ID XTH_BRAOB Reviewed; 295 AA. AC Q6YDN9; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 88. DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase; DE EC=2.4.1.207; DE AltName: Full=BobXET16A; DE Flags: Precursor; GN Name=XET16A; OS Brassica oleracea var. botrytis (Cauliflower). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica. OX NCBI_TaxID=3715; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-38 AND 75-133, MASS RP SPECTROMETRY, AND GLYCOSYLATION. RX PubMed=12826015; DOI=10.1042/bj20030485; RA Henriksson H., Denman S.E., Campuzano I.D.G., Ademark P., Master E.R., RA Teeri T.T., Brumer H. III; RT "N-linked glycosylation of native and recombinant cauliflower xyloglucan RT endotransglycosylase 16A."; RL Biochem. J. 375:61-73(2003). 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 {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 -!- PTM: The N-glycan consists of an (GlcNAc)2(Hex)6 oligosaccharide; not CC essential for its enzymatic activity. CC -!- MASS SPECTROMETRY: Mass=33115; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:12826015}; CC -!- MISCELLANEOUS: No hydrolytic activity detected in vitro. 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; AY156708; AAO00727.1; -; mRNA. DR AlphaFoldDB; Q6YDN9; -. DR SMR; Q6YDN9; -. DR CAZy; GH16; Glycoside Hydrolase Family 16. DR GlyConnect; 629; 6 N-Linked glycans. DR GlyCosmos; Q6YDN9; 1 site, 9 glycans. DR iPTMnet; Q6YDN9; -. DR BRENDA; 2.4.1.207; 948. 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; 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:SF319; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 4; 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 1: Evidence at protein level; KW Apoplast; Cell wall; Cell wall biogenesis/degradation; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase; KW Hydrolase; Secreted; Signal; Transferase. FT SIGNAL 1..23 FT /evidence="ECO:0000269|PubMed:12826015" FT CHAIN 24..295 FT /note="Xyloglucan endotransglucosylase/hydrolase" FT /id="PRO_0000011834" FT DOMAIN 25..222 FT /note="GH16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098" FT ACT_SITE 108 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064" FT ACT_SITE 112 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064" FT BINDING 112 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 125..127 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 135..137 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 201..202 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 206 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 110 FT /note="Important for catalytic activity" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT CARBOHYD 116 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12826015" FT DISULFID 230..239 FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT DISULFID 276..289 FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" SQ SEQUENCE 295 AA; 34105 MW; 15054A3E4929BD4E CRC64; MAVSSTPWAL VALFLMASST VMAIPPRKAI DVPFGRNYVP TWAFDHQKQL NGGSELQLIL DKYTGTGFQS KGSYLFGHFS MHIKLPAGDT AGVVTAFYLS STNNEHDEID FEFLGNRTGQ PVILQTNVFT GGKGNREQRI YLWFDPSKAY HTYSVLWNLY QIVFFVDNIP IRVFKNAKDL GVRFPFNQPM KLYSSLWNAD DWATRGGLEK TNWANAPFIA SYRGFHIDGC QASVEAKYCA TQGRMWWDQN EFRDLDAEQY RRLKWVRMKW TIYNYCTDRT RFPVMPAECR RDRDV //