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   24-JAN-2024, entry version 140.
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;
GN   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.Q8L7S6; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   GlyCosmos; Q8L7S6; 5 sites, No reported glycans.
DR   PaxDb; 3702-AT1G65590-1; -.
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; AT1G65590; HEXO3.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_4_1; -.
DR   InParanoid; Q8L7S6; -.
DR   OMA; VVEVWPM; -.
DR   OrthoDB; 178991at2759; -.
DR   PhylomeDB; Q8L7S6; -.
DR   BioCyc; ARA:AT1G65590-MONOMER; -.
DR   BRENDA; 3.2.1.52; 399.
DR   PRO; PR:Q8L7S6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8L7S6; baseline and differential.
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   CDD; cd06562; GH20_HexA_HexB-like; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 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; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR   Genevisible; Q8L7S6; AT.
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
//