XTH1_SOYBN
ID XTH1_SOYBN Reviewed; 296 AA.
AC Q39857; C6TM30;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase 1 {ECO:0000305};
DE EC=2.4.1.207 {ECO:0000250|UniProtKB:Q38857};
DE Flags: Precursor;
GN Name=XTH1 {ECO:0000305};
GN Synonyms=EXT {ECO:0000303|PubMed:8244968}, XTH {ECO:0000305};
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].
RA Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-296.
RX PubMed=8244968; DOI=10.1016/s0021-9258(19)74400-7;
RA Okazawa K., Sato Y., Nakagawa T., Asada K., Kato I., Tomita E.,
RA Nishitani K.;
RT "Molecular cloning and cDNA sequencing of endoxyloglucan transferase, a
RT novel class of glycosyltransferase that mediates molecular grafting between
RT matrix polysaccharides in plant cell walls.";
RL J. Biol. Chem. 268:25364-25368(1993).
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 -!- 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. XTH group 1
CC subfamily. {ECO:0000305}.
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DR EMBL; BT098780; ACU23972.1; -; mRNA.
DR EMBL; D16455; BAA03922.1; -; mRNA.
DR PIR; B49539; B49539.
DR RefSeq; NP_001242655.1; NM_001255726.2.
DR AlphaFoldDB; Q39857; -.
DR SMR; Q39857; -.
DR STRING; 3847.GLYMA16G04950.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PRIDE; Q39857; -.
DR GeneID; 547775; -.
DR KEGG; gmx:547775; -.
DR eggNOG; ENOG502QQUC; Eukaryota.
DR HOGENOM; CLU_048041_0_0_1; -.
DR InParanoid; Q39857; -.
DR OrthoDB; 1209387at2759; -.
DR Proteomes; UP000008827; Unplaced.
DR Genevisible; Q39857; GM.
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: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 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; PTHR31062; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF06955; XET_C; 1.
DR PIRSF; PIRSF005604; XET; 1.
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; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..296
FT /note="Xyloglucan endotransglucosylase/hydrolase 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000011839"
FT DOMAIN 24..222
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 112
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 125..127
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 135..137
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 201..202
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 206
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 281
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 110
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 230..239
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 276..290
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CONFLICT 2..5
FT /note="GSSS -> IPVF (in Ref. 2; BAA03922)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="M -> V (in Ref. 2; BAA03922)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="P -> L (in Ref. 2; BAA03922)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="P -> S (in Ref. 2; BAA03922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 34435 MW; 9BF579B92A56D07F CRC64;
MGSSSSMWTV CVILASLASA ALCANPRRPV DVQFGRNYVP TWAFDHIKYF NGGSDIQPHL
DKYTGTGFQP KGSYLFGHFS MYIKMVPGDS AGTVTAFYLS SQNAEHDEID FEFLGNRTGQ
PYILQTNVFT GGKGDREQRI YLWFDPTKEY HRYSILWNLY QIVFFVDEVP IRVFKNSKDL
GVKFPFDQPM KIYNSLWNAD DWATRGGLEK TDWSKAPFIA AYKGFHIDGC EASVNAKFCD
TQGKRWWDQP EFRDLDAAQW RRLRWVRQKY TIYNYCTDTK RYPHISPPEC KRDRDI
