XTH1_DIOKA
ID XTH1_DIOKA Reviewed; 287 AA.
AC G5DAC6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Xyloglucan endotransglucosylase protein 1 {ECO:0000305};
DE Short=XET protein 1 {ECO:0000305};
DE EC=2.4.1.207 {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:25849978};
DE AltName: Full=DkXTH1 {ECO:0000303|PubMed:23265513, ECO:0000303|PubMed:25849978, ECO:0000303|PubMed:28155115};
DE AltName: Full=Xyloglucan endotransglucosylase/hydrolase protein 1 {ECO:0000305};
DE Short=XTH protein 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=XTH1 {ECO:0000303|PubMed:23265513, ECO:0000303|PubMed:25849978,
GN ECO:0000312|EMBL:AEQ37175.1};
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:AEQ37175.1};
RN [1] {ECO:0000312|EMBL:AEQ37175.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, AND PHYLOGENETIC ANALYSIS.
RC STRAIN=cv. Fuping Jianshi {ECO:0000303|PubMed:23265513};
RC TISSUE=Fruit flesh {ECO:0000303|PubMed:23265513};
RX PubMed=23265513; DOI=10.1016/j.foodchem.2012.09.141;
RA Zhu Q., Zhang Z., Rao J., Huber D.J., Lv J., Hou Y., Song K.;
RT "Identification of xyloglucan endotransglucosylase/hydrolase genes (XTHs)
RT and their expression in persimmon fruit as influenced by 1-
RT methylcyclopropene and gibberellic acid during storage at ambient
RT temperature.";
RL Food Chem. 138:471-477(2013).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND
RP PHYLOGENETIC ANALYSIS.
RC STRAIN=cv. Fuping Jianshi {ECO:0000303|PubMed:25849978};
RX PubMed=25849978; DOI=10.1371/journal.pone.0123668;
RA Han Y., Zhu Q., Zhang Z., Meng K., Hou Y., Ban Q., Suo J., Rao J.;
RT "Analysis of xyloglucan endotransglycosylase/hydrolase (XTH) genes and
RT diverse roles of isoenzymes during persimmon fruit development and
RT postharvest softening.";
RL PLoS ONE 10:e0123668-e0123668(2015).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Ganmaokui {ECO:0000303|PubMed:28155115};
RX PubMed=28155115; DOI=10.1007/s00299-017-2105-4;
RA Han Y., Han S., Ban Q., He Y., Jin M., Rao J.;
RT "Overexpression of persimmon DkXTH1 enhanced tolerance to abiotic stress
RT and delayed fruit softening in transgenic plants.";
RL Plant Cell Rep. 36:583-596(2017).
CC -!- FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves
CC and religates xyloglucan polymers. Does not catalyze xyloglucan
CC endohydrolysis (XEH) (PubMed:25849978). Overexpression in Arabidopsis
CC transgenic plants results in elevated tolerance to abiotic stress, such
CC as salt, ABA (abscisic acid) and drought stresses, and in the
CC production of wider leaves. Overexpression in transgenic tomato plants
CC slows down fruit ripening and softening, and the plants produce larger
CC fruits. Both transgenic plants have larger and more irregular cells.
CC Moreover, the fruits of the transgenic tomato have higher density of
CC cell wall and intercellular spaces. May provide cells with more
CC strength and thickness to maintain structural integrity
CC (PubMed:28155115). Probably involved in cell wall assembly and
CC synthesis in fast growing tissues and in the maintenance of firmness in
CC mature fruits (PubMed:25849978, PubMed:28155115).
CC {ECO:0000269|PubMed:25849978, ECO:0000269|PubMed:28155115}.
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:25849978};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is between 5-5.5. Loses activity rapidly when pH is
CC lowered from 5 to 4. {ECO:0000269|PubMed:25849978};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:25849978}. Secreted,
CC extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}.
CC -!- TISSUE SPECIFICITY: Expressed in fruit pulp (PubMed:23265513,
CC PubMed:25849978). Expressed in leaves, flowers, calyces, stems and
CC fruits. Highest expression in leaves and lowest in fruits
CC (PubMed:28155115). {ECO:0000269|PubMed:23265513,
CC ECO:0000269|PubMed:25849978, ECO:0000269|PubMed:28155115}.
CC -!- DEVELOPMENTAL STAGE: Expressed during fruit ripening (PubMed:23265513,
CC PubMed:25849978, PubMed:28155115). During storage, highest expression
CC is on day 3, decreasing until day 12 where expression increases again,
CC but after which it decreases sharply until end of storage (day 18)
CC (PubMed:23265513). Expression is very high in immature growing fruits,
CC with the highest expression 100 days after full bloom, after which
CC expressed at low levels during the mature stage (PubMed:25849978,
CC PubMed:28155115). Expression in fruits during storage at 25 degrees
CC Celsius is lower than the expression at the time of harvest
CC (PubMed:25849978). Expression in young leaves is significantly higher
CC than in mature leaves (PubMed:28155115). {ECO:0000269|PubMed:23265513,
CC ECO:0000269|PubMed:25849978, ECO:0000269|PubMed:28155115}.
CC -!- INDUCTION: In fruits, expression is decreased by gibberellic acid (GA3)
CC or 1-methylcyclopropene (1-MCP) at the beginning of storage (until day
CC 6) (PubMed:23265513). Expression in harvested fruits is increased by
CC low (0 degrees Celsius) temperature treatment, particularly at the end
CC of storage (day 32) (PubMed:25849978). {ECO:0000269|PubMed:23265513,
CC ECO:0000269|PubMed:25849978}.
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; JN605344; AEQ37175.1; -; 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: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; 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 PRINTS; PR00737; GLHYDRLASE16.
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..28
FT /evidence="ECO:0000255|RuleBase:RU361120"
FT CHAIN 29..287
FT /note="Xyloglucan endotransglucosylase protein 1"
FT /evidence="ECO:0000255|RuleBase:RU361120"
FT /id="PRO_5005132398"
FT DOMAIN 29..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 ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 109
FT /note="Proton donor"
FT /evidence="ECO:0000255|PIRSR:PIRSR005604-1,
FT ECO:0000255|PROSITE-ProRule:PRU10064"
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 271
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..231
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 266..280
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 287 AA; 32903 MW; 984973A6BE1E7786 CRC64;
MAFMSFINGF STLFLVALLA SSMMAAKGGN FYQDFDVTWG DHRAKIFNGG QLLSLSLDKT
SGSGFRSKKE YLFGRIDMQL KLVAGNSAGT VTAYYLSSQG PTHDEIDFEF LGNLSGDPYI
VHTNVFTQGK GNREQQFYLW FDPTRNFHTY SVVWNPRQII FLIDNTPIRV FKNAESIGVP
FPKNQPMRIY SSLWNADDWA TRGGLVKTDW TKAPFTAYYR NFNAKTCSGA CTESFGDGAW
QSQELDAHSR RRLRWVQKNF MIYNYCTDLK RFPEGLPKEC QRRSRFL
