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Xyloglucan endotransglucosylase/hydrolase protein 31 (At-XTH31) (AtXTR8) (XTH-31) (EC 2.4.1.207) (EC 3.2.1.151)

 XTH31_ARATH             Reviewed;         293 AA.
P93046; Q9LXH6;
28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
28-NOV-2003, sequence version 2.
22-NOV-2017, entry version 128.
RecName: Full=Xyloglucan endotransglucosylase/hydrolase protein 31 {ECO:0000303|PubMed:12514239};
Short=At-XTH31 {ECO:0000303|PubMed:12514239};
Short=AtXTR8;
Short=XTH-31;
EC=2.4.1.207 {ECO:0000269|PubMed:23104861};
EC=3.2.1.151 {ECO:0000269|PubMed:23104861};
Flags: Precursor;
Name=XTH31 {ECO:0000303|PubMed:12514239}; Synonyms=ATXG, XTR8;
OrderedLocusNames=At3g44990; ORFNames=F14D17.60;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
AND INDUCTION.
TISSUE=Seed;
Aubert D., Herzog M.;
"A new cDNA encoding a xyloglucan endo-transglycosylase-related
polypeptide (AtXTR8) preferentially expressed in seedling, root and
stem of Arabidopsis thaliana.";
Plant Sci. 121:187-196(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
TISSUE SPECIFICITY.
PubMed=11673616; DOI=10.1093/pcp/pce154;
Yokoyama R., Nishitani K.;
"A comprehensive expression analysis of all members of a gene family
encoding cell-wall enzymes allowed us to predict cis-regulatory
regions involved in cell-wall construction in specific organs of
Arabidopsis.";
Plant Cell Physiol. 42:1025-1033(2001).
[6]
NOMENCLATURE.
PubMed=12514239; DOI=10.1093/pcp/pcf171;
Rose J.K.C., Braam J., Fry S.C., Nishitani K.;
"The XTH family of enzymes involved in xyloglucan
endotransglucosylation and endohydrolysis: current perspectives and a
new unifying nomenclature.";
Plant Cell Physiol. 43:1421-1435(2002).
[7]
INDUCTION BY ALUMINUM.
PubMed=21285327; DOI=10.1104/pp.111.172221;
Yang J.L., Zhu X.F., Peng Y.X., Zheng C., Li G.X., Liu Y., Shi Y.Z.,
Zheng S.J.;
"Cell wall hemicellulose contributes significantly to aluminum
adsorption and root growth in Arabidopsis.";
Plant Physiol. 155:1885-1892(2011).
[8]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INDUCTION BY ALUMINUM.
PubMed=23204407; DOI=10.1105/tpc.112.106039;
Zhu X.F., Shi Y.Z., Lei G.J., Fry S.C., Zhang B.C., Zhou Y.H.,
Braam J., Jiang T., Xu X.Y., Mao C.Z., Pan Y.J., Yang J.L., Wu P.,
Zheng S.J.;
"XTH31, encoding an in vitro XEH/XET-active enzyme, regulates aluminum
sensitivity by modulating in vivo XET action, cell wall xyloglucan
content, and aluminum binding capacity in Arabidopsis.";
Plant Cell 24:4731-4747(2012).
[9]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY,
AND DISRUPTION PHENOTYPE.
PubMed=23104861; DOI=10.1104/pp.112.207308;
Kaewthai N., Gendre D., Eklof J.M., Ibatullin F.M., Ezcurra I.,
Bhalerao R.P., Brumer H.;
"Group III-A XTH genes of Arabidopsis encode predominant xyloglucan
endohydrolases that are dispensable for normal growth.";
Plant Physiol. 161:440-454(2013).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=25446234; DOI=10.1016/j.phytochem.2014.09.020;
Shi Y.Z., Zhu X.F., Miller J.G., Gregson T., Zheng S.J., Fry S.C.;
"Distinct catalytic capacities of two aluminium-repressed Arabidopsis
thaliana xyloglucan endotransglucosylase/hydrolases, XTH15 and XTH31,
heterologously produced in Pichia.";
Phytochemistry 112:160-169(2015).
[11]
INTERACTION WITH XTH17.
PubMed=24948835; DOI=10.1104/pp.114.243790;
Zhu X.F., Wan J.X., Sun Y., Shi Y.Z., Braam J., Li G.X., Zheng S.J.;
"Xyloglucan endotransglucosylase-hydrolase17 interacts with xyloglucan
endotransglucosylase-hydrolase31 to confer xyloglucan
endotransglucosylase action and affect aluminum sensitivity in
Arabidopsis.";
Plant Physiol. 165:1566-1574(2014).
-!- FUNCTION: Catalyzes xyloglucan endohydrolysis (XEH) and/or
endotransglycosylation (XET). Cleaves and religates xyloglucan
polymers, an essential constituent of the primary cell wall, and
thereby participates in cell wall construction of growing tissues.
Involved in the accumulation of hemicelluloses. Has a high XEH
activity and only a slight XET activity in vitro, but the main in
planta activity seems to be XET, thus controlling aluminum
sensitivity (PubMed:23204407, PubMed:23104861, PubMed:25446234).
Acceptor preferences are XXXGol = XXFGol > XXLGol > XLLGol =
XLFGol (PubMed:25446234). {ECO:0000269|PubMed:23104861,
ECO:0000269|PubMed:23204407, ECO:0000269|PubMed:25446234}.
-!- CATALYTIC ACTIVITY: Breaks a beta-(1->4) bond in the backbone of a
xyloglucan and transfers the xyloglucanyl segment on to O-4 of the
non-reducing terminal glucose residue of an acceptor, which can be
a xyloglucan or an oligosaccharide of xyloglucan.
{ECO:0000269|PubMed:23104861}.
-!- CATALYTIC ACTIVITY: Xyloglucan + H(2)O = xyloglucan
oligosaccharides. {ECO:0000269|PubMed:23104861,
ECO:0000269|PubMed:25446234}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=86 uM for XXXGol {ECO:0000269|PubMed:25446234};
Note=KM for xyloglucan as donor substrate is 1.6 mg/ml. KM is
quoted in mg/ml, not uM, because XTHs are able to utilise any
segment of the polysaccharide chain equally well, not just one
site per molecule as with the acceptor.
{ECO:0000269|PubMed:25446234};
pH dependence:
Optimum pH is 5 for the XET activity. Optimum pH is 4.5 - 4.75
for the XEH activity. {ECO:0000269|PubMed:23104861,
ECO:0000269|PubMed:25446234};
-!- SUBUNIT: Interacts with XTH17. The formation of an XTH17-XTH31
dimer may be required for XET activity.
{ECO:0000269|PubMed:24948835}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
extracellular space, apoplast {ECO:0000305}. Cell membrane
{ECO:0000269|PubMed:23204407}.
-!- TISSUE SPECIFICITY: Predominantly expressed in root
(PubMed:11673616, Ref.1). Weakly expressed in influorescence stems
(PubMed:11673616). Expressed in root tips and elongation zones,
stems, young leaves, flowers and siliques (PubMed:23204407).
Expressed in root, hypocotyl, and etiolated whole seedlings
(PubMed:23104861). {ECO:0000269|PubMed:11673616,
ECO:0000269|PubMed:23104861, ECO:0000269|PubMed:23204407,
ECO:0000269|Ref.1}.
-!- DEVELOPMENTAL STAGE: Expressed in germinating seeds from 24 hours
after imbibation, and reaches a maximum level at 72 hours. After
96 hours, it then decreases. {ECO:0000269|Ref.1}.
-!- INDUCTION: Up-regulated by gibberellins (Probable). Not induced by
auxin (Ref.1). Down-regulated by aluminum (PubMed:21285327,
PubMed:23204407). {ECO:0000269|PubMed:21285327,
ECO:0000269|PubMed:23204407, ECO:0000269|Ref.1, ECO:0000305}.
-!- PTM: Contains at least one intrachain disulfide bond essential for
its enzymatic activity. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Reduced growth, decreased cell wall
xyloglucan content and increased aluminum resistance
(PubMed:23204407). No visible phenotype under normal growth
conditions (PubMed:23104861). {ECO:0000269|PubMed:23104861,
ECO:0000269|PubMed:23204407}.
-!- MISCELLANEOUS: In contrast to group 1 and group 2
endotransglucosylase/hydrolase proteins, it may not contain the
ligase activity, and may catalyze endohydrolysis xyloglucan
polymers only.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group
3 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X92975; CAA63553.1; -; mRNA.
EMBL; AL353992; CAB89314.1; -; Genomic_DNA.
EMBL; CP002686; AEE77976.1; -; Genomic_DNA.
EMBL; AY056163; AAL07012.1; -; mRNA.
EMBL; AY136454; AAM97119.1; -; mRNA.
EMBL; BT006326; AAP13434.1; -; mRNA.
PIR; T48975; T48975.
RefSeq; NP_190085.1; NM_114368.3.
UniGene; At.20372; -.
ProteinModelPortal; P93046; -.
SMR; P93046; -.
BioGrid; 8954; 1.
STRING; 3702.AT3G44990.1; -.
CAZy; GH16; Glycoside Hydrolase Family 16.
PaxDb; P93046; -.
EnsemblPlants; AT3G44990.1; AT3G44990.1; AT3G44990.
GeneID; 823634; -.
Gramene; AT3G44990.1; AT3G44990.1; AT3G44990.
KEGG; ath:AT3G44990; -.
Araport; AT3G44990; -.
TAIR; locus:2075919; AT3G44990.
eggNOG; ENOG410J8R0; Eukaryota.
eggNOG; ENOG411167N; LUCA.
HOGENOM; HOG000236368; -.
InParanoid; P93046; -.
KO; K08235; -.
OMA; EFRTLWG; -.
OrthoDB; EOG09360KA4; -.
PhylomeDB; P93046; -.
BioCyc; ARA:AT3G44990-MONOMER; -.
PRO; PR:P93046; -.
Proteomes; UP000006548; Chromosome 3.
Genevisible; P93046; AT.
GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0033946; F:xyloglucan-specific endo-beta-1,4-glucanase activity; IDA:TAIR.
GO; GO:0016762; F:xyloglucan:xyloglucosyl transferase activity; IEA:UniProtKB-EC.
GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
GO; GO:0016998; P:cell wall macromolecule catabolic process; IMP:TAIR.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0010411; P:xyloglucan metabolic process; IEA:InterPro.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR000757; GH16.
InterPro; IPR010713; XET_C.
InterPro; IPR016455; XTH.
Pfam; PF00722; Glyco_hydro_16; 1.
Pfam; PF06955; XET_C; 1.
PIRSF; PIRSF005604; XET; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS51762; GH16_2; 1.
1: Evidence at protein level;
Apoplast; Cell membrane; Cell wall; Cell wall biogenesis/degradation;
Complete proteome; Disulfide bond; Glycosidase; Hydrolase; Membrane;
Reference proteome; Secreted; Signal; Transferase.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 293 Xyloglucan endotransglucosylase/hydrolase
protein 31.
/FTId=PRO_0000011831.
DOMAIN 29 230 GH16. {ECO:0000255|PROSITE-
ProRule:PRU01098}.
ACT_SITE 114 114 Nucleophile. {ECO:0000250}.
ACT_SITE 118 118 Proton donor. {ECO:0000250}.
CONFLICT 11 11 L -> V (in Ref. 1; CAA63553).
{ECO:0000305}.
CONFLICT 260 260 S -> T (in Ref. 1; CAA63553).
{ECO:0000305}.
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


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