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Database: UniProt
Entry: N0DXB5_CUCSA
LinkDB: N0DXB5_CUCSA
Original site: N0DXB5_CUCSA 
ID   N0DXB5_CUCSA            Unreviewed;       288 AA.
AC   N0DXB5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Xyloglucan endotransglucosylase/hydrolase {ECO:0000256|RuleBase:RU361120};
DE            EC=2.4.1.207 {ECO:0000256|RuleBase:RU361120};
GN   Name=xth23 {ECO:0000313|EMBL:CCH26633.1};
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659 {ECO:0000313|EMBL:CCH26633.1};
RN   [1] {ECO:0000313|EMBL:CCH26633.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Malinowski R., Fry S., Zuzga S., Wisniewska A., Godlewski M.,
RA   Noyszewski A., Malepszy S., Filipecki M.;
RT   "Developmental expression of the cucumber Cs-XTH1 and Cs-XTH3 genes,
RT   encoding xyloglucan endotransglucosylase/hydrolases, can be influenced by
RT   mechanical stimuli.";
RL   Submitted (APR-2012) 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; HE803073; CCH26633.1; -; Genomic_DNA.
DR   AlphaFoldDB; N0DXB5; -.
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   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:SF146; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 31; 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|ARBA:ARBA00022523, ECO:0000256|RuleBase:RU361120};
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512, 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|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361120};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361120}.
FT   DOMAIN          15..223
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   ACT_SITE        107
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT   ACT_SITE        111
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
SQ   SEQUENCE   288 AA;  32997 MW;  8AA61FE1A1FB113F CRC64;
     MSHYFFFSFS LSSSSSSSLS PLPKTILPPL AIFQVFRNRW GSQHQKVDQG TLTIWLDSSS
     GSGFKSLHRY QSGYFGAAIK LHPGYTAGVI TSFYLSNNED YPGNHDEIDI EFLGTTSDKP
     YVLQTNVFMR GSGDGNIIGR EMRFHLWFNP TQDFHNYAIL WTPEEIIFLV DDVPIRRYER
     KSEATFPVRP MWVYGSIWDA SSWATEDGKY KADYKYQPFI GRYNNFKLSG CTTDGAASCR
     PLNSGPGRGG RGRMSQQQEK AMEWVQNNYL VYNYCHDPRR DHTLTPEC
//
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