ID A2ZZJ6_ORYSJ Unreviewed; 290 AA. AC A2ZZJ6; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 29-OCT-2014, entry version 38. DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase {ECO:0000256|RuleBase:RU361120}; DE EC=2.4.1.207 {ECO:0000256|RuleBase:RU361120}; GN ORFNames=OsJ_04071 {ECO:0000313|EMBL:EAZ14143.1}; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=39947 {ECO:0000313|EMBL:EAZ14143.1, ECO:0000313|Proteomes:UP000000763}; RN [1] {ECO:0000313|EMBL:EAZ14143.1, ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., RA Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., RA Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., RA Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., RA Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., RA Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., RA Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., RA Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., RA Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., RA Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., RA Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J., RA Samudrala R., Wang J., Wong G.K., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). 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 -!- CATALYTIC ACTIVITY: Breaks a beta-(1->4) bond in the backbone of a CC xyloglucan and transfers the xyloglucanyl segment on to O-4 of the CC non-reducing terminal glucose residue of an acceptor, which can be CC a xyloglucan or an oligosaccharide of xyloglucan. 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 CC its enzymatic activity. {ECO:0000256|RuleBase:RU361120}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. CC {ECO:0000256|RuleBase:RU361120}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CM000138; EAZ14143.1; -; Genomic_DNA. DR Gramene; A2ZZJ6; -. DR ExpressionAtlas; A2ZZJ6; baseline. DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell. DR GO; GO:0005618; C:cell wall; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0006073; P:cellular glucan metabolic process; IEA:InterPro. DR Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR008264; Beta_glucanase. DR InterPro; IPR013320; ConA-like_dom. DR InterPro; IPR000757; Glyco_hydro_16. DR InterPro; IPR008263; Glycoside_hydrolase_16_AS. DR InterPro; IPR016455; XET. DR InterPro; IPR010713; XET_C. 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; SSF49899; 1. DR PROSITE; PS01034; GLYCOSYL_HYDROL_F16; 1. PE 3: Inferred from homology; 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|RuleBase:RU361120}; KW Hydrolase {ECO:0000256|RuleBase:RU361120}; KW Secreted {ECO:0000256|RuleBase:RU361120}; KW Signal {ECO:0000256|RuleBase:RU361120}; KW Transferase {ECO:0000256|RuleBase:RU361120}. SQ SEQUENCE 290 AA; 32075 MW; B9CE677AF2013E50 CRC64; MAKHLALSVA AAVAVSWLAA SSAAAAGFYE KFDVVGAGDH VRVVSDDGKT QQVALTLDRS SGSGFTSKDT YLFGEFSVQM KLVGGNSAGT VTSFYLSSGE GDGHDEIDIE FMGNLSGNPY VMNTNVWANG DGKKEHQFYL WFDPTADFHT YKIIWNPQNI IFQVDDVPVR TFKKYDDLAY PQSKPMRLDA TLWDGSYWAT RHGDVKIDWS GAPFVVSYRG YSTNACVNNN PAGGWSSSWC PEGTSAWIHR ELDGAELGTV AWAERNYMSY NYCADGWRFP QGFPAECYRK //