ID J7H8Q7_9GENT Unreviewed; 304 AA.
AC J7H8Q7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase {ECO:0000256|RuleBase:RU361120};
DE EC=2.4.1.207 {ECO:0000256|RuleBase:RU361120};
GN Name=XTH2 {ECO:0000313|EMBL:AFP93558.1};
OS Neolamarckia cadamba.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Rubiaceae; Cinchonoideae; Naucleeae;
OC Neolamarckia.
OX NCBI_TaxID=153762 {ECO:0000313|EMBL:AFP93558.1};
RN [1] {ECO:0000313|EMBL:AFP93558.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Developing xylem {ECO:0000313|EMBL:AFP93558.1};
RA Tiong S.Y., Ho W.S., Pang S.L., Jusoh I.;
RT "Full-length cDNA cloning and SNP discovery of xyloglucan
RT endotransglycosylase/hydrolase (XTH) and cellulose synthase (CesA) genes in
RT kelampayan (Neolamarckia cadamba).";
RL Submitted (JUN-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; JX134620; AFP93558.1; -; mRNA.
DR AlphaFoldDB; J7H8Q7; -.
DR GlyCosmos; J7H8Q7; 1 site, No reported glycans.
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; IPR008264; Beta_glucanase.
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:SF108; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 9; 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; 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 Signal {ECO:0000256|RuleBase:RU361120};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361120}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|RuleBase:RU361120"
FT CHAIN 32..304
FT /note="Xyloglucan endotransglucosylase/hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361120"
FT /id="PRO_5005136928"
FT DOMAIN 2..222
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR005604-2"
SQ SEQUENCE 304 AA; 34734 MW; 180E406425942EBD CRC64;
MASLNLIPMS KLRVFLVFCC LALSMVGMVS SASKFDELFQ PSWANDHFIY EGDEVLKMKL
DYNSGAGFQS KSKYMFGKVT VQIKLVEGDS AGTVTAFYMS SDGPTHNEFD FEFLGNTTGE
PYSVQTNLYI NGVGNREQRL NLWFDPTKDF HSYSIHWSPR QVIFSVDETP IREHSNLEHR
GIPFPKDQPM GVYSSIWNAD DWATQGGRVK TDWSHAPFVT SYRGFEIDAC ELPASVAVAD
IARKCSSSNE KRYWWDEPTA GELSVHQSHQ LIWVRANHMF YDYCTDTARF PVAPLECEHH
QHRH
//
