HEXO1_ARATH
ID HEXO1_ARATH Reviewed; 541 AA.
AC A7WM73; Q0WUA8; Q8LFK0; Q9M3C5;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Beta-hexosaminidase 1;
DE EC=3.2.1.52;
DE AltName: Full=Beta-GlcNAcase 1;
DE AltName: Full=Beta-N-acetylhexosaminidase 1;
DE AltName: Full=Beta-hexosaminidase 2;
DE Short=AtHEX2;
DE AltName: Full=N-acetyl-beta-glucosaminidase 1;
DE Flags: Precursor;
GN Name=HEXO1; Synonyms=HEX2; OrderedLocusNames=At3g55260;
GN ORFNames=T26I12.140;
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION,
RP GENE FAMILY, AND 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-541.
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-541.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
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 pyridylaminated chitotriose, pyridylaminated
CC chitobiose, p-nitrophenyl-beta-N-acetylglucosaminide, p-nitrophenyl-2-
CC acetamido-2-deoxy-beta-D-glucopyranoside (pNP-GlcNAc), p-nitrophenyl-2-
CC acetamido-2-deoxy-beta-D-galactopyranoside (pNP-GalNAc), 4-
CC 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. Required
CC for the presence of paucimannosidic N-glycans in glycoproteins of roots
CC and, to a lower extent, of leaves. {ECO:0000269|PubMed:17636254,
CC ECO:0000269|PubMed:17644627, 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, 2-acet-
CC amido-1,2-dideoxynojirimycin and PUGNAc. {ECO:0000269|PubMed:17636254}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:17636254, ECO:0000269|PubMed:17644627};
CC Vmax=151 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: Vacuole {ECO:0000269|PubMed:17644627,
CC ECO:0000269|PubMed:21252225}.
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 -!- DISRUPTION PHENOTYPE: Reduced amounts of paucimannosidic N-glycans-
CC containing glycoproteins in roots and, to a lower extent, in leaves.
CC {ECO:0000269|PubMed:21252225}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM61367.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB75760.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM493720; CAM35467.1; -; mRNA.
DR EMBL; AL132954; CAB75760.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79360.1; -; Genomic_DNA.
DR EMBL; AK227260; BAE99290.1; -; mRNA.
DR EMBL; AY084801; AAM61367.1; ALT_INIT; mRNA.
DR EMBL; BT000920; AAN41320.1; -; mRNA.
DR PIR; T47665; T47665.
DR RefSeq; NP_567017.2; NM_115384.4.
DR AlphaFoldDB; A7WM73; -.
DR SMR; A7WM73; -.
DR IntAct; A7WM73; 1.
DR STRING; 3702.AT3G55260.1; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR PaxDb; A7WM73; -.
DR PRIDE; A7WM73; -.
DR ProMEX; A7WM73; -.
DR ProteomicsDB; 230220; -.
DR EnsemblPlants; AT3G55260.1; AT3G55260.1; AT3G55260.
DR GeneID; 824692; -.
DR Gramene; AT3G55260.1; AT3G55260.1; AT3G55260.
DR KEGG; ath:AT3G55260; -.
DR Araport; AT3G55260; -.
DR TAIR; locus:2100706; AT3G55260.
DR eggNOG; KOG2499; Eukaryota.
DR HOGENOM; CLU_007082_0_4_1; -.
DR InParanoid; A7WM73; -.
DR OMA; QNENECP; -.
DR OrthoDB; 545162at2759; -.
DR PhylomeDB; A7WM73; -.
DR BioCyc; ARA:AT3G55260-MON; -.
DR BRENDA; 3.2.1.52; 399.
DR PRO; PR:A7WM73; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; A7WM73; baseline and differential.
DR Genevisible; A7WM73; AT.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; 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: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 Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Signal; Vacuole.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..541
FT /note="Beta-hexosaminidase 1"
FT /id="PRO_0000420286"
FT ACT_SITE 332
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 295..337
FT /evidence="ECO:0000250"
FT DISULFID 511..538
FT /evidence="ECO:0000250"
FT CONFLICT 84
FT /note="G -> V (in Ref. 5; AAM61367)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="D -> G (in Ref. 4; BAE99290)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="W -> R (in Ref. 4; BAE99290)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 61230 MW; 441D48C6F1FCCF56 CRC64;
MSTNLLRLIL LFITLSITSS LSTPSPADSP PYLWPLPAEF SFGNETLSVD PTVTLIVAGN
GGGSLIIRAA FDRYMGIIFK HASGRGSLLS RIRFLKMVEY DITSLKIVVH SDSEELQLGV
DESYTLMVSK KNEQSIVGAA TIEANTVYGA LRGLETFSQL CAFDYITKSV QIYKAPWYIQ
DKPRFGYRGL LIDTSRHYLP IDVIKQIIES MSFAKLNVLH WHIVDEQSFP LETPTYPNLW
KGAYSRWERY TVEDASEIVR FAKMRGINVM AEVDVPGHAE SWGTGYPDLW PSLSCREPLD
VTKNFTFDVI SGILADMRKI FPFELFHLGG DEVNTDCWKN TTHVKEWLQG RNFTTKDAYK
YFVLRAQQIA ISKNWTPVNW EETFSSFGKD LDPRTVIQNW LVSDICQKAV AKGFRCIFSN
QGYWYLDHLD VPWEEVYNTE PLNGIEDPSL QKLVIGGEVC MWGETADTSV VLQTIWPRAA
AAAERMWSTR EAVSKGNITL TALPRLHYFR CLLNNRGVPA APVDNFYARR PPLGPGSCYA
Q
