ID J3JT78_DENPD Unreviewed; 593 AA.
AC J3JT78;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 08-NOV-2023, entry version 39.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:AEE61398.1};
RN [1] {ECO:0000313|EMBL:AEE61398.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Midgut and adhering fatbody of emerged adults of both sexes
RC after feeding on lodgepole pine for up to 64 h
RC {ECO:0000313|EMBL:AEE61398.1};
RX PubMed=22516182; DOI=10.1016/j.ibmb.2012.03.010;
RA Keeling C.I., Henderson H., Li M., Yuen M., Clark E.L., Fraser J.D.,
RA Huber D.P., Liao N.Y., Roderick Docking T., Birol I., Chan S.K.,
RA Taylor G.A., Palmquist D., Jones S.J., Bohlmann J.;
RT "Transcriptome and full-length cDNA resources for the mountain pine beetle,
RT Dendroctonus ponderosae Hopkins, a major insect pest of pine forests.";
RL Insect Biochem. Mol. Biol. 42:525-536(2012).
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:0000256|ARBA:ARBA00001231,
CC ECO:0000256|PIRNR:PIRNR001093};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285, ECO:0000256|PIRNR:PIRNR001093}.
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DR EMBL; BT126434; AEE61398.1; -; mRNA.
DR RefSeq; XP_019760631.1; XM_019905072.1.
DR RefSeq; XP_019768087.1; XM_019912528.1.
DR AlphaFoldDB; J3JT78; -.
DR HOGENOM; CLU_807921_0_0_1; -.
DR OrthoDB; 178991at2759; -.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
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:SF48; BETA-N-ACETYLHEXOSAMINIDASE; 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.
PE 2: Evidence at transcript level;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001093};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001093};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..593
FT /note="Beta-hexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003771275"
FT DOMAIN 61..183
FT /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14845"
FT DOMAIN 207..550
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 365
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ SEQUENCE 593 AA; 66107 MW; 173C8789BA651CDE CRC64;
MMGRVFLLLF AAFLPNCSGY NSKWHYECTD GYCEKTLITE NTTSPLSLAE CNILCLDYAS
VWPQPTGNIS IDNLTLIDVS AFSFTSEENT TISSLVEAAF GIFTCQFTLQ LPRKPFLRNA
SSNGSAVQVQ FEITDQDTEQ LSFGTNESYT VRGLATDDGA INVTITAETF FGARHALETL
SQLVVFDDLR NRTLFPASIA VSDQPAFNWR GVCLDTARNY ITPKAIKRTL RAMAASKLNT
FHWHLTDTAS FPYVSSSHPE LSEYGAYSSS KVYTDDDVKS IIEYARVRGI RVVPELDSPA
HVGEGWQTSG VLTCFNQKPW TDYCAEPPCG QFDPSQSGVY DILEDLYGDL LTQFGTDVFH
MGGDEVNVAC WNITSNLTAW MVDEMGWGLS KSDFQEKVWP YFQNESAQRL YKQAGAQIPI
ILWSSDLTAL DNVTSILPPE DYIIQIWDSA DSSSIQTLLS QNYSVILSNY DGLYLDCGFA
GWVTNGTNWC SPYKGWQTVY DNKPVNIAGT SVAQVLGGET VLWTEEAESD TVDSRLWPRA
AAFAETLWSA PETTWEAAEE RMLFHRERLV ALGIGADALQ PEWCRRNQQN CPT
//
