XTH8_DIOKA
ID XTH8_DIOKA Reviewed; 288 AA.
AC A0A067YMX8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Xyloglucan endotransglucosylase protein 8 {ECO:0000305};
DE Short=XET protein 8 {ECO:0000305};
DE EC=2.4.1.207 {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27966647};
DE AltName: Full=DkXTH8 {ECO:0000303|PubMed:27966647};
DE AltName: Full=Xyloglucan endotransglucosylase/hydrolase protein 8 {ECO:0000305};
DE Short=XTH protein 8 {ECO:0000305};
DE Flags: Precursor;
GN Name=XTH8 {ECO:0000303|PubMed:27966647, ECO:0000312|EMBL:AHE13905.1};
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:AHE13905.1};
RN [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:27966647};
RC TISSUE=Fruit {ECO:0000303|PubMed:27966647};
RX PubMed=27966647; DOI=10.1038/srep39155;
RA Han Y., Ban Q., Li H., Hou Y., Jin M., Han S., Rao J.;
RT "DkXTH8, a novel xyloglucan endotransglucosylase/hydrolase in persimmon,
RT alters cell wall structure and promotes leaf senescence and fruit
RT postharvest softening.";
RL Sci. Rep. 6:39155-39155(2016).
CC -!- FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves
CC and religates xyloglucan polymers. Does not catalyze xyloglucan
CC endohydrolysis (XEH). Overexpression in Arabidopsis transgenic plants
CC causes accelerated dark-induced leaf senescence and higher lipid
CC peroxidation of the leaf cells. Overexpression in transgenic tomato
CC plants promotes fruit ripening and softening. Probably involved in cell
CC wall restructuring during postharvest fruit softening.
CC {ECO:0000269|PubMed:27966647}.
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:27966647};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is around 6. Activity decreases sharply when the pH is
CC lowered from 5 to 4. {ECO:0000269|PubMed:27966647};
CC Temperature dependence:
CC Optimum temperature is between 30-40 degrees Celsius.
CC {ECO:0000269|PubMed:27966647};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27966647}. Secreted,
CC extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}.
CC -!- TISSUE SPECIFICITY: Highly expressed in mature fruits. Very low
CC expression in leaves, flowers, calyces and stems.
CC {ECO:0000269|PubMed:27966647}.
CC -!- DEVELOPMENTAL STAGE: Expressed during fruit ripening. Fruits harvested
CC 140 days after full bloom show much higher expression levels than
CC fruits harvested 20, 60 or 100 days after full bloom. Expression in
CC fruits increases rapidly during storage and is highest on day 12,
CC simultaneously with a dramatic fruit softening.
CC {ECO:0000269|PubMed:27966647}.
CC -!- INDUCTION: In fruits, expression increases by propylene or abscisic
CC acid (ABA) treatment, and is highest on day 4 and 8 of storage,
CC respectively. Expression decreases by 1-methylcyclopropene (1-MCP) or
CC gibberellic acid (GA3) treatment during storage.
CC {ECO:0000269|PubMed:27966647}.
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 2
CC subfamily. {ECO:0000305}.
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DR EMBL; KF318888; AHE13905.1; -; mRNA.
DR BRENDA; 2.4.1.207; 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:0030247; F:polysaccharide binding; ISS:UniProtKB.
DR GO; GO:0016762; F:xyloglucan:xyloglucosyl transferase activity; IDA:UniProtKB.
DR GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IC:UniProtKB.
DR GO; GO:0071370; P:cellular response to gibberellin stimulus; IEP:UniProtKB.
DR GO; GO:0009835; P:fruit ripening; IEP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:2000899; P:xyloglucan catabolic process; IDA:UniProtKB.
DR CDD; cd02176; GH16_XET; 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; PTHR31062; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF06955; XET_C; 1.
DR PIRSF; PIRSF005604; XET; 1.
DR SUPFAM; SSF49899; SSF49899; 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; 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..288
FT /note="Xyloglucan endotransglucosylase protein 8"
FT /evidence="ECO:0000255|RuleBase:RU361120"
FT /id="PRO_5005103795"
FT DOMAIN 26..215
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098,
FT ECO:0000305"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PIRSR:PIRSR005604-1,
FT ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000255|PIRSR:PIRSR005604-1,
FT ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 106
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 119..121
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 129..131
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 194..195
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 199
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 273
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 104
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PIRSR:PIRSR005604-2,
FT ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 224..233
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 268..282
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 288 AA; 32526 MW; 670458BCD2C7A02D CRC64;
MAASPYSIFA VQLLLLASWM LSSSSSNFNQ DFNIAWGGGR ARILNNGELV TLSLDKASGS
GFRSKNLYLF GKIDMQLKLV PGNSAGTVTT YYLSSEGSVR DEIDFEFLGN LTGEPYTLHT
NVYSHGKGER EQQFRLWFDP AADFHTYSIL WNSKTIVFYV DQTPVREFKN MESIGVPYLR
QPMRLFSSIW NADEWATRGG LIKTDWTQAP FTTSYRNFRA DNACVWAAKA SSCGLAAGGN
AWLSVELDAK SRGRLRWVRR NQMIYDYCVD GKRFPRGVPP ECKLNLHI
