HEXO2_ARATH
ID HEXO2_ARATH Reviewed; 580 AA.
AC Q9SYK0;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Beta-hexosaminidase 2;
DE EC=3.2.1.52;
DE AltName: Full=Beta-GlcNAcase 2;
DE AltName: Full=Beta-N-acetylhexosaminidase 2;
DE AltName: Full=Beta-hexosaminidase 3;
DE Short=AtHEX3;
DE AltName: Full=N-acetyl-beta-glucosaminidase 2;
DE Flags: Precursor;
GN Name=HEXO2; Synonyms=HEX3; OrderedLocusNames=At1g05590; ORFNames=F3F20.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND REVIEW.
RX PubMed=17636254; DOI=10.1074/jbc.m704235200;
RA Gutternigg M., Kretschmer-Lubich D., Paschinger K., Rendic D., Hader J.,
RA Geier P., Ranftl R., Jantsch V., Lochnit G., Wilson I.B.H.;
RT "Biosynthesis of truncated N-linked oligosaccharides results from non-
RT orthologous hexosaminidase-mediated mechanisms in nematodes, plants, and
RT insects.";
RL J. Biol. Chem. 282:27825-27840(2007).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=17644627; DOI=10.1104/pp.107.101162;
RA Strasser R., Bondili J.S., Schoberer J., Svoboda B., Liebminger E.,
RA Glossl J., Altmann F., Steinkellner H., Mach L.;
RT "Enzymatic properties and subcellular localization of Arabidopsis beta-N-
RT acetylhexosaminidases.";
RL Plant Physiol. 145:5-16(2007).
RN [6]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=21252225; DOI=10.1074/jbc.m110.178020;
RA Liebminger E., Veit C., Pabst M., Batoux M., Zipfel C., Altmann F.,
RA Mach L., Strasser R.;
RT "Beta-N-acetylhexosaminidases HEXO1 and HEXO3 are responsible for the
RT formation of paucimannosidic N-glycans in Arabidopsis thaliana.";
RL J. Biol. Chem. 286:10793-10802(2011).
CC -!- FUNCTION: Has a broad substrate specificity. Can use synthetic
CC substrates such as p-nitrophenyl-beta-N-acetylglucosaminide, p-
CC nitrophenyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (pNP-GlcNAc), p-
CC nitrophenyl-2-acetamido-2-deoxy-beta-D-galactopyranoside (pNP-GalNAc),
CC 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-
CC GlcNAc), and 4-methylumbelliferyl-6-sulfo-2-acetamido-2-deoxy-beta-D-
CC glucopyranoside (MU-GlcNAc-6SO(4)) as substrates. Removes terminal
CC GlcNAc residues from alpha1,3- and alpha1,6-mannosyl branches of
CC biantennary N-glycans without any strict branch preference.
CC {ECO:0000269|PubMed:17636254, ECO:0000269|PubMed:17644627,
CC ECO:0000269|PubMed:21252225}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000269|PubMed:17644627};
CC -!- ACTIVITY REGULATION: Inhibited by N-acetylcastanospermine.
CC {ECO:0000269|PubMed:17636254}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:17636254, ECO:0000269|PubMed:17644627};
CC Vmax=7.9 umol/min/mg enzyme with pNP-GlcNAc as substrate (at pH 4.6
CC and 37 degrees Celsius) {ECO:0000269|PubMed:17636254,
CC ECO:0000269|PubMed:17644627};
CC pH dependence:
CC Optimum pH is 4-5. {ECO:0000269|PubMed:17636254,
CC ECO:0000269|PubMed:17644627};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17644627}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:17644627}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17644627}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK229119; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC007153; AAD30612.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27861.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60833.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60834.1; -; Genomic_DNA.
DR EMBL; AK229119; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; H86189; H86189.
DR RefSeq; NP_001318927.1; NM_001331557.1.
DR RefSeq; NP_001323090.1; NM_001331558.1.
DR RefSeq; NP_172050.1; NM_100439.3.
DR AlphaFoldDB; Q9SYK0; -.
DR SMR; Q9SYK0; -.
DR STRING; 3702.AT1G05590.1; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR PaxDb; Q9SYK0; -.
DR PRIDE; Q9SYK0; -.
DR ProteomicsDB; 230360; -.
DR EnsemblPlants; AT1G05590.1; AT1G05590.1; AT1G05590.
DR EnsemblPlants; AT1G05590.2; AT1G05590.2; AT1G05590.
DR EnsemblPlants; AT1G05590.3; AT1G05590.3; AT1G05590.
DR GeneID; 837064; -.
DR Gramene; AT1G05590.1; AT1G05590.1; AT1G05590.
DR Gramene; AT1G05590.2; AT1G05590.2; AT1G05590.
DR Gramene; AT1G05590.3; AT1G05590.3; AT1G05590.
DR KEGG; ath:AT1G05590; -.
DR Araport; AT1G05590; -.
DR TAIR; locus:2031988; AT1G05590.
DR eggNOG; KOG2499; Eukaryota.
DR HOGENOM; CLU_007082_0_2_1; -.
DR InParanoid; Q9SYK0; -.
DR OMA; QYWVDHA; -.
DR OrthoDB; 545162at2759; -.
DR PhylomeDB; Q9SYK0; -.
DR BioCyc; ARA:AT1G05590-MON; -.
DR BRENDA; 3.2.1.52; 399.
DR PRO; PR:Q9SYK0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYK0; baseline and differential.
DR Genevisible; Q9SYK0; AT.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IDA:TAIR.
DR GO; GO:0015929; F:hexosaminidase activity; IDA:TAIR.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030203; P:glycosaminoglycan metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR029019; HEX_eukaryotic_N.
DR PANTHER; PTHR22600; PTHR22600; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF14845; Glycohydro_20b2; 1.
DR PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..580
FT /note="Beta-hexosaminidase 2"
FT /id="PRO_0000420287"
FT ACT_SITE 337
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 279..342
FT /evidence="ECO:0000250"
SQ SEQUENCE 580 AA; 64991 MW; 4C1421A5CA71C853 CRC64;
MLTLSKFHVI LIPILFFITL LSPLFSIALP INIWPKPRFL SWPQHKAIAL SPNFTILAPE
HQYLSASVTR YHNLIRSENY SPLISYPVKL MKRYTLRNLV VTVTDFSLPL HHGVDESYKL
SIPIGSFSAH LLAHSAWGAM RGLETFSQMI WGTSPDLCLP VGIYIQDSPL FGHRGVLLDT
SRNYYGVDDI MRTIKAMSAN KLNVFHWHIT DSQSFPLVLP SEPSLAAKGS LGPDMVYTPE
DVSKIVQYGF EHGVRVLPEI DTPGHTGSWG EAYPEIVTCA NMFWWPAGKS WEERLASEPG
TGQLNPLSPK TYEVVKNVIQ DIVNQFPESF FHGGGDEVIP GCWKTDPAIN SFLSSGGTLS
QLLEKYINST LPYIVSQNRT VVYWEDVLLD AQIKADPSVL PKEHTILQTW NNGPENTKRI
VAAGYRVIVS SSEFYYLDCG HGGFLGNDSI YDQKESGGGS WCAPFKTWQS IYNYDIADGL
LNEEERKLVL GGEVALWSEQ ADSTVLDSRL WPRASALAES LWSGNRDERG VKRCGEAVDR
LNLWRYRMVK RGIGAEPIQP LWCLKNPGMC NTVHGALQDQ
