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Database: UniProt
Entry: A0A061DWT1_THECC
LinkDB: A0A061DWT1_THECC
Original site: A0A061DWT1_THECC 
ID   A0A061DWT1_THECC        Unreviewed;       295 AA.
AC   A0A061DWT1;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Xyloglucan endotransglucosylase/hydrolase {ECO:0000256|RuleBase:RU361120};
DE            EC=2.4.1.207 {ECO:0000256|RuleBase:RU361120};
GN   ORFNames=TCM_006329 {ECO:0000313|EMBL:EOX97249.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX97249.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOX97249.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
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; CM001880; EOX97249.1; -; Genomic_DNA.
DR   RefSeq; XP_007041418.1; XM_007041356.2.
DR   AlphaFoldDB; A0A061DWT1; -.
DR   SMR; A0A061DWT1; -.
DR   STRING; 3641.A0A061DWT1; -.
DR   EnsemblPlants; EOX97249; EOX97249; TCM_006329.
DR   EnsemblPlants; Tc02v2_t002400.2; Tc02v2_p002400.2; Tc02v2_g002400.
DR   GeneID; 18607281; -.
DR   Gramene; EOX97249; EOX97249; TCM_006329.
DR   Gramene; Tc02v2_t002400.2; Tc02v2_p002400.2; Tc02v2_g002400.
DR   KEGG; tcc:18607281; -.
DR   eggNOG; ENOG502QQ71; Eukaryota.
DR   HOGENOM; CLU_048041_0_0_1; -.
DR   InParanoid; A0A061DWT1; -.
DR   OMA; IDACVWN; -.
DR   OrthoDB; 337487at2759; -.
DR   Proteomes; UP000026915; Chromosome 2.
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; 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:SF120; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 10-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   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|ARBA:ARBA00023316,
KW   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   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361120};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361120};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361120}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|RuleBase:RU361120"
FT   CHAIN           26..295
FT                   /note="Xyloglucan endotransglucosylase/hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361120"
FT                   /id="PRO_5005102828"
FT   DOMAIN          20..221
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"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-2"
SQ   SEQUENCE   295 AA;  34495 MW;  BAB443CE3F593701 CRC64;
     MSKCFNLLAF IISLLFLNLL RISIASVVST GDFSNDFFVM WAPSHVNTSA DGRERSLKLD
     QESGSGFASN QMFLFGRIDM QIKLVPGNSA GTVLAYYLTS DQPNRDEIDI EFLGNVSGQP
     YIVQTNIYAD GFDNREERIY LWFDPTEDFH TYSVLWNLYQ IMFMVDSIPI RLYRNHADKG
     VAYPRWQPMS IKVSLWNGGS WATRGGLEKI DWSKGPFIAS FKDYKIDACV WQGNPRFCRA
     DSSLNWWNRP RFSTLTRVQK RWFKWVRKYH MVYDYCQDNQ RFQNNLPKEC SLPKY
//
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