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A7WM73

- HEXO1_ARATH

UniProt

A7WM73 - HEXO1_ARATH

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Protein

Beta-hexosaminidase 1

Gene

HEXO1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

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

Enzyme regulationi

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

Kineticsi

  1. KM=0.7 mM for pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius)2 Publications

Vmax=151 µmol/min/mg enzyme with pNP-GlcNAc as substrate (at pH 4.6 and 37 degrees Celsius)2 Publications

pH dependencei

Optimum pH is 4-5.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei332 – 3321Proton donorBy similarity

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: TAIR
  2. hexosaminidase activity Source: TAIR

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciARA:AT3G55260-MONOMER.
ReactomeiREACT_187588. Hyaluronan uptake and degradation.
REACT_187659. Glycosphingolipid metabolism.
REACT_187663. Keratan sulfate degradation.
REACT_215132. CS/DS degradation.

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:HEXO1
Synonyms:HEX2
Ordered Locus Names:At3g55260
ORF Names:T26I12.140
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G55260.

Subcellular locationi

Vacuole 2 Publications

GO - Cellular componenti

  1. cytosol Source: TAIR
  2. plant-type cell wall Source: TAIR
  3. vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Disruption phenotypei

Reduced amounts of paucimannosidic N-glycans-containg glycoproteins in roots and, to a lower extent, in leaves.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 541521Beta-hexosaminidase 1PRO_0000420286Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi44 – 441N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi295 ↔ 337By similarity
Glycosylationi304 – 3041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi352 – 3521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi497 – 4971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi511 ↔ 538By similarity

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiA7WM73.
PRIDEiA7WM73.
ProMEXiA7WM73.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriA7WM73.

Interactioni

Protein-protein interaction databases

IntActiA7WM73. 1 interaction.
STRINGi3702.AT3G55260.1-P.

Structurei

3D structure databases

ProteinModelPortaliA7WM73.
SMRiA7WM73. Positions 29-490.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 20 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3525.
HOGENOMiHOG000157972.
InParanoidiA7WM73.
KOiK12373.
OMAiWTPVNWE.
PhylomeDBiA7WM73.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR025705. Beta_hexosaminidase_sua/sub.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR029019. HEX_eukaryotic_N.
[Graphical view]
PfamiPF00728. Glyco_hydro_20. 1 hit.
PF14845. Glycohydro_20b2. 1 hit.
[Graphical view]
PIRSFiPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSiPR00738. GLHYDRLASE20.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A7WM73-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTNLLRLIL LFITLSITSS LSTPSPADSP PYLWPLPAEF SFGNETLSVD
60 70 80 90 100
PTVTLIVAGN GGGSLIIRAA FDRYMGIIFK HASGRGSLLS RIRFLKMVEY
110 120 130 140 150
DITSLKIVVH SDSEELQLGV DESYTLMVSK KNEQSIVGAA TIEANTVYGA
160 170 180 190 200
LRGLETFSQL CAFDYITKSV QIYKAPWYIQ DKPRFGYRGL LIDTSRHYLP
210 220 230 240 250
IDVIKQIIES MSFAKLNVLH WHIVDEQSFP LETPTYPNLW KGAYSRWERY
260 270 280 290 300
TVEDASEIVR FAKMRGINVM AEVDVPGHAE SWGTGYPDLW PSLSCREPLD
310 320 330 340 350
VTKNFTFDVI SGILADMRKI FPFELFHLGG DEVNTDCWKN TTHVKEWLQG
360 370 380 390 400
RNFTTKDAYK YFVLRAQQIA ISKNWTPVNW EETFSSFGKD LDPRTVIQNW
410 420 430 440 450
LVSDICQKAV AKGFRCIFSN QGYWYLDHLD VPWEEVYNTE PLNGIEDPSL
460 470 480 490 500
QKLVIGGEVC MWGETADTSV VLQTIWPRAA AAAERMWSTR EAVSKGNITL
510 520 530 540
TALPRLHYFR CLLNNRGVPA APVDNFYARR PPLGPGSCYA Q
Length:541
Mass (Da):61,230
Last modified:October 23, 2007 - v1
Checksum:i441D48C6F1FCCF56
GO

Sequence cautioni

The sequence AAM61367.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB75760.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841G → V in AAM61367. 1 PublicationCurated
Sequence conflicti181 – 1811D → G in BAE99290. 1 PublicationCurated
Sequence conflicti347 – 3471W → R in BAE99290. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT47665.
RefSeqiNP_567017.2. NM_115384.3.
UniGeneiAt.21628.

Genome annotation databases

EnsemblPlantsiAT3G55260.1; AT3G55260.1; AT3G55260.
GeneIDi824692.
KEGGiath:AT3G55260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi T47665.
RefSeqi NP_567017.2. NM_115384.3.
UniGenei At.21628.

3D structure databases

ProteinModelPortali A7WM73.
SMRi A7WM73. Positions 29-490.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi A7WM73. 1 interaction.
STRINGi 3702.AT3G55260.1-P.

Protein family/group databases

CAZyi GH20. Glycoside Hydrolase Family 20.

Proteomic databases

PaxDbi A7WM73.
PRIDEi A7WM73.
ProMEXi A7WM73.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G55260.1 ; AT3G55260.1 ; AT3G55260 .
GeneIDi 824692.
KEGGi ath:AT3G55260.

Organism-specific databases

TAIRi AT3G55260.

Phylogenomic databases

eggNOGi COG3525.
HOGENOMi HOG000157972.
InParanoidi A7WM73.
KOi K12373.
OMAi WTPVNWE.
PhylomeDBi A7WM73.

Enzyme and pathway databases

BioCyci ARA:AT3G55260-MONOMER.
Reactomei REACT_187588. Hyaluronan uptake and degradation.
REACT_187659. Glycosphingolipid metabolism.
REACT_187663. Keratan sulfate degradation.
REACT_215132. CS/DS degradation.

Miscellaneous databases

PROi A7WM73.

Gene expression databases

Genevestigatori A7WM73.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProi IPR025705. Beta_hexosaminidase_sua/sub.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR029019. HEX_eukaryotic_N.
[Graphical view ]
Pfami PF00728. Glyco_hydro_20. 1 hit.
PF14845. Glycohydro_20b2. 1 hit.
[Graphical view ]
PIRSFi PIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSi PR00738. GLHYDRLASE20.
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.
    , 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.

Entry informationi

Entry nameiHEXO1_ARATH
AccessioniPrimary (citable) accession number: A7WM73
Secondary accession number(s): Q0WUA8, Q8LFK0, Q9M3C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: October 23, 2007
Last modified: November 26, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3