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Q9SV61 (XTH1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative xyloglucan endotransglucosylase/hydrolase protein 1

Short name=At-XTH1
Short name=XTH-1
EC=2.4.1.207
Gene names
Name:XTH1
Ordered Locus Names:At4g13080
ORF Names:F25G13.170
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

May catalyze 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 By similarity.

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.

Subcellular location

Secretedcell wall Probable. Secretedextracellular spaceapoplast Probable.

Post-translational modification

Contains at least one intrachain disulfide bond essential for its enzymatic activity By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 16 family. XTH group 1 subfamily.

Sequence caution

The sequence CAB45507.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAB78350.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 292271Putative xyloglucan endotransglucosylase/hydrolase protein 1
PRO_0000011801

Sites

Active site1101Nucleophile By similarity
Active site1141Proton donor By similarity

Amino acid modifications

Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9SV61 [UniParc].

Last modified May 31, 2011. Version 2.
Checksum: B4459C51EECBB139

FASTA29233,247
        10         20         30         40         50         60 
MEYLSIFGFV SVLYLIIRVD ARAYEVNGID QSKVGFDDNY VVTWGQNNVL KLNQGKEVQL 

        70         80         90        100        110        120 
SLDHSSGSGF ESKNHYESGF FQIRIKVPPK DTSGVVTAFY LTSKGNTHDE VDFEFLGNKE 

       130        140        150        160        170        180 
GKLAVQTNVF TNGKGNREQK LALWFDPSKD FHTYAILWNP YQIVLYVDNI PVRVFKNTTS 

       190        200        210        220        230        240 
QGMNYPSKPM QVVVSLWNGE NWATDGGKSK INWSLAPFKA NFQGFNNSGC FTNAEKNACG 

       250        260        270        280        290 
SSAYWWNTGS YSKLSDSEQK AYTNVRQKYM NYDYCSDKVR FHVPPSECKW NN 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"The XTH family of enzymes involved in xyloglucan endotransglucosylation and endohydrolysis: current perspectives and a new unifying nomenclature."
Rose J.K.C., Braam J., Fry S.C., Nishitani K.
Plant Cell Physiol. 43:1421-1435(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL079349 Genomic DNA. Translation: CAB45507.1. Different initiation.
AL161535 Genomic DNA. Translation: CAB78350.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE83228.1.
PIRT10210.
RefSeqNP_193044.2. NM_117377.2.
UniGeneAt.54296.

3D structure databases

ProteinModelPortalQ9SV61.
SMRQ9SV61. Positions 34-289.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G13080.1-P.

Protein family/group databases

CAZyGH16. Glycoside Hydrolase Family 16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G13080.1; AT4G13080.1; AT4G13080.
GeneID826922.
KEGGath:AT4G13080.

Organism-specific databases

TAIRAT4G13080.

Phylogenomic databases

eggNOGCOG2273.
HOGENOMHOG000236368.
InParanoidQ9SV61.
KOK08235.
OMAPAADFHD.

Enzyme and pathway databases

BioCycARA:AT4G13080-MONOMER.

Gene expression databases

GenevestigatorQ9SV61.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008264. Beta_glucanase.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
IPR016455. XET.
IPR010713. XET_C.
[Graphical view]
PfamPF00722. Glyco_hydro_16. 1 hit.
PF06955. XET_C. 1 hit.
[Graphical view]
PIRSFPIRSF005604. XET. 1 hit.
PRINTSPR00737. GLHYDRLASE16.
SUPFAMSSF49899. SSF49899. 1 hit.
ProtoNetSearch...

Entry information

Entry nameXTH1_ARATH
AccessionPrimary (citable) accession number: Q9SV61
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: May 31, 2011
Last modified: May 14, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names