GenomeNet

Database: UniProt
Entry: Q84L65_PYRCO
LinkDB: Q84L65_PYRCO
Original site: Q84L65_PYRCO 
ID   Q84L65_PYRCO            Unreviewed;       337 AA.
AC   Q84L65;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Xyloglucan endotransglucosylase/hydrolase {ECO:0000256|RuleBase:RU361120};
DE            EC=2.4.1.207 {ECO:0000256|RuleBase:RU361120};
GN   Name=PC-XET1 {ECO:0000313|EMBL:BAC58038.1};
OS   Pyrus communis (Pear) (Pyrus domestica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX   NCBI_TaxID=23211 {ECO:0000313|EMBL:BAC58038.1};
RN   [1] {ECO:0000313|EMBL:BAC58038.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Softening fruit {ECO:0000313|EMBL:BAC58038.1};
RA   Hiwasa K., Nakano R., Inaba A., Kubo Y.;
RT   "Expression analysis of genes encoding xyloglucan endotransglycosylase
RT   during ripening in pear fruit.";
RL   Submitted (NOV-2002) 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; AB095368; BAC58038.1; -; mRNA.
DR   AlphaFoldDB; Q84L65; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GlyCosmos; Q84L65; 1 site, No reported glycans.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR008263; GH16_AS.
DR   InterPro; IPR010713; XET_C.
DR   InterPro; IPR016455; XTH.
DR   PANTHER; PTHR31062; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 8-RELATED; 1.
DR   PANTHER; PTHR31062:SF243; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE-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; PS01034; GH16_1; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   2: Evidence at transcript level;
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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361120};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361120};
KW   Membrane {ECO:0000256|SAM:Phobius};
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};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        43..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          61..258
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   ACT_SITE        144
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT   ACT_SITE        148
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-2"
SQ   SEQUENCE   337 AA;  38834 MW;  285D64530B39CFD1 CRC64;
     MQIKSHTTNR AALLSFFLIT PQSVSLSLPL LLCAGEKMAS CKQWTVFLSL LCLVSATMAA
     PLKKPVAVPF GRNYMPTWAF DHIKYFNGGK EIQLHLDKYT GTGFQSKGNY LFGHFHMQIK
     MVPGDSAGTV TAYYLSSQNN EHDEIDFEFL GNRTGQPYIL QTNVFTGGKG DREQRIFLWF
     DPTAAYHSYA VLWNLYQIVF LVDDIPIRVF KNSKDLGVKF PFNQPMKLYS SLWNADDWAT
     RGGLEKTDWS KAPFIASYRG FHIDGCEASV EAKFCATQGK RWWDQKEFQD LDAQQWRRLR
     WVRRKFTIYN YCMTESDTLL CHRSARGTET YNTKSKL
//
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