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Database: UniProt
Entry: M8CDV3_AEGTA
LinkDB: M8CDV3_AEGTA
Original site: M8CDV3_AEGTA 
ID   M8CDV3_AEGTA            Unreviewed;       290 AA.
AC   M8CDV3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Xyloglucan endotransglucosylase/hydrolase {ECO:0000256|RuleBase:RU361120};
DE            EC=2.4.1.207 {ECO:0000256|RuleBase:RU361120};
OS   Aegilops tauschii (Tausch's goatgrass) (Aegilops squarrosa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=37682 {ECO:0000313|EnsemblPlants:EMT32589};
RN   [1] {ECO:0000313|EnsemblPlants:EMT32589}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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.
CC       {ECO:0000256|RuleBase:RU361120}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000256|RuleBase:RU361120}. Secreted, extracellular space,
CC       apoplast {ECO:0000256|RuleBase:RU361120}.
CC   -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC       enzymatic activity. {ECO:0000256|RuleBase:RU361120}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC       {ECO:0000256|RuleBase:RU361120}.
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DR   AlphaFoldDB; M8CDV3; -.
DR   SMR; M8CDV3; -.
DR   EnsemblPlants; EMT32589; EMT32589; F775_05590.
DR   OMA; MLIRASM; -.
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:0010411; P:xyloglucan metabolic process; IEA:InterPro.
DR   CDD; cd02176; GH16_XET; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR044791; Beta-glucanase/XTH.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR010713; XET_C.
DR   InterPro; IPR016455; XTH.
DR   PANTHER; PTHR31062:SF272; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE; 1.
DR   PANTHER; PTHR31062; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 8-RELATED; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   Pfam; PF06955; XET_C; 1.
DR   PIRSF; PIRSF005604; XET; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   3: Inferred from homology;
KW   Apoplast {ECO:0000256|RuleBase:RU361120};
KW   Cell wall {ECO:0000256|RuleBase:RU361120};
KW   Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU361120};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361120};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361120};
KW   Secreted {ECO:0000256|RuleBase:RU361120};
KW   Signal {ECO:0000256|RuleBase:RU361120};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361120}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU361120"
FT   CHAIN           24..290
FT                   /note="Xyloglucan endotransglucosylase/hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361120"
FT                   /id="PRO_5014486546"
FT   ACT_SITE        104
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT   ACT_SITE        108
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
SQ   SEQUENCE   290 AA;  32853 MW;  C425BBECBE8B2376 CRC64;
     MASSVRQPWQ LLLIVLLPSL AAATVFDDNY VPSWGADGYH LVDQGTETRL TMDRTSGAGF
     RSRSTYGSGF FHMRIKVPGG YTAGVITAFY LASEAPYDGS DRDEVDFEFL GNVDGENITL
     QTNVFVNGDG DREQRLNLWF DPAADFHEYK ILWNPYQLVI LVDDVPIRVL RNLTGQVPEY
     EFPVKQMGVR ASLWDGSDWA TDGGRIKIDW GRAPFTAGFQ GFDVDACANT SSTPCDSTDL
     WWNARRHRRL SVREQAAYEH VRRTYMNYDY CADKDRFQNG KVPVECSYTT
//
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