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Database: UniProt
Entry: A0A0R0GL47_SOYBN
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ID   A0A0R0GL47_SOYBN        Unreviewed;       283 AA.
AC   A0A0R0GL47;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Xyloglucan endotransglucosylase/hydrolase {ECO:0000256|RuleBase:RU361120};
DE            EC=2.4.1.207 {ECO:0000256|RuleBase:RU361120};
GN   ORFNames=GLYMA_13G103100 {ECO:0000313|EMBL:KRH19136.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH19136.1};
RN   [1] {ECO:0000313|EMBL:KRH19136.1, ECO:0000313|EnsemblPlants:KRH19136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH19136};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH19136.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH19136}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH19136};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH19136.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH19136.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) 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; CM000846; KRH19136.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R0GL47; -.
DR   SMR; A0A0R0GL47; -.
DR   STRING; 3847.A0A0R0GL47; -.
DR   PaxDb; 3847-GLYMA13G00280-1; -.
DR   EnsemblPlants; KRH19136; KRH19136; GLYMA_13G103100.
DR   Gramene; KRH19136; KRH19136; GLYMA_13G103100.
DR   eggNOG; ENOG502QQ71; Eukaryota.
DR   InParanoid; A0A0R0GL47; -.
DR   OMA; GQSRIKW; -.
DR   Proteomes; UP000008827; Chromosome 13.
DR   ExpressionAtlas; A0A0R0GL47; baseline and differential.
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; 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:SF312; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE; 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; 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|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:UP000008827};
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..20
FT                   /evidence="ECO:0000256|RuleBase:RU361120"
FT   CHAIN           21..283
FT                   /note="Xyloglucan endotransglucosylase/hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361120"
FT                   /id="PRO_5014484090"
FT   DOMAIN          17..211
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   ACT_SITE        97
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT   ACT_SITE        101
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-2"
SQ   SEQUENCE   283 AA;  31750 MW;  9B54C73E1BA472D4 CRC64;
     MASEIFLALL ITTFVVAASA GNFNQDFEIT WGDGRAKILN SGELLTLSLD KTSGSGFRSR
     NEYLFGKIDM QLKLVPGNSA GTVTAYYLSS LGDTHDEIDF EFLGNLSGDP YILHTNVFTQ
     GKGNREQQFY LWFDPTQDFH TYSILWNPQS IIFSVDGTPI REFKNLESKG VSFPKNQPMR
     IYSSLWNADD WATRGGLVKT DWSQAPFTAS YRKFNAQACV WTSSSGSSCS SNNPSSNQAW
     LKQSLDSTGQ ARIQWVQKNY MIYNYCTDTK RFPQGLPPEC TIA
//
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