XTH32_ARATH
ID XTH32_ARATH Reviewed; 299 AA.
AC Q9SJL9;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase protein 32;
DE Short=At-XTH32;
DE Short=XTH-32;
DE EC=2.4.1.207;
DE Flags: Precursor;
GN Name=XTH32; OrderedLocusNames=At2g36870; ORFNames=T1J8.5;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [5]
RP TISSUE SPECIFICITY.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SJL9-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in stems.
CC {ECO:0000269|PubMed:11673616}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: In contrast to group 1 and group 2
CC endotransglucosylase/hydrolase proteins, it may not contain the ligase
CC activity, and may catalyze endohydrolysis xyloglucan polymers only.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 3
CC subfamily. {ECO:0000305}.
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DR EMBL; AC006922; AAD31572.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09308.1; -; Genomic_DNA.
DR EMBL; AY045840; AAK76514.1; -; mRNA.
DR EMBL; AY133846; AAM91780.1; -; mRNA.
DR EMBL; AY088557; AAM66089.1; -; mRNA.
DR PIR; F84785; F84785.
DR RefSeq; NP_181224.1; NM_129242.3. [Q9SJL9-1]
DR AlphaFoldDB; Q9SJL9; -.
DR SMR; Q9SJL9; -.
DR STRING; 3702.AT2G36870.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; Q9SJL9; -.
DR PRIDE; Q9SJL9; -.
DR ProteomicsDB; 242470; -. [Q9SJL9-1]
DR EnsemblPlants; AT2G36870.1; AT2G36870.1; AT2G36870. [Q9SJL9-1]
DR GeneID; 818259; -.
DR Gramene; AT2G36870.1; AT2G36870.1; AT2G36870. [Q9SJL9-1]
DR KEGG; ath:AT2G36870; -.
DR Araport; AT2G36870; -.
DR TAIR; locus:2058006; AT2G36870.
DR eggNOG; ENOG502QQC7; Eukaryota.
DR HOGENOM; CLU_048041_1_1_1; -.
DR InParanoid; Q9SJL9; -.
DR OMA; RCHPVTA; -.
DR PhylomeDB; Q9SJL9; -.
DR BioCyc; ARA:AT2G36870-MON; -.
DR BRENDA; 3.2.1.151; 399.
DR PRO; PR:Q9SJL9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJL9; baseline and differential.
DR Genevisible; Q9SJL9; 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:0016998; P:cell wall macromolecule catabolic process; IMP:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0010411; P:xyloglucan metabolic process; IEA:InterPro.
DR InterPro; IPR044791; Beta-glucanase/XTH.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
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; PS51762; GH16_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Apoplast; Cell wall;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..299
FT /note="Probable xyloglucan endotransglucosylase/hydrolase
FT protein 32"
FT /id="PRO_0000011832"
FT DOMAIN 25..234
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 118
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT ACT_SITE 122
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 122
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 145..152
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 213..214
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 289
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 120
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 242..250
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 284..297
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 299 AA; 34482 MW; F14F02472ADAE61E CRC64;
MGNSLISLLS IFHLLVLWGS SVNAYWPPSP GYWPSSKVGS LNFYKGFRNL WGPQHQRMDQ
NALTIWLDRT SGSGFKSVKP FRSGYFGANI KLQPGYTAGV ITSLYLSNNE AHPGFHDEVD
IEFLGTTFGK PYTLQTNVYI RGSGDGKIIG REMKFRLWFD PTKDFHHYAI LWSPREIIFL
VDDIPIRRYP KKSASTFPLR PMWLYGSIWD ASSWATEDGK YKADYKYQPF TAKYTNFKAL
GCTAYSSARC YPLSASPYRS GGLTRQQHQA MRWVQTHSMV YNYCKDYKRD HSLTPECWR
