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Beta-hexosaminidase 3 (EC 3.2.1.52) (Beta-GlcNAcase 3) (Beta-N-acetylhexosaminidase 3) (Beta-hexosaminidase 1) (AtHEX1) (N-acetyl-beta-glucosaminidase 3)

 HEXO3_ARATH             Reviewed;         535 AA.
Q8L7S6; O04477;
28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-APR-2018, entry version 114.
RecName: Full=Beta-hexosaminidase 3;
EC=3.2.1.52;
AltName: Full=Beta-GlcNAcase 3;
AltName: Full=Beta-N-acetylhexosaminidase 3;
AltName: Full=Beta-hexosaminidase 1;
Short=AtHEX1;
AltName: Full=N-acetyl-beta-glucosaminidase 3;
Flags: Precursor;
Name=HEXO3; Synonyms=HEX1; OrderedLocusNames=At1g65590;
ORFNames=F5I14.13;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
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.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND
REVIEW.
PubMed=17636254; DOI=10.1074/jbc.M704235200;
Gutternigg M., Kretschmer-Lubich D., Paschinger K., Rendic D.,
Hader J., Geier P., Ranftl R., Jantsch V., Lochnit G., Wilson I.B.H.;
"Biosynthesis of truncated N-linked oligosaccharides results from non-
orthologous hexosaminidase-mediated mechanisms in nematodes, plants,
and insects.";
J. Biol. Chem. 282:27825-27840(2007).
[5]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, CATALYTIC
ACTIVITY, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY,
AND NOMENCLATURE.
PubMed=17644627; DOI=10.1104/pp.107.101162;
Strasser R., Bondili J.S., Schoberer J., Svoboda B., Liebminger E.,
Glossl J., Altmann F., Steinkellner H., Mach L.;
"Enzymatic properties and subcellular localization of Arabidopsis
beta-N-acetylhexosaminidases.";
Plant Physiol. 145:5-16(2007).
[6]
FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=21252225; DOI=10.1074/jbc.M110.178020;
Liebminger E., Veit C., Pabst M., Batoux M., Zipfel C., Altmann F.,
Mach L., Strasser R.;
"Beta-N-acetylhexosaminidases HEXO1 and HEXO3 are responsible for the
formation of paucimannosidic N-glycans in Arabidopsis thaliana.";
J. Biol. Chem. 286:10793-10802(2011).
-!- FUNCTION: 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-6SO(4)) 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. {ECO:0000269|PubMed:17636254,
ECO:0000269|PubMed:17644627, ECO:0000269|PubMed:21252225}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
{ECO:0000269|PubMed:17644627}.
-!- ENZYME REGULATION: Slightly inhibited by N-acetylcastanospermine.
{ECO:0000269|PubMed:17636254}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.2 mM for pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius)
{ECO:0000269|PubMed:17636254, ECO:0000269|PubMed:17644627};
Vmax=50.3 umol/min/mg enzyme with pNP-GlcNAc as substrate (at pH
4.6 and 37 degrees Celsius) {ECO:0000269|PubMed:17636254,
ECO:0000269|PubMed:17644627};
pH dependence:
Optimum pH is 4-5. {ECO:0000269|PubMed:17636254,
ECO:0000269|PubMed:17644627};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17644627,
ECO:0000269|PubMed:21252225}.
-!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
siliques. {ECO:0000269|PubMed:17644627}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:17644627}.
-!- DISRUPTION PHENOTYPE: Reduced amounts of paucimannosidic N-
glycans-containing glycoproteins in roots and leaves.
{ECO:0000269|PubMed:21252225}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB60911.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AC001229; AAB60911.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE34399.1; -; Genomic_DNA.
EMBL; AY128283; AAM91092.1; -; mRNA.
EMBL; BT000831; AAN33206.1; -; mRNA.
PIR; A96681; A96681.
RefSeq; NP_176737.2; NM_105233.5.
UniGene; At.24164; -.
ProteinModelPortal; Q8L7S6; -.
STRING; 3702.AT1G65590.1; -.
CAZy; GH20; Glycoside Hydrolase Family 20.
PaxDb; Q8L7S6; -.
PRIDE; Q8L7S6; -.
EnsemblPlants; AT1G65590.1; AT1G65590.1; AT1G65590.
GeneID; 842871; -.
Gramene; AT1G65590.1; AT1G65590.1; AT1G65590.
KEGG; ath:AT1G65590; -.
Araport; AT1G65590; -.
TAIR; locus:2034147; AT1G65590.
eggNOG; KOG2499; Eukaryota.
eggNOG; COG3525; LUCA.
HOGENOM; HOG000157972; -.
InParanoid; Q8L7S6; -.
KO; K12373; -.
OMA; DSSFPYE; -.
OrthoDB; EOG093609RX; -.
PhylomeDB; Q8L7S6; -.
BioCyc; ARA:AT1G65590-MONOMER; -.
BRENDA; 3.2.1.52; 399.
Reactome; R-ATH-1660662; Glycosphingolipid metabolism.
Reactome; R-ATH-2022857; Keratan sulfate degradation.
Reactome; R-ATH-2024101; CS/DS degradation.
Reactome; R-ATH-2160916; Hyaluronan uptake and degradation.
Reactome; R-ATH-6798695; Neutrophil degranulation.
PRO; PR:Q8L7S6; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q8L7S6; baseline and differential.
Genevisible; Q8L7S6; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IDA:TAIR.
GO; GO:0015929; F:hexosaminidase activity; IDA:TAIR.
GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
Gene3D; 3.30.379.10; -; 1.
InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
InterPro; IPR015883; Glyco_hydro_20_cat.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR029018; Hex-like_dom2.
InterPro; IPR029019; HEX_eukaryotic_N.
Pfam; PF00728; Glyco_hydro_20; 1.
Pfam; PF14845; Glycohydro_20b2; 1.
PIRSF; PIRSF001093; B-hxosamndse_ab_euk_; 1.
PRINTS; PR00738; GLHYDRLASE20.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF55545; SSF55545; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Glycosidase; Hydrolase; Membrane; Reference proteome; Signal.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 535 Beta-hexosaminidase 3.
/FTId=PRO_0000420288.
ACT_SITE 329 329 Proton donor. {ECO:0000250}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 331 331 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 405 405 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 441 441 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 496 496 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 292 334 {ECO:0000250}.
DISULFID 506 532 {ECO:0000250}.
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


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