XTH_BRAOB
ID XTH_BRAOB Reviewed; 295 AA.
AC Q6YDN9;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase;
DE EC=2.4.1.207;
DE AltName: Full=BobXET16A;
DE Flags: Precursor;
GN Name=XET16A;
OS Brassica oleracea var. botrytis (Cauliflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3715;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-38 AND 75-133, MASS
RP SPECTROMETRY, AND GLYCOSYLATION.
RX PubMed=12826015; DOI=10.1042/bj20030485;
RA Henriksson H., Denman S.E., Campuzano I.D.G., Ademark P., Master E.R.,
RA Teeri T.T., Brumer H. III;
RT "N-linked glycosylation of native and recombinant cauliflower xyloglucan
RT endotransglycosylase 16A.";
RL Biochem. J. 375:61-73(2003).
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 -!- 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 -!- 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}.
CC -!- PTM: The N-glycan consists of an (GlcNAc)2(Hex)6 oligosaccharide; not
CC essential for its enzymatic activity.
CC -!- MASS SPECTROMETRY: Mass=33115; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12826015};
CC -!- MISCELLANEOUS: No hydrolytic activity detected in vitro.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 1
CC subfamily. {ECO:0000305}.
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DR EMBL; AY156708; AAO00727.1; -; mRNA.
DR AlphaFoldDB; Q6YDN9; -.
DR SMR; Q6YDN9; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR GlyConnect; 629; 6 N-Linked glycans.
DR iPTMnet; Q6YDN9; -.
DR PRIDE; Q6YDN9; -.
DR BRENDA; 2.4.1.207; 948.
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 1: Evidence at protein level;
KW Apoplast; Cell wall; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Secreted; Signal; Transferase.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:12826015"
FT CHAIN 24..295
FT /note="Xyloglucan endotransglucosylase/hydrolase"
FT /id="PRO_0000011834"
FT DOMAIN 25..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:0000269|PubMed:12826015"
FT DISULFID 230..239
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 276..289
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 295 AA; 34105 MW; 15054A3E4929BD4E CRC64;
MAVSSTPWAL VALFLMASST VMAIPPRKAI DVPFGRNYVP TWAFDHQKQL NGGSELQLIL
DKYTGTGFQS KGSYLFGHFS MHIKLPAGDT AGVVTAFYLS STNNEHDEID FEFLGNRTGQ
PVILQTNVFT GGKGNREQRI YLWFDPSKAY HTYSVLWNLY QIVFFVDNIP IRVFKNAKDL
GVRFPFNQPM KLYSSLWNAD DWATRGGLEK TNWANAPFIA SYRGFHIDGC QASVEAKYCA
TQGRMWWDQN EFRDLDAEQY RRLKWVRMKW TIYNYCTDRT RFPVMPAECR RDRDV
