XTH2_DIOKA
ID XTH2_DIOKA Reviewed; 295 AA.
AC G5DAC7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Xyloglucan endotransglucosylase protein 2 {ECO:0000305};
DE Short=XET protein 2 {ECO:0000305};
DE EC=2.4.1.207 {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:25849978};
DE AltName: Full=DkXTH2 {ECO:0000303|PubMed:23265513, ECO:0000303|PubMed:25849978};
DE AltName: Full=Xyloglucan endotransglucosylase/hydrolase protein 2 {ECO:0000305};
DE Short=XTH protein 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=XTH2 {ECO:0000303|PubMed:23265513, ECO:0000303|PubMed:25849978,
GN ECO:0000312|EMBL:AEQ37176.1};
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:AEQ37176.1};
RN [1] {ECO:0000312|EMBL:AEQ37176.1}
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,
RC ECO:0000312|EMBL:AEQ37176.1};
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).
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 fruit ripening and postharvest fruit softening.
CC {ECO:0000269|PubMed:25849978}.
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 4.5-6.5. 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.
CC {ECO:0000269|PubMed:23265513, ECO:0000269|PubMed:25849978}.
CC -!- DEVELOPMENTAL STAGE: Expressed during fruit ripening (PubMed:23265513,
CC PubMed:25849978). During storage, highest expression in fruits on day
CC 12, decreasing sharply thereafter until end of storage (day 18)
CC (PubMed:23265513). Expression is low in immature growing fruits, but
CC increases significantly during the mature stage with the highest
CC expression 120 days after full bloom. Expression in fruits is rapidly
CC increased during storage at 25 degrees Celsius, with the highest
CC expression on day 12, after which the expression decreases steadily
CC until the end of storage (PubMed:25849978).
CC {ECO:0000269|PubMed:23265513, ECO:0000269|PubMed:25849978}.
CC -!- INDUCTION: In fruits, expression is greatly decreased by gibberellic
CC acid (GA3) on day 12 of storage and by 1-methylcyclopropene (1-MCP)
CC until day 12 of storage (PubMed:23265513). Expression in fruits is also
CC decreased by low (0 degrees Celsius) temperature treatment throughout
CC the storage (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 1
CC subfamily. {ECO:0000305}.
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DR EMBL; JN605345; AEQ37176.1; -; 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; 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..23
FT /evidence="ECO:0000255|RuleBase:RU361120"
FT CHAIN 24..295
FT /note="Xyloglucan endotransglucosylase protein 2"
FT /evidence="ECO:0000255|RuleBase:RU361120"
FT /id="PRO_5005132397"
FT DOMAIN 24..222
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098,
FT ECO:0000305"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PIRSR:PIRSR005604-1,
FT ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000255|PIRSR:PIRSR005604-1,
FT ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 112
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 125..127
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 135..137
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 201..202
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 206
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 281
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 110
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PIRSR:PIRSR005604-2,
FT ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 230..239
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 276..289
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 295 AA; 34317 MW; 1BAAAB0FF4958507 CRC64;
MAMGTHFGGL WLALLCMVSA TMGAVPRKPV DVPFGRNYVP TWAFDHIKYF NGGSQIQLSL
DKYTGTGFQS KGSYLFGHFS MQIKMVPGDS AGTVTAFYLS SQNSEHDEID FEFLGNRTGQ
PYILQTNVFT GGKGDREQRI FLWFDPTKEY HSYSVLWNLF LIIFFVDDVP IRVFKNSKDL
GVRFPFDQPM KIYSSLWNAD DWATRGGLEK TDWSKAPFVA SYRSFHVDGC EASVNAKFCD
TQGKRWWDQK EFQDLDSFQY RRLRWVRSKY TIYNYCTDRK RYPVMPPECK RDRDI
