XTH6_DIOKA
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 03-AUG-2022, entry version 26.
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}.
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DR EMBL; KC511053; AGT29356.1; -; mRNA.
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 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; PTHR31062; 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; SSF49899; 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
