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Database: UniProt
Entry: A0A0D3EC54_BRAOL
LinkDB: A0A0D3EC54_BRAOL
Original site: A0A0D3EC54_BRAOL 
ID   A0A0D3EC54_BRAOL        Unreviewed;       284 AA.
AC   A0A0D3EC54;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, 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=106316170 {ECO:0000313|EnsemblPlants:Bo9g133240.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo9g133240.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo9g133240.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo9g133240.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
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   RefSeq; XP_013609492.1; XM_013754038.1.
DR   AlphaFoldDB; A0A0D3EC54; -.
DR   STRING; 109376.A0A0D3EC54; -.
DR   GlyCosmos; A0A0D3EC54; 1 site, No reported glycans.
DR   EnsemblPlants; Bo9g133240.1; Bo9g133240.1; Bo9g133240.
DR   GeneID; 106316170; -.
DR   Gramene; Bo9g133240.1; Bo9g133240.1; Bo9g133240.
DR   KEGG; boe:106316170; -.
DR   eggNOG; ENOG502QQ71; Eukaryota.
DR   HOGENOM; CLU_048041_0_0_1; -.
DR   OMA; KMQPMRL; -.
DR   OrthoDB; 337487at2759; -.
DR   Proteomes; UP000032141; Chromosome C9.
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:SF189; 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; 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:UP000032141};
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..26
FT                   /evidence="ECO:0000256|RuleBase:RU361120"
FT   CHAIN           27..284
FT                   /note="Xyloglucan endotransglucosylase/hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361120"
FT                   /id="PRO_5005113347"
FT   DOMAIN          23..217
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   ACT_SITE        103
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT   ACT_SITE        107
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-2"
SQ   SEQUENCE   284 AA;  32602 MW;  84B1A10A141D86FC CRC64;
     MDRHSTLIIS ILLTALTTTF FSPVYAGTFD RDFDITWGGG RGKVLNNGEL LTLSLDRASG
     SGFQSKKEYL FGKIDMQIKL VPGNSAGTVT TYYLKSKGDT WDEIDFEFLG NLTGDPYVMH
     TNVYTKGKGD REQQFHLWFD PTADFHTYSV LWNHHHIVFL VDGIPIRQFK NLEHRRIPYP
     KMQPMRLYSS LWNADQWATR GGLVKTDWSK APFTASYRNF RADACVSHTG KPSCPAGSPR
     WLSHRFDLTA ENNMRVVQRK FMVYNYCTDS KRFPQGFPKE CGIH
//
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