HEXO3_ARATH
ID HEXO3_ARATH Reviewed; 535 AA.
AC Q8L7S6; O04477;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Beta-hexosaminidase 3;
DE EC=3.2.1.52;
DE AltName: Full=Beta-GlcNAcase 3;
DE AltName: Full=Beta-N-acetylhexosaminidase 3;
DE AltName: Full=Beta-hexosaminidase 1;
DE Short=AtHEX1;
DE AltName: Full=N-acetyl-beta-glucosaminidase 3;
DE Flags: Precursor;
GN Name=HEXO3; Synonyms=HEX1; OrderedLocusNames=At1g65590; ORFNames=F5I14.13;
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;
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 [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 GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES, 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, 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, p-nitrophenyl-beta-N-
CC acetylglucosaminide, p-nitrophenyl-2-acetamido-2-deoxy-beta-D-
CC glucopyranoside (pNP-GlcNAc), p-nitrophenyl-2-acetamido-2-deoxy-beta-D-
CC galactopyranoside (pNP-GalNAc), 4-methylumbelliferyl-2-acetamido-2-
CC deoxy-beta-D-glucopyranoside (MU-GlcNAc), and 4-methylumbelliferyl-6-
CC sulfo-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc-6SO(4)) as
CC substrates. Removes terminal GlcNAc residues from alpha1,3- and
CC alpha1,6-mannosyl branches of biantennary N-glycans without any strict
CC branch preference. Required for the presence of paucimannosidic N-
CC glycans in glycoproteins of roots and leaves.
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: Slightly inhibited by N-acetylcastanospermine.
CC {ECO:0000269|PubMed:17636254}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.2 mM for pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:17636254, ECO:0000269|PubMed:17644627};
CC Vmax=50.3 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 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 leaves.
CC {ECO:0000269|PubMed:21252225}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB60911.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC001229; AAB60911.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34399.1; -; Genomic_DNA.
DR EMBL; AY128283; AAM91092.1; -; mRNA.
DR EMBL; BT000831; AAN33206.1; -; mRNA.
DR PIR; A96681; A96681.
DR RefSeq; NP_176737.2; NM_105233.5.
DR AlphaFoldDB; Q8L7S6; -.
DR SMR; Q8L7S6; -.
DR STRING; 3702.AT1G65590.1; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR PaxDb; Q8L7S6; -.
DR PRIDE; Q8L7S6; -.
DR ProteomicsDB; 230361; -.
DR EnsemblPlants; AT1G65590.1; AT1G65590.1; AT1G65590.
DR GeneID; 842871; -.
DR Gramene; AT1G65590.1; AT1G65590.1; AT1G65590.
DR KEGG; ath:AT1G65590; -.
DR Araport; AT1G65590; -.
DR TAIR; locus:2034147; AT1G65590.
DR eggNOG; KOG2499; Eukaryota.
DR HOGENOM; CLU_007082_0_4_1; -.
DR InParanoid; Q8L7S6; -.
DR OMA; VEVWPMP; -.
DR OrthoDB; 545162at2759; -.
DR PhylomeDB; Q8L7S6; -.
DR BioCyc; ARA:AT1G65590-MON; -.
DR BRENDA; 3.2.1.52; 399.
DR PRO; PR:Q8L7S6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L7S6; baseline and differential.
DR Genevisible; Q8L7S6; AT.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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: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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..535
FT /note="Beta-hexosaminidase 3"
FT /id="PRO_0000420288"
FT ACT_SITE 329
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 292..334
FT /evidence="ECO:0000250"
FT DISULFID 506..532
FT /evidence="ECO:0000250"
SQ SEQUENCE 535 AA; 60014 MW; 9295E14DB073F966 CRC64;
MRGSGAKIAG VLPLFMLFIA GTISAFEDIE RLRIWPLPAQ VSHGGRRMYL SGDFKLVTEG
SKYGDASGIL KEGFDRMLGV VRLSHVISGD RNSSGTGGSA LLQGLHVIIS SSTDELEYGA
DESYKLVVPS PEKPSYAQLE AKSVYGALHG LQTFSQLCHF NLKKKVIEIL MTPWNIIDQP
RFSYRGLLID TSRHYLPLPV IKNVIDSMTY AKLNVLHWHI VDTQSFPLEI PSYPKLWNGA
YSSSQRYTFE DAAEIVNYAR RRGIHVLAEI DVPGHALSWG KGYPALWPSK NCQEPLDVSS
DFTFKVIDGI LSDFSKIFKF KFVHLGGDEV NTTCWSATPR IAQWLKKHRM SEKEAYQYFV
LRAQKIALSH GYEIINWEET FINFGSKLNR KTVVHNWLNT GLVENVTASG LRCIVSNQEF
WYLDHIDAPW QGFYANEPFQ NITDKKQQSL VLGGEVCMWG EHIDASDIEQ TIWPRAAAAA
ERLWTPYAKL AKNPNNVTTR LAHFRCLLNQ RGVAAAPLVG GGRVVPFEPG SCLAQ
