH_TOBAC
ID XTH_TOBAC Reviewed; 295 AA.
AC P93349;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase protein;
DE EC=2.4.1.207;
DE Flags: Precursor;
GN Name=XTH; Synonyms=EXGT;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nishitani K., Okazawa K., Takeda S., Asada K., Kato I.;
RT "Endo-xyloglucan transferase (EXGT).";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=11266580; DOI=10.1093/pcp/pce034;
RA Yokoyama R., Nishitani K.;
RT "Endoxyloglucan transferase is localized both in the cell plate and in the
RT secretory pathway destined for the apoplast in tobacco cells.";
RL Plant Cell Physiol. 42:292-300(2001).
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 -!- 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
CC {ECO:0000269|PubMed:11266580}. Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:11266580}.
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; D86730; BAA13163.1; -; mRNA.
DR RefSeq; NP_001312331.1; NM_001325402.1.
DR AlphaFoldDB; P93349; -.
DR SMR; P93349; -.
DR STRING; 4097.P93349; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR GeneID; 107785465; -.
DR KEGG; nta:107785465; -.
DR OMA; ASWGADH; -.
DR PhylomeDB; P93349; -.
DR BRENDA; 2.4.1.207; 3645.
DR Proteomes; UP000084051; Unplaced.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..295
FT /note="Probable xyloglucan endotransglucosylase/hydrolase
FT protein"
FT /id="PRO_0000011840"
FT DOMAIN 22..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 281
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..239
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 276..289
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 295 AA; 33882 MW; D379980DC2DA1765 CRC64;
MGVKGLLFSI VLINLSLLGL CGYPRKPVDV PFWKNYEPSW ASHHIKYLSG GSTVDLVLDR
SSGAGFQSKK SYLFGHFSMK LKLVGGDSAG VVTAFYLSSN NAEHDEIDFE FLGNRTGQPY
ILQTNVFTGG KGDREQRIYL WFDPTKGYHS YSVLWNTFQI VIFVDDVPIR AFKNSKDLGV
KFPFNQPMKI YSSLWDADDW ATRGGLEKTD WSNAPFTASY TSFHVDGCEA ATPQEVQVCN
TKGMRWWDQK AFQDLDALQY RRLRWVRQKY TIYNYCTDRK RYPTLPPECT KDRDI
