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A7WM73 (HEXO1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. 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:
Beta-hexosaminidase 1

EC=3.2.1.52
Alternative name(s):
Beta-GlcNAcase 1
Beta-N-acetylhexosaminidase 1
Beta-hexosaminidase 2
Short name=AtHEX2
N-acetyl-beta-glucosaminidase 1
Gene names
Name:HEXO1
Synonyms:HEX2
Ordered Locus Names:At3g55260
ORF Names:T26I12.140
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a broad substrate specificity. Can use synthetic substrates such as pyridylaminated chitotriose, pyridylaminated chitobiose, p-nitrophenyl-beta-N-acetylglucosaminide, p-nitrophenyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (pNP-GlcNAc), p-nitrophenyl-2-acetamido-2-deoxy-beta-D-galactopyranoside (pNP-GalNAc), 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc), and 4-methylumbelliferyl-6-sulfo-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc-6SO4) as substrates. Removes terminal GlcNAc residues from alpha1,3- and alpha1,6-mannosyl branches of biantennary N-glycans without any strict branch preference. Required for the presence of paucimannosidic N-glycans in glycoproteins of roots and, to a lower extent, of leaves. Ref.1 Ref.7 Ref.8

Catalytic activity

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. Ref.1

Enzyme regulation

Inhibited by N-acetylcastanospermine, 2-acet-amido-1,2-dideoxynojirimycin and PUGNAc. Ref.7

Subcellular location

Vacuole Ref.1 Ref.8.

Tissue specificity

Expressed in roots, leaves, stems, flowers and siliques. Ref.1

Post-translational modification

N-glycosylated. Ref.1

Disruption phenotype

Reduced amounts of paucimannosidic N-glycans-containg glycoproteins in roots and, to a lower extent, in leaves. Ref.8

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.7 mM for pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius) Ref.1 Ref.7

Vmax=151 µmol/min/mg enzyme with pNP-GlcNAc as substrate (at pH 4.6 and 37 degrees Celsius)

pH dependence:

Optimum pH is 4-5.

Sequence caution

The sequence AAM61367.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAB75760.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 541521Beta-hexosaminidase 1
PRO_0000420286

Sites

Active site3321Proton donor By similarity

Amino acid modifications

Glycosylation441N-linked (GlcNAc...) Potential
Glycosylation3041N-linked (GlcNAc...) Potential
Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation3521N-linked (GlcNAc...) Potential
Glycosylation4971N-linked (GlcNAc...) Potential
Disulfide bond295 ↔ 337 By similarity
Disulfide bond511 ↔ 538 By similarity

Experimental info

Sequence conflict841G → V in AAM61367. Ref.5
Sequence conflict1811D → G in BAE99290. Ref.4
Sequence conflict3471W → R in BAE99290. Ref.4

Sequences

Sequence LengthMass (Da)Tools
A7WM73 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 441D48C6F1FCCF56

FASTA54161,230
        10         20         30         40         50         60 
MSTNLLRLIL LFITLSITSS LSTPSPADSP PYLWPLPAEF SFGNETLSVD PTVTLIVAGN 

        70         80         90        100        110        120 
GGGSLIIRAA FDRYMGIIFK HASGRGSLLS RIRFLKMVEY DITSLKIVVH SDSEELQLGV 

       130        140        150        160        170        180 
DESYTLMVSK KNEQSIVGAA TIEANTVYGA LRGLETFSQL CAFDYITKSV QIYKAPWYIQ 

       190        200        210        220        230        240 
DKPRFGYRGL LIDTSRHYLP IDVIKQIIES MSFAKLNVLH WHIVDEQSFP LETPTYPNLW 

       250        260        270        280        290        300 
KGAYSRWERY TVEDASEIVR FAKMRGINVM AEVDVPGHAE SWGTGYPDLW PSLSCREPLD 

       310        320        330        340        350        360 
VTKNFTFDVI SGILADMRKI FPFELFHLGG DEVNTDCWKN TTHVKEWLQG RNFTTKDAYK 

       370        380        390        400        410        420 
YFVLRAQQIA ISKNWTPVNW EETFSSFGKD LDPRTVIQNW LVSDICQKAV AKGFRCIFSN 

       430        440        450        460        470        480 
QGYWYLDHLD VPWEEVYNTE PLNGIEDPSL QKLVIGGEVC MWGETADTSV VLQTIWPRAA 

       490        500        510        520        530        540 
AAAERMWSTR EAVSKGNITL TALPRLHYFR CLLNNRGVPA APVDNFYARR PPLGPGSCYA 


Q 

« Hide

References

« Hide 'large scale' references
[1]"Enzymatic properties and subcellular localization of Arabidopsis beta-N-acetylhexosaminidases."
Strasser R., Bondili J.S., Schoberer J., Svoboda B., Liebminger E., Glossl J., Altmann F., Steinkellner H., Mach L.
Plant Physiol. 145:5-16(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, GENE FAMILY, NOMENCLATURE.
[2]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
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. expand/collapse author list , 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.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-541.
[6]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-541.
Strain: cv. Columbia.
[7]"Biosynthesis of truncated N-linked oligosaccharides results from non-orthologous hexosaminidase-mediated mechanisms in nematodes, plants, and insects."
Gutternigg M., Kretschmer-Lubich D., Paschinger K., Rendic D., Hader J., Geier P., Ranftl R., Jantsch V., Lochnit G., Wilson I.B.H.
J. Biol. Chem. 282:27825-27840(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, REVIEW.
[8]"Beta-N-acetylhexosaminidases HEXO1 and HEXO3 are responsible for the formation of paucimannosidic N-glycans in Arabidopsis thaliana."
Liebminger E., Veit C., Pabst M., Batoux M., Zipfel C., Altmann F., Mach L., Strasser R.
J. Biol. Chem. 286:10793-10802(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
Strain: cv. Columbia.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM493720 mRNA. Translation: CAM35467.1.
AL132954 Genomic DNA. Translation: CAB75760.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE79360.1.
AK227260 mRNA. Translation: BAE99290.1.
AY084801 mRNA. Translation: AAM61367.1. Different initiation.
BT000920 mRNA. Translation: AAN41320.1.
PIRT47665.
RefSeqNP_567017.2. NM_115384.3.
UniGeneAt.21628.

3D structure databases

ProteinModelPortalA7WM73.
SMRA7WM73. Positions 31-529.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActA7WM73. 1 interaction.
STRING3702.AT3G55260.1-P.

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

Proteomic databases

PaxDbA7WM73.
PRIDEA7WM73.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G55260.1; AT3G55260.1; AT3G55260.
GeneID824692.
KEGGath:AT3G55260.

Organism-specific databases

TAIRAT3G55260.

Phylogenomic databases

eggNOGCOG3525.
HOGENOMHOG000157972.
InParanoidA7WM73.
KOK12373.
OMAGINVMAE.
PhylomeDBA7WM73.
ProtClustDBCLSN2680418.

Enzyme and pathway databases

BioCycARA:AT3G55260-MONOMER.

Gene expression databases

GenevestigatorA7WM73.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR025705. Beta_hexosaminidase_sua/sub.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00728. Glyco_hydro_20. 1 hit.
[Graphical view]
PIRSFPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSPR00738. GLHYDRLASE20.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

PROA7WM73.

Entry information

Entry nameHEXO1_ARATH
AccessionPrimary (citable) accession number: A7WM73
Secondary accession number(s): Q0WUA8, Q8LFK0, Q9M3C5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: October 23, 2007
Last modified: April 16, 2014
This is version 59 of the entry and version 1 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