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Database: UniProt
Entry: E6Y2R9_BAMOL
LinkDB: E6Y2R9_BAMOL
Original site: E6Y2R9_BAMOL 
ID   E6Y2R9_BAMOL            Unreviewed;       280 AA.
AC   E6Y2R9;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Xyloglucan endotransglucosylase/hydrolase {ECO:0000256|RuleBase:RU361120};
DE            EC=2.4.1.207 {ECO:0000256|RuleBase:RU361120};
OS   Bambusa oldhamii (Giant timber bamboo).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Bambusoideae; Bambusodae; Bambuseae; Bambusinae; Bambusa.
OX   NCBI_TaxID=58923 {ECO:0000313|EMBL:ABV46534.1};
RN   [1] {ECO:0000313|EMBL:ABV46534.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Jeang C.-L., Huang Y.-C., Wang A.-Y.;
RT   "Green Bamboo xyloglucan endotransglucosylase hydrolase 2 (BoXTH2) cDNA
RT   sequence.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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   EMBL; EF680732; ABV46534.1; -; mRNA.
DR   AlphaFoldDB; E6Y2R9; -.
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; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 8-RELATED; 1.
DR   PANTHER; PTHR31062:SF149; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE; 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   2: Evidence at transcript level;
KW   Apoplast {ECO:0000256|RuleBase:RU361120};
KW   Cell wall {ECO:0000256|RuleBase:RU361120};
KW   Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU361120};
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361120}.
FT   DOMAIN          9..203
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   ACT_SITE        89
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT   ACT_SITE        93
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-2"
SQ   SEQUENCE   280 AA;  31537 MW;  C45791A199407D73 CRC64;
     MAMACLVAIA QGGNFYQDAE MSWGQGRGKV VDGGRGLDLT LDRSSGSGFQ SKNEYLFGKI
     DMQIRLVPGN SAGTVTTFYL SSQGSTHDEI DMEFLGNVTG EPYTLHTNVF TQGQGQREQQ
     FRLWFDPTKA FHTYSIIWNP QHVIFAVDGT PIRDFKNMEA RGVAFPKSQP MRLYASLWNA
     DDWATQGGRV KADWSQAPFV ASFRNFNADA CVWSAGAQRC PVGTMEAAAA PGGRSSWWNQ
     EFSDMSYRRM RWVQRKFMIY NYCTDTKRYP QGVPAECKLR
//
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