XTH31_ARATH
ID XTH31_ARATH Reviewed; 293 AA.
AC P93046; Q9LXH6;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase protein 31 {ECO:0000303|PubMed:12514239};
DE Short=At-XTH31 {ECO:0000303|PubMed:12514239};
DE Short=AtXTR8;
DE Short=XTH-31;
DE EC=2.4.1.207 {ECO:0000269|PubMed:23104861};
DE EC=3.2.1.151 {ECO:0000269|PubMed:23104861};
DE Flags: Precursor;
GN Name=XTH31 {ECO:0000303|PubMed:12514239}; Synonyms=ATXG, XTR8;
GN OrderedLocusNames=At3g44990; ORFNames=F14D17.60;
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 [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC TISSUE=Seed;
RA Aubert D., Herzog M.;
RT "A new cDNA encoding a xyloglucan endo-transglycosylase-related polypeptide
RT (AtXTR8) preferentially expressed in seedling, root and stem of Arabidopsis
RT thaliana.";
RL Plant Sci. 121:187-196(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [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).
RN [7]
RP INDUCTION BY ALUMINUM.
RX PubMed=21285327; DOI=10.1104/pp.111.172221;
RA Yang J.L., Zhu X.F., Peng Y.X., Zheng C., Li G.X., Liu Y., Shi Y.Z.,
RA Zheng S.J.;
RT "Cell wall hemicellulose contributes significantly to aluminum adsorption
RT and root growth in Arabidopsis.";
RL Plant Physiol. 155:1885-1892(2011).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY ALUMINUM.
RX PubMed=23204407; DOI=10.1105/tpc.112.106039;
RA Zhu X.F., Shi Y.Z., Lei G.J., Fry S.C., Zhang B.C., Zhou Y.H., Braam J.,
RA Jiang T., Xu X.Y., Mao C.Z., Pan Y.J., Yang J.L., Wu P., Zheng S.J.;
RT "XTH31, encoding an in vitro XEH/XET-active enzyme, regulates aluminum
RT sensitivity by modulating in vivo XET action, cell wall xyloglucan content,
RT and aluminum binding capacity in Arabidopsis.";
RL Plant Cell 24:4731-4747(2012).
RN [9]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23104861; DOI=10.1104/pp.112.207308;
RA Kaewthai N., Gendre D., Eklof J.M., Ibatullin F.M., Ezcurra I.,
RA Bhalerao R.P., Brumer H.;
RT "Group III-A XTH genes of Arabidopsis encode predominant xyloglucan
RT endohydrolases that are dispensable for normal growth.";
RL Plant Physiol. 161:440-454(2013).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=25446234; DOI=10.1016/j.phytochem.2014.09.020;
RA Shi Y.Z., Zhu X.F., Miller J.G., Gregson T., Zheng S.J., Fry S.C.;
RT "Distinct catalytic capacities of two aluminium-repressed Arabidopsis
RT thaliana xyloglucan endotransglucosylase/hydrolases, XTH15 and XTH31,
RT heterologously produced in Pichia.";
RL Phytochemistry 112:160-169(2015).
RN [11]
RP INTERACTION WITH XTH17.
RX PubMed=24948835; DOI=10.1104/pp.114.243790;
RA Zhu X.F., Wan J.X., Sun Y., Shi Y.Z., Braam J., Li G.X., Zheng S.J.;
RT "Xyloglucan endotransglucosylase-hydrolase17 interacts with xyloglucan
RT endotransglucosylase-hydrolase31 to confer xyloglucan endotransglucosylase
RT action and affect aluminum sensitivity in Arabidopsis.";
RL Plant Physiol. 165:1566-1574(2014).
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 Involved in the accumulation of hemicelluloses. Has a high XEH activity
CC and only a slight XET activity in vitro, but the main in planta
CC activity seems to be XET, thus controlling aluminum sensitivity
CC (PubMed:23204407, PubMed:23104861, PubMed:25446234). Acceptor
CC preferences are XXXGol = XXFGol > XXLGol > XLLGol = XLFGol
CC (PubMed:25446234). {ECO:0000269|PubMed:23104861,
CC ECO:0000269|PubMed:23204407, ECO:0000269|PubMed:25446234}.
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:0000269|PubMed:23104861};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=xyloglucan + H2O = xyloglucan oligosaccharides.; EC=3.2.1.151;
CC Evidence={ECO:0000269|PubMed:23104861, ECO:0000269|PubMed:25446234};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=86 uM for XXXGol {ECO:0000269|PubMed:25446234};
CC Note=KM for xyloglucan as donor substrate is 1.6 mg/ml. KM is quoted
CC in mg/ml, not uM, because XTHs are able to utilise any segment of the
CC polysaccharide chain equally well, not just one site per molecule as
CC with the acceptor. {ECO:0000269|PubMed:25446234};
CC pH dependence:
CC Optimum pH is 5 for the XET activity. Optimum pH is 4.5 - 4.75 for
CC the XEH activity. {ECO:0000269|PubMed:23104861,
CC ECO:0000269|PubMed:25446234};
CC -!- SUBUNIT: Interacts with XTH17. The formation of an XTH17-XTH31 dimer
CC may be required for XET activity. {ECO:0000269|PubMed:24948835}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC extracellular space, apoplast {ECO:0000305}. Cell membrane
CC {ECO:0000269|PubMed:23204407}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in root (PubMed:11673616,
CC Ref.1). Weakly expressed in influorescence stems (PubMed:11673616).
CC Expressed in root tips and elongation zones, stems, young leaves,
CC flowers and siliques (PubMed:23204407). Expressed in root, hypocotyl,
CC and etiolated whole seedlings (PubMed:23104861).
CC {ECO:0000269|PubMed:11673616, ECO:0000269|PubMed:23104861,
CC ECO:0000269|PubMed:23204407, ECO:0000269|Ref.1}.
CC -!- DEVELOPMENTAL STAGE: Expressed in germinating seeds from 24 hours after
CC imbibation, and reaches a maximum level at 72 hours. After 96 hours, it
CC then decreases. {ECO:0000269|Ref.1}.
CC -!- INDUCTION: Up-regulated by gibberellins (Probable). Not induced by
CC auxin (Ref.1). Down-regulated by aluminum (PubMed:21285327,
CC PubMed:23204407). {ECO:0000269|PubMed:21285327,
CC ECO:0000269|PubMed:23204407, ECO:0000269|Ref.1, ECO:0000305}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth, decreased cell wall xyloglucan
CC content and increased aluminum resistance (PubMed:23204407). No visible
CC phenotype under normal growth conditions (PubMed:23104861).
CC {ECO:0000269|PubMed:23104861, ECO:0000269|PubMed:23204407}.
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; X92975; CAA63553.1; -; mRNA.
DR EMBL; AL353992; CAB89314.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77976.1; -; Genomic_DNA.
DR EMBL; AY056163; AAL07012.1; -; mRNA.
DR EMBL; AY136454; AAM97119.1; -; mRNA.
DR EMBL; BT006326; AAP13434.1; -; mRNA.
DR PIR; T48975; T48975.
DR RefSeq; NP_190085.1; NM_114368.3.
DR AlphaFoldDB; P93046; -.
DR SMR; P93046; -.
DR BioGRID; 8954; 1.
DR STRING; 3702.AT3G44990.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; P93046; -.
DR PRIDE; P93046; -.
DR ProteomicsDB; 243029; -.
DR EnsemblPlants; AT3G44990.1; AT3G44990.1; AT3G44990.
DR GeneID; 823634; -.
DR Gramene; AT3G44990.1; AT3G44990.1; AT3G44990.
DR KEGG; ath:AT3G44990; -.
DR Araport; AT3G44990; -.
DR TAIR; locus:2075919; AT3G44990.
DR eggNOG; ENOG502QQC7; Eukaryota.
DR HOGENOM; CLU_048041_1_1_1; -.
DR InParanoid; P93046; -.
DR OMA; PKIHRIY; -.
DR OrthoDB; 1209387at2759; -.
DR PhylomeDB; P93046; -.
DR BioCyc; ARA:AT3G44990-MON; -.
DR BRENDA; 2.4.1.207; 399.
DR BRENDA; 3.2.1.151; 399.
DR SABIO-RK; P93046; -.
DR PRO; PR:P93046; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P93046; baseline and differential.
DR Genevisible; P93046; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030247; F:polysaccharide binding; ISS:UniProtKB.
DR GO; GO:0033946; F:xyloglucan-specific endo-beta-1,4-glucanase activity; IDA:TAIR.
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 1: Evidence at protein level;
KW Apoplast; Cell membrane; Cell wall; Cell wall biogenesis/degradation;
KW Disulfide bond; Glycosidase; Hydrolase; Membrane; Reference proteome;
KW Secreted; Signal; Transferase.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..293
FT /note="Xyloglucan endotransglucosylase/hydrolase protein
FT 31"
FT /id="PRO_0000011831"
FT DOMAIN 29..230
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 118
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 131..133
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 141..148
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 209..210
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 285
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 116
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 238..246
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 280..293
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CONFLICT 11
FT /note="L -> V (in Ref. 1; CAA63553)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="S -> T (in Ref. 1; CAA63553)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 33541 MW; D999B4C62C5ABCA8 CRC64;
MALSLIFLAL LVLCPSSGHS QRSPSPGYYP SSRVPTSPFD REFRTLWGSQ HQRREQDVVT
LWLDKSTGSG FKSLRPYRSG YFGASIKLQP GFTAGVDTSL YLSNNQEHPG DHDEVDIEFL
GTTPGKPYSL QTNVFVRGSG DRNVIGREMK FTLWFDPTQD FHHYAILWNP NQIVFFVDDV
PIRTYNRKNE AIFPTRPMWV YGSIWDASDW ATENGRIKAD YRYQPFVAKY KNFKLAGCTA
DSSSSCRPPS PAPMRNRGLS RQQMAALTWA QRNFLVYNYC HDPKRDHTQT PEC
