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XTH1_SOLLC
ID   XTH1_SOLLC              Reviewed;         296 AA.
AC   Q40144;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase 1;
DE            Short=LeXTH1;
DE            EC=2.4.1.207;
DE   Flags: Precursor;
GN   Name=XTH1; Synonyms=EXT;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8244968; DOI=10.1016/s0021-9258(19)74400-7;
RA   Okazawa K., Sato Y., Nakagawa T., Asada K., Kato I., Tomita E.,
RA   Nishitani K.;
RT   "Molecular cloning and cDNA sequencing of endoxyloglucan transferase, a
RT   novel class of glycosyltransferase that mediates molecular grafting between
RT   matrix polysaccharides in plant cell walls.";
RL   J. Biol. Chem. 268:25364-25368(1993).
CC   -!- FUNCTION: Catalyzes xyloglucan endohydrolysis (XEH) and/or
CC       endotransglycosylation (XET). Cleaves and religates xyloglucan
CC       polymers, an essential constituent of the primary cell wall, and
CC       thereby participates in cell wall construction of growing tissues (By
CC       similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC       extracellular space, apoplast {ECO:0000305}.
CC   -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC       enzymatic activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; D16456; BAA03923.1; -; mRNA.
DR   PIR; D49539; D49539.
DR   RefSeq; NP_001233858.1; NM_001246929.2.
DR   AlphaFoldDB; Q40144; -.
DR   SMR; Q40144; -.
DR   STRING; 4081.Solyc01g099630.2.1; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   PaxDb; Q40144; -.
DR   PRIDE; Q40144; -.
DR   EnsemblPlants; Solyc01g099630.3.1; Solyc01g099630.3.1; Solyc01g099630.3.
DR   GeneID; 544272; -.
DR   Gramene; Solyc01g099630.3.1; Solyc01g099630.3.1; Solyc01g099630.3.
DR   KEGG; sly:544272; -.
DR   eggNOG; ENOG502QQ71; Eukaryota.
DR   HOGENOM; CLU_048041_2_1_1; -.
DR   InParanoid; Q40144; -.
DR   OMA; HHIKFLN; -.
DR   OrthoDB; 1209387at2759; -.
DR   PhylomeDB; Q40144; -.
DR   BRENDA; 2.4.1.207; 3101.
DR   BRENDA; 3.2.1.151; 3101.
DR   Proteomes; UP000004994; Chromosome 1.
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; 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: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   2: Evidence at transcript level;
KW   Apoplast; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
KW   Transferase.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..296
FT                   /note="Probable xyloglucan endotransglucosylase/hydrolase
FT                   1"
FT                   /id="PRO_0000011835"
FT   DOMAIN          23..221
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        107
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   ACT_SITE        111
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   BINDING         111
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         124..126
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         134..136
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         200..201
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         205
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         282
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   SITE            109
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        229..240
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   DISULFID        277..290
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ   SEQUENCE   296 AA;  34011 MW;  B4BD0A255406F444 CRC64;
     MGIIKGVLFS IVLINLSLVV FCGYPRRPVD VPFWKNYEPS WASHHIKFLN GGTTTDLILD
     RSSGAGFQSK KSYLFGHFSM KMRLVGGDSA GVVTAFYLSS NNAEHDEIDF EFLGNRTGQP
     YILQTNVFTG GKGNREQRIY LWFDPTKGYH SYSVLWNTYL IVIFVDDVPI RAFKNSKDLG
     VKFPFNQPMK IYSSLWDADD WATRGGLEKT NWANAPFTAS YTSFHVDGCE AATPQEVQVC
     NTKGMKWWDQ KAFQDLDALQ YRRLRWVRQK YTVYNYCTDK ARYPVPPPEC TKDRDI
 
 
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