XTH5_ARATH
ID XTH5_ARATH Reviewed; 293 AA.
AC Q9XIW1;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase protein 5;
DE Short=At-XTH5;
DE Short=XTH-5;
DE EC=2.4.1.207;
DE Flags: Precursor;
GN Name=XTH5; Synonyms=EXGT-A4, XTR12; OrderedLocusNames=At5g13870;
GN ORFNames=MAC12.33;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10557219; DOI=10.1104/pp.121.3.715;
RA Akamatsu T., Hanzawa Y., Ohtake Y., Takahashi T., Nishitani K., Komeda Y.;
RT "Expression of endoxyloglucan transferase genes in acaulis mutants of
RT Arabidopsis.";
RL Plant Physiol. 121:715-721(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Okamoto S., Hayashida N., Shinozaki K., Nishitani K.;
RT "Endoxyloglucan transferase homologue from Arabidopsis thaliana.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [4]
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 [5]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11673616; DOI=10.1093/pcp/pce154;
RA Yokoyama R., Nishitani K.;
RT "A comprehensive expression analysis of all members of a gene family
RT encoding cell-wall enzymes allowed us to predict cis-regulatory regions
RT involved in cell-wall construction in specific organs of Arabidopsis.";
RL Plant Cell Physiol. 42:1025-1033(2001).
RN [6]
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 -!- TISSUE SPECIFICITY: Root specific. {ECO:0000269|PubMed:10557219,
CC ECO:0000269|PubMed:11673616}.
CC -!- INDUCTION: By brassinolide. Strongly down-regulated by abscisic acid.
CC {ECO:0000269|PubMed:11673616}.
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 1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF163822; AAD45126.1; -; Genomic_DNA.
DR EMBL; AB026486; BAA81669.1; -; mRNA.
DR EMBL; AB005230; BAB11115.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91952.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69716.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69717.1; -; Genomic_DNA.
DR RefSeq; NP_001331375.1; NM_001343298.1.
DR RefSeq; NP_001331376.1; NM_001343297.1.
DR RefSeq; NP_196891.1; NM_121390.5.
DR AlphaFoldDB; Q9XIW1; -.
DR SMR; Q9XIW1; -.
DR STRING; 3702.AT5G13870.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; Q9XIW1; -.
DR PRIDE; Q9XIW1; -.
DR ProteomicsDB; 242404; -.
DR EnsemblPlants; AT5G13870.1; AT5G13870.1; AT5G13870.
DR EnsemblPlants; AT5G13870.2; AT5G13870.2; AT5G13870.
DR EnsemblPlants; AT5G13870.3; AT5G13870.3; AT5G13870.
DR GeneID; 831233; -.
DR Gramene; AT5G13870.1; AT5G13870.1; AT5G13870.
DR Gramene; AT5G13870.2; AT5G13870.2; AT5G13870.
DR Gramene; AT5G13870.3; AT5G13870.3; AT5G13870.
DR KEGG; ath:AT5G13870; -.
DR Araport; AT5G13870; -.
DR TAIR; locus:2159118; AT5G13870.
DR eggNOG; ENOG502QQUC; Eukaryota.
DR HOGENOM; CLU_048041_0_0_1; -.
DR InParanoid; Q9XIW1; -.
DR OMA; CTDRERY; -.
DR OrthoDB; 1209387at2759; -.
DR PhylomeDB; Q9XIW1; -.
DR BioCyc; ARA:AT5G13870-MON; -.
DR PRO; PR:Q9XIW1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XIW1; baseline and differential.
DR Genevisible; Q9XIW1; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..293
FT /note="Probable xyloglucan endotransglucosylase/hydrolase
FT protein 5"
FT /id="PRO_0000011805"
FT DOMAIN 23..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 279
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"
FT DISULFID 228..237
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 274..287
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 293 AA; 33949 MW; 1025767DDA2BA9F4 CRC64;
MGRLSSTLCL TFLILATVAF GVPPKKSINV PFGRNYFPTW AFDHIKYLNG GSEVHLVLDK
YTGTGFQSKG SYLFGHFSMH IKMVAGDSAG TVTAFYLSSQ NSEHDEIDFE FLGNRTGQPY
ILQTNVFTGG AGNREQRINL WFDPSKDYHS YSVLWNMYQI VFFVDDVPIR VFKNSKDVGV
KFPFNQPMKI YSSLWNADDW ATRGGLEKTN WEKAPFVASY RGFHVDGCEA SVNAKFCETQ
GKRWWDQKEF QDLDANQYKR LKWVRKRYTI YNYCTDRVRF PVPPPECRRD RDI
