ID XTH6_DIOKA Reviewed; 299 AA. AC A0A067XRK9; DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2014, sequence version 1. DT 28-JUN-2023, entry version 29. DE RecName: Full=Xyloglucan endotransglucosylase protein 6 {ECO:0000305}; DE Short=XET protein 6 {ECO:0000305}; DE EC=2.4.1.207 {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27242828}; DE AltName: Full=DkXTH6 {ECO:0000303|PubMed:27242828}; DE AltName: Full=Xyloglucan endotransglucosylase/hydrolase protein 6 {ECO:0000305}; DE Short=XTH protein 6 {ECO:0000305}; DE Flags: Precursor; GN Name=XTH6 {ECO:0000303|PubMed:27242828, ECO:0000312|EMBL:AGT29356.1}; OS Diospyros kaki (Kaki persimmon) (Diospyros chinensis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; Ericales; Ebenaceae; Diospyros. OX NCBI_TaxID=35925 {ECO:0000312|EMBL:AGT29356.1}; RN [1] {ECO:0000312|EMBL:AGT29356.1} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, INDUCTION, AND PHYLOGENETIC ANALYSIS. RC STRAIN=cv. Fuping Jianshi {ECO:0000303|PubMed:27242828}; RC TISSUE=Fruit {ECO:0000303|PubMed:27242828}; RX PubMed=27242828; DOI=10.3389/fpls.2016.00624; RA Han Y., Ban Q., Hou Y., Meng K., Suo J., Rao J.; RT "Isolation and Characterization of Two Persimmon Xyloglucan RT Endotransglycosylase/Hydrolase (XTH) Genes That Have Divergent Functions in RT Cell Wall Modification and Fruit Postharvest Softening."; RL Front. Plant Sci. 7:624-624(2016). CC -!- FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves CC and religates xyloglucan polymers. Does not catalyze xyloglucan CC endohydrolysis (XEH). Probably involved in cell wall restructuring CC during postharvest fruit softening. {ECO:0000269|PubMed:27242828}. 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 Evidence={ECO:0000255|RuleBase:RU361120, CC ECO:0000269|PubMed:27242828}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is around 6. Highly active between pH range 4.5-6.5. CC {ECO:0000269|PubMed:27242828}; CC -!- SUBCELLULAR LOCATION: Secreted, cell wall CC {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27242828}. Secreted, CC extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}. CC -!- TISSUE SPECIFICITY: Highest expression in ripe leaves after full CC expansion. Also expressed in fruits, and at a lower level in flowers CC and stems (picked at anthesis). {ECO:0000269|PubMed:27242828}. CC -!- DEVELOPMENTAL STAGE: Expressed during fruit ripening. Expression in CC mature tissues, such as ripe leaves and fruits, is considerably higher CC than in fast growing tissues, such as young leaves and fruits. In CC fruits, expression increases rapidly during storage at 25 degees CC Celsius, and is highest on day 12 after which it decreases CC dramatically. {ECO:0000269|PubMed:27242828}. CC -!- INDUCTION: In fruits, up-regulated by abscisic acid (ABA) or by CC propylene treatment, and down-regulated by gibberellic acid (GA3) or by CC cold treatment during storage. {ECO:0000269|PubMed:27242828}. CC -!- PTM: Contains at least one intrachain disulfide bond essential for its CC enzymatic activity. {ECO:0000255|RuleBase:RU361120}. 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; KC511053; AGT29356.1; -; mRNA. DR AlphaFoldDB; A0A067XRK9; -. DR SMR; A0A067XRK9; -. DR GlyCosmos; A0A067XRK9; 1 site, No reported glycans. DR BRENDA; 2.4.1.207; 7744. DR BRENDA; 3.2.1.151; 7744. 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:0009835; P:fruit ripening; 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; IPR010713; XET_C. DR InterPro; IPR016455; XTH. DR PANTHER; PTHR31062; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 8-RELATED; 1. DR PANTHER; PTHR31062:SF108; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 9; 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; PS51762; GH16_2; 1. PE 1: Evidence at protein level; KW Apoplast; Cell wall; Cell wall biogenesis/degradation; Disulfide bond; KW Fruit ripening; Glycoprotein; Glycosidase; Glycosyltransferase; Hydrolase; KW Secreted; Signal; Transferase. FT SIGNAL 1..25 FT /evidence="ECO:0000255|RuleBase:RU361120" FT CHAIN 26..299 FT /note="Xyloglucan endotransglucosylase protein 6" FT /evidence="ECO:0000255|RuleBase:RU361120" FT /id="PRO_5005103835" FT DOMAIN 26..219 FT /note="GH16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098, FT ECO:0000305" FT ACT_SITE 105 FT /note="Nucleophile" FT /evidence="ECO:0000255|PIRSR:PIRSR005604-1" FT ACT_SITE 109 FT /note="Proton donor" FT /evidence="ECO:0000255|PIRSR:PIRSR005604-1" FT BINDING 109 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 122..124 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 132..134 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 198..199 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 203 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 286 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT SITE 107 FT /note="Important for catalytic activity" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT CARBOHYD 113 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PIRSR:PIRSR005604-2, FT ECO:0000255|PROSITE-ProRule:PRU00498" FT DISULFID 227..242 FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT DISULFID 281..294 FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" SQ SEQUENCE 299 AA; 33764 MW; BC9D8247C489CFFD CRC64; MASSLTLPMA MAFTLLALSF ASAMGGSMNS SRFDELFQPS WAFDHFVYEG EVLKMKLDNY SGAGFSSKGK YLFGKVTVQI KLVEGDSAGT VTAFYMSSDG TNHNEFDFEF LGNTTGEPYL VQTNVYVNGV GNREQRLNLW FDPTKDFHSY SLLWNQRQVV FMVDETPIRV HSNLEHRGIP FPKDQPMGVY SSIWNADDWA TQGGRIKTDW SHAPFVASYQ GFAIDACECP AAVAATDNAR RCSSSAEKQF WWDMPTLSEL SLHQSHQLIW VRANHLVYDY CTDTARFPVT PAECEHHRH //