XTH7_DIOKA
ID XTH7_DIOKA Reviewed; 268 AA.
AC A0A067XR63;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Xyloglucan endotransglucosylase protein 7 {ECO:0000305};
DE Short=XET protein 7 {ECO:0000305};
DE EC=2.4.1.207 {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27242828};
DE AltName: Full=DkXTH7 {ECO:0000303|PubMed:27242828};
DE AltName: Full=Xyloglucan endotransglucosylase/hydrolase protein 7 {ECO:0000305};
DE Short=XTH protein 7 {ECO:0000305};
GN Name=XTH7 {ECO:0000303|PubMed:27242828, ECO:0000312|EMBL:AGT29357.1};
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:AGT29357.1};
RN [1] {ECO:0000312|EMBL:AGT29357.1}
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 assembly and
CC synthesis in fast growing tissues and in the maintenance of firmness in
CC mature fruits. {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 between 5-6. Activity decreases sharply when the pH is
CC lowered from 5 to 4. {ECO:0000269|PubMed:27242828};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27242828}.
CC Note=Dispersed throughout the cell. {ECO:0000269|PubMed:27242828}.
CC -!- TISSUE SPECIFICITY: Expressed at a very high level in flowers and stems
CC (picked at anthesis), and at a lower level in ripe leaves and fruits.
CC {ECO:0000269|PubMed:27242828}.
CC -!- DEVELOPMENTAL STAGE: Expressed during fruit ripening. Expressed at an
CC extremely high level in fast growing tissues, such as young leaves and
CC fruits. {ECO:0000269|PubMed:27242828}.
CC -!- INDUCTION: In fruits, up-regulated by gibberellic acid (GA3) or by cold
CC 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 2
CC subfamily. {ECO:0000305}.
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DR EMBL; KC541541; AGT29357.1; -; mRNA.
DR BRENDA; 2.4.1.207; 7744.
DR BRENDA; 3.2.1.151; 7744.
DR GO; GO:0048046; C:apoplast; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; 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; IDA:UniProtKB.
DR GO; GO:0070726; P:cell wall assembly; IEP:UniProtKB.
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 Cell wall biogenesis/degradation; Cytoplasm; Disulfide bond;
KW Fruit ripening; Glycoprotein; Glycosidase; Glycosyltransferase; Hydrolase;
KW Transferase.
FT CHAIN 1..268
FT /note="Xyloglucan endotransglucosylase protein 7"
FT /id="PRO_0000454652"
FT DOMAIN 1..196
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PIRSR:PIRSR005604-1,
FT ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 86
FT /note="Proton donor"
FT /evidence="ECO:0000255|PIRSR:PIRSR005604-1,
FT ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 86
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 99..101
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 109..111
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 175..176
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 180
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 256
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 84
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PIRSR:PIRSR005604-2,
FT ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 204..213
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 251..265
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 268 AA; 30834 MW; 2663EFE369E0F158 CRC64;
MNAEGGNLHR EFEITWGDGR ARIHNNGGLL TLSLDRASGS GFRSKNEYLF GRIEIQIKLV
AGNSAGTVAT YYLSSEGPTH DEIDFEFLGN SSGEPYTLHT NVFSQGKGNR EQQFFLWFDP
TMDFHTYTIL WNPQRIIFYV DETPIREFKN LERHGIPFPR SQAMRVYSSM WNADDWATRG
GLVKTDWTKA PFTASYRSYK ADACVWSGEA SSCGSQDSNP SDKWWMTEEL NATRMKRLRW
VQKKYMVYNY CVDKMRFPEG LAPECNIS
