Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8L7S6

- HEXO3_ARATH

UniProt

Q8L7S6 - HEXO3_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Beta-hexosaminidase 3

Gene

HEXO3

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, 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 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

Slightly inhibited by N-acetylcastanospermine.1 Publication

Kineticsi

  1. KM=2.2 mM for pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius)2 Publications

Vmax=50.3 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 sitei329 – 3291Proton 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:AT1G65590-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 3 (EC:3.2.1.52)
Alternative name(s):
Beta-GlcNAcase 3
Beta-N-acetylhexosaminidase 3
Beta-hexosaminidase 1
Short name:
AtHEX1
N-acetyl-beta-glucosaminidase 3
Gene namesi
Name:HEXO3
Synonyms:HEX1
Ordered Locus Names:At1g65590
ORF Names:F5I14.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G65590.

Subcellular locationi

Cell membrane 2 Publications

GO - Cellular componenti

  1. cell wall Source: TAIR
  2. plant-type cell wall Source: TAIR
  3. plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Reduced amounts of paucimannosidic N-glycans-containg glycoproteins in roots and leaves.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 535511Beta-hexosaminidase 3PRO_0000420288Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi292 ↔ 334By similarity
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi405 – 4051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi441 – 4411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi496 – 4961N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi506 ↔ 532By similarity

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ8L7S6.

Expressioni

Tissue specificityi

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

Gene expression databases

ExpressionAtlasiQ8L7S6. baseline and differential.
GenevestigatoriQ8L7S6.

Structurei

3D structure databases

ProteinModelPortaliQ8L7S6.
SMRiQ8L7S6. Positions 34-521.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 20 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000157972.
InParanoidiQ8L7S6.
KOiK12373.
OMAiSATCKEP.
PhylomeDBiQ8L7S6.

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.

Q8L7S6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRGSGAKIAG VLPLFMLFIA GTISAFEDIE RLRIWPLPAQ VSHGGRRMYL
60 70 80 90 100
SGDFKLVTEG SKYGDASGIL KEGFDRMLGV VRLSHVISGD RNSSGTGGSA
110 120 130 140 150
LLQGLHVIIS SSTDELEYGA DESYKLVVPS PEKPSYAQLE AKSVYGALHG
160 170 180 190 200
LQTFSQLCHF NLKKKVIEIL MTPWNIIDQP RFSYRGLLID TSRHYLPLPV
210 220 230 240 250
IKNVIDSMTY AKLNVLHWHI VDTQSFPLEI PSYPKLWNGA YSSSQRYTFE
260 270 280 290 300
DAAEIVNYAR RRGIHVLAEI DVPGHALSWG KGYPALWPSK NCQEPLDVSS
310 320 330 340 350
DFTFKVIDGI LSDFSKIFKF KFVHLGGDEV NTTCWSATPR IAQWLKKHRM
360 370 380 390 400
SEKEAYQYFV LRAQKIALSH GYEIINWEET FINFGSKLNR KTVVHNWLNT
410 420 430 440 450
GLVENVTASG LRCIVSNQEF WYLDHIDAPW QGFYANEPFQ NITDKKQQSL
460 470 480 490 500
VLGGEVCMWG EHIDASDIEQ TIWPRAAAAA ERLWTPYAKL AKNPNNVTTR
510 520 530
LAHFRCLLNQ RGVAAAPLVG GGRVVPFEPG SCLAQ
Length:535
Mass (Da):60,014
Last modified:October 1, 2002 - v1
Checksum:i9295E14DB073F966
GO

Sequence cautioni

The sequence AAB60911.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC001229 Genomic DNA. Translation: AAB60911.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE34399.1.
AY128283 mRNA. Translation: AAM91092.1.
BT000831 mRNA. Translation: AAN33206.1.
PIRiA96681.
RefSeqiNP_176737.2. NM_105233.4.
UniGeneiAt.24164.

Genome annotation databases

EnsemblPlantsiAT1G65590.1; AT1G65590.1; AT1G65590.
GeneIDi842871.
KEGGiath:AT1G65590.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC001229 Genomic DNA. Translation: AAB60911.1 . Sequence problems.
CP002684 Genomic DNA. Translation: AEE34399.1 .
AY128283 mRNA. Translation: AAM91092.1 .
BT000831 mRNA. Translation: AAN33206.1 .
PIRi A96681.
RefSeqi NP_176737.2. NM_105233.4.
UniGenei At.24164.

3D structure databases

ProteinModelPortali Q8L7S6.
SMRi Q8L7S6. Positions 34-521.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH20. Glycoside Hydrolase Family 20.

Proteomic databases

PRIDEi Q8L7S6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G65590.1 ; AT1G65590.1 ; AT1G65590 .
GeneIDi 842871.
KEGGi ath:AT1G65590.

Organism-specific databases

TAIRi AT1G65590.

Phylogenomic databases

HOGENOMi HOG000157972.
InParanoidi Q8L7S6.
KOi K12373.
OMAi SATCKEP.
PhylomeDBi Q8L7S6.

Enzyme and pathway databases

BioCyci ARA:AT1G65590-MONOMER.
Reactomei REACT_187588. Hyaluronan uptake and degradation.
REACT_187659. Glycosphingolipid metabolism.
REACT_187663. Keratan sulfate degradation.
REACT_215132. CS/DS degradation.

Gene expression databases

ExpressionAtlasi Q8L7S6. baseline and differential.
Genevestigatori Q8L7S6.

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. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [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. "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].
    Strain: cv. Columbia.
  4. "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.
  5. "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: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY, NOMENCLATURE.
  6. "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 nameiHEXO3_ARATH
AccessioniPrimary (citable) accession number: Q8L7S6
Secondary accession number(s): O04477
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 87 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