ID A0A067XRK9_DIOKA Unreviewed; 299 AA. AC A0A067XRK9; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 10-FEB-2021, entry version 22. DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase {ECO:0000256|RuleBase:RU361120}; DE EC=2.4.1.207 {ECO:0000256|RuleBase:RU361120}; GN Name=XTH6 {ECO:0000313|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:0000313|EMBL:AGT29356.1}; RN [1] {ECO:0000313|EMBL:AGT29356.1} RP NUCLEOTIDE SEQUENCE. 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 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 {ECO:0000256|RuleBase:RU361120}. 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:0000256|ARBA:ARBA00000284, CC ECO:0000256|RuleBase:RU361120}; CC -!- SUBCELLULAR LOCATION: Secreted, cell wall CC {ECO:0000256|RuleBase:RU361120}. Secreted, extracellular space, CC apoplast {ECO:0000256|ARBA:ARBA00004271, CC ECO:0000256|RuleBase:RU361120}. CC -!- PTM: Contains at least one intrachain disulfide bond essential for its CC enzymatic activity. {ECO:0000256|RuleBase:RU361120}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. CC {ECO:0000256|RuleBase:RU361120}. 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 GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell. DR GO; GO:0005618; C:cell wall; 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:0010411; P:xyloglucan metabolic process; IEA:InterPro. 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 Pfam; PF00722; Glyco_hydro_16; 1. DR Pfam; PF06955; XET_C; 1. DR PIRSF; PIRSF005604; XET; 1. DR PRINTS; PR00737; GLHYDRLASE16. DR SUPFAM; SSF49899; SSF49899; 1. DR PROSITE; PS51762; GH16_2; 1. PE 2: Evidence at transcript level; KW Apoplast {ECO:0000256|ARBA:ARBA00022523, ECO:0000256|RuleBase:RU361120}; KW Cell wall {ECO:0000256|ARBA:ARBA00022512, ECO:0000256|RuleBase:RU361120}; KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU361120}; KW Glycosidase {ECO:0000256|RuleBase:RU361120}; KW Hydrolase {ECO:0000256|RuleBase:RU361120, ECO:0000313|EMBL:AGT29356.1}; KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361120}; KW Signal {ECO:0000256|RuleBase:RU361120}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361120}. FT SIGNAL 1..25 FT /evidence="ECO:0000256|RuleBase:RU361120" FT CHAIN 26..299 FT /note="Xyloglucan endotransglucosylase/hydrolase" FT /evidence="ECO:0000256|RuleBase:RU361120" FT /id="PRO_5005103835" FT DOMAIN 22..219 FT /note="GH16" FT /evidence="ECO:0000259|PROSITE:PS51762" FT ACT_SITE 105 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR005604-1" FT ACT_SITE 109 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR005604-1" FT CARBOHYD 113 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR005604-2" 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 //