ID XTH1_SOLLC Reviewed; 296 AA. AC Q40144; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 121. DE RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase 1; DE Short=LeXTH1; DE EC=2.4.1.207; DE Flags: Precursor; GN Name=XTH1; Synonyms=EXT; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum; OC Solanum subgen. Lycopersicon. OX NCBI_TaxID=4081; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D16456; BAA03923.1; -; mRNA. DR PIR; D49539; D49539. DR RefSeq; NP_001233858.1; NM_001246929.2. DR AlphaFoldDB; Q40144; -. DR SMR; Q40144; -. DR STRING; 4081.Q40144; -. DR CAZy; GH16; Glycoside Hydrolase Family 16. DR GlyCosmos; Q40144; 1 site, No reported glycans. DR PaxDb; 4081-Solyc01g099630-2-1; -. DR EnsemblPlants; Solyc01g099630.3.1; Solyc01g099630.3.1; Solyc01g099630.3. DR GeneID; 544272; -. DR Gramene; Solyc01g099630.3.1; Solyc01g099630.3.1; Solyc01g099630.3. DR KEGG; sly:544272; -. DR eggNOG; ENOG502QQ71; Eukaryota. DR HOGENOM; CLU_048041_2_1_1; -. DR InParanoid; Q40144; -. DR OMA; HHIKFLN; -. DR OrthoDB; 337487at2759; -. DR PhylomeDB; Q40144; -. DR BRENDA; 2.4.1.207; 3101. DR BRENDA; 3.2.1.151; 3101. DR Proteomes; UP000004994; Chromosome 1. 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 Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR044791; Beta-glucanase/XTH. DR InterPro; IPR008264; Beta_glucanase. 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:SF227; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE 1-RELATED; 1. DR Pfam; PF00722; Glyco_hydro_16; 1. DR Pfam; PF06955; XET_C; 1. DR PIRSF; PIRSF005604; XET; 1. DR PRINTS; PR00737; GLHYDRLASE16. 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; 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..296 FT /note="Probable xyloglucan endotransglucosylase/hydrolase FT 1" FT /id="PRO_0000011835" FT DOMAIN 23..221 FT /note="GH16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098" FT ACT_SITE 107 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064" FT ACT_SITE 111 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064" FT BINDING 111 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 124..126 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 134..136 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 200..201 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 205 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 282 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT SITE 109 FT /note="Important for catalytic activity" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT CARBOHYD 115 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 229..240 FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT DISULFID 277..290 FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" SQ SEQUENCE 296 AA; 34011 MW; B4BD0A255406F444 CRC64; MGIIKGVLFS IVLINLSLVV FCGYPRRPVD VPFWKNYEPS WASHHIKFLN GGTTTDLILD RSSGAGFQSK KSYLFGHFSM KMRLVGGDSA GVVTAFYLSS NNAEHDEIDF EFLGNRTGQP YILQTNVFTG GKGNREQRIY LWFDPTKGYH SYSVLWNTYL IVIFVDDVPI RAFKNSKDLG VKFPFNQPMK IYSSLWDADD WATRGGLEKT NWANAPFTAS YTSFHVDGCE AATPQEVQVC NTKGMKWWDQ KAFQDLDALQ YRRLRWVRQK YTVYNYCTDK ARYPVPPPEC TKDRDI //