XTH2_SOYBN
ID XTH2_SOYBN Reviewed; 283 AA.
AC P35694; C6TH31;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase 2 {ECO:0000250|UniProtKB:Q38857};
DE EC=2.4.1.207 {ECO:0000250|UniProtKB:Q38857};
DE AltName: Full=Brassinosteroid-regulated protein BRU1 {ECO:0000303|PubMed:8115544};
DE Flags: Precursor;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND INDUCTION BY
RP BRASSINOSTEROIDS.
RC TISSUE=Epicotyl;
RX PubMed=8115544; DOI=10.1104/pp.104.1.161;
RA Zurek D.M., Clouse S.D.;
RT "Molecular cloning and characterization of a brassinosteroid-regulated gene
RT from elongating soybean (Glycine max L.) epicotyls.";
RL Plant Physiol. 104:161-170(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL Submitted (AUG-2009) 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:0000250|UniProtKB:Q38857}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and
CC transfers the xyloglucanyl segment on to O-4 of the non-reducing
CC terminal glucose residue of an acceptor, which can be a xyloglucan or
CC an oligosaccharide of xyloglucan.; EC=2.4.1.207;
CC Evidence={ECO:0000250|UniProtKB:Q38857};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC extracellular space, apoplast {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed at highest levels in epicotyls and
CC hypocotyls of 14-day seedlings. Detected at low levels in stem apices
CC and root tips of 14-day seedlings, and in 2-day etiolated seedlings.
CC Not detected in 75-day plants. {ECO:0000269|PubMed:8115544}.
CC -!- INDUCTION: Up-regulated by brassinosteroids, at a post-transcriptional
CC level. {ECO:0000269|PubMed:8115544}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000250|UniProtKB:Q38857}.
CC -!- PTM: N-glycosylated; not essential for its enzymatic activity.
CC {ECO:0000250|UniProtKB:Q9ZSU4}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR EMBL; L22162; AAA81350.1; -; mRNA.
DR EMBL; BT096944; ACU21133.1; -; mRNA.
DR PIR; T07678; T07678.
DR RefSeq; NP_001238152.1; NM_001251223.1.
DR AlphaFoldDB; P35694; -.
DR SMR; P35694; -.
DR STRING; 3847.GLYMA08G11300.2; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PRIDE; P35694; -.
DR EnsemblPlants; KRH42721; KRH42721; GLYMA_08G107300.
DR GeneID; 547802; -.
DR Gramene; KRH42721; KRH42721; GLYMA_08G107300.
DR KEGG; gmx:547802; -.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR OMA; EWHTTEL; -.
DR OrthoDB; 1209387at2759; -.
DR Proteomes; UP000008827; Chromosome 8.
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:0030247; F:polysaccharide binding; ISS:UniProtKB.
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:0010411; P:xyloglucan metabolic process; IEA:InterPro.
DR CDD; cd02176; GH16_XET; 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; PTHR31062; 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; SSF49899; 1.
DR PROSITE; PS01034; GH16_1; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 2: Evidence at transcript level;
KW Apoplast; Cell wall; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..283
FT /note="Xyloglucan endotransglucosylase/hydrolase 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000011800"
FT DOMAIN 31..220
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 110
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 110
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 123..125
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 133..135
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 199..200
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 204
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 272
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 108
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 267..281
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 283 AA; 32255 MW; C248810EC7835737 CRC64;
MAPSSAHNNG FYVLMLVGIV VSTMVATCAG SFYQDFDLTW GGDRAKIFNG GQLLSLSLDK
VSGSGFKSKK EYLFGRIDMQ LKLVAGNSAG TVTAYYLSSQ GPTHDEIDFE FLGNLSGDPY
ILHTNIFTQG KGNREQQFYL WFDPTRNFHT YSIIWKPQHI IFLVDNTPIR VFKNAEPLGV
PFPKNQPMRI YSSLWNADDW ATRGGLVKTD WSKAPFTAYY RNFKAIEFSS KSSISNSGAE
YEANELDAYS RRRLRWVQKY FMIYNYCSDL KRFPQGLPAE CKR
