ID   XTH16_ARATH             Reviewed;         291 AA.
AC   Q8LG58; Q9LK45;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase protein 16;
DE            Short=At-XTH16;
DE            Short=XTH-16;
DE            EC=2.4.1.207;
DE   Flags: Precursor;
GN   Name=XTH16; OrderedLocusNames=At3g23730; ORFNames=MYM9.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NOMENCLATURE.
RX   PubMed=12514239; DOI=10.1093/pcp/pcf171;
RA   Rose J.K.C., Braam J., Fry S.C., Nishitani K.;
RT   "The XTH family of enzymes involved in xyloglucan endotransglucosylation
RT   and endohydrolysis: current perspectives and a new unifying nomenclature.";
RL   Plant Cell Physiol. 43:1421-1435(2002).
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 (By
CC       similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AP000377; BAB01849.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76807.1; -; Genomic_DNA.
DR   EMBL; AY084449; AAM61021.1; -; mRNA.
DR   RefSeq; NP_566738.1; NM_113277.3.
DR   AlphaFoldDB; Q8LG58; -.
DR   SMR; Q8LG58; -.
DR   STRING; 3702.AT3G23730.1; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   PaxDb; Q8LG58; -.
DR   PRIDE; Q8LG58; -.
DR   ProteomicsDB; 242429; -.
DR   EnsemblPlants; AT3G23730.1; AT3G23730.1; AT3G23730.
DR   GeneID; 821955; -.
DR   Gramene; AT3G23730.1; AT3G23730.1; AT3G23730.
DR   KEGG; ath:AT3G23730; -.
DR   Araport; AT3G23730; -.
DR   TAIR; locus:2095168; AT3G23730.
DR   eggNOG; ENOG502QQ71; Eukaryota.
DR   HOGENOM; CLU_048041_0_0_1; -.
DR   InParanoid; Q8LG58; -.
DR   OMA; TWGEHRG; -.
DR   OrthoDB; 1209387at2759; -.
DR   PhylomeDB; Q8LG58; -.
DR   BioCyc; ARA:AT3G23730-MON; -.
DR   PRO; PR:Q8LG58; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8LG58; baseline and differential.
DR   Genevisible; Q8LG58; AT.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..291
FT                   /note="Probable xyloglucan endotransglucosylase/hydrolase
FT                   protein 16"
FT                   /id="PRO_0000011816"
FT   DOMAIN          25..215
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        101
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   ACT_SITE        105
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   BINDING         105
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         118..120
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         128..130
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         194..195
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         199
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         277
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   SITE            103
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        223..232
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   DISULFID        272..286
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   CONFLICT        256
FT                   /note="R -> I (in Ref. 3; AAM61021)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   291 AA;  33147 MW;  3AE0B913F783C764 CRC64;
     MGRILNRTVL MTLLVVTMAG TAFSGSFNEE FDLTWGEHRG KIFSGGKMLS LSLDRVSGSG
     FKSKKEYLFG RIDMQLKLVA GNSAGTVTAY YLSSEGPTHD EIDFEFLGNE TGKPYVLHTN
     VFAQGKGNRE QQFYLWFDPT KNFHTYSLVW RPQHIIFMVD NVPIRVFNNA EQLGVPFPKN
     QPMKIYSSLW NADDWATRGG LVKTDWSKAP FTAYYRGFNA AACTVSSGSS FCDPKFKSSF
     TNGESQVANE LNAYGRRRLR WVQKYFMIYD YCSDLKRFPQ GFPPECRKSR V