ID   HEXC_BOMMO              Reviewed;         596 AA.
AC   P49010;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   24-JAN-2024, entry version 115.
DE   RecName: Full=Chitooligosaccharidolytic beta-N-acetylglucosaminidase;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-GlcNAcase;
DE   AltName: Full=Beta-N-acetylhexosaminidase;
DE   AltName: Full=Beta-hexosaminidase;
DE   Flags: Precursor;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Kinshu X Showa;
RX   PubMed=7766021; DOI=10.1271/bbb.59.219;
RA   Nagamatsu Y., Yanagisawa I., Kimoto M., Okamoto E., Koga D.;
RT   "Purification of a chitooligosaccharidolytic beta-N-acetylglucosaminidase
RT   from Bombyx mori larvae during metamorphosis and the nucleotide sequence of
RT   its cDNA.";
RL   Biosci. Biotechnol. Biochem. 59:219-225(1995).
CC   -!- FUNCTION: Active during metamorphosis to degrade chitin.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR   EMBL; S77548; AAC60521.1; -; mRNA.
DR   PIR; JC2539; JC2539.
DR   RefSeq; NP_001037466.1; NM_001044001.1.
DR   AlphaFoldDB; P49010; -.
DR   SMR; P49010; -.
DR   STRING; 7091.P49010; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   PaxDb; 7091-BGIBMGA005899-TA; -.
DR   GeneID; 693032; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_1_1; -.
DR   InParanoid; P49010; -.
DR   OrthoDB; 178991at2759; -.
DR   BRENDA; 3.2.1.52; 890.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IDA:UniProtKB.
DR   GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Direct protein sequencing;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..596
FT                   /note="Chitooligosaccharidolytic beta-N-
FT                   acetylglucosaminidase"
FT                   /id="PRO_0000012013"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        377
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   596 AA;  68213 MW;  F302963E94A3A2FF CRC64;
     MWLQAICIYT VFIIIGCGIP TAAEEHSLWR WTCENNRCTK IRNEPENKEP VLSLEACKMF
     CDDYGLLWPK PTIETNLGNF LSKINMNTID IQITKQGKSD DLLTAAADRF KTLVSSSVPK
     GFSAKAAGKS VTVYLVNENP YIREFSLDMD ESYELYISST SSDKVNATIR GNSFFGVRNG
     LETLSQLIVY DDIRNNLLIV RDVTIKDRPV YPYRGILLDT ARNFYSIDSI KRTIDAMAAV
     KLNTFHWHIT DSQSFPLVLQ KRPNLSKLGA YSPTKVYTKQ DIREVVEYGL ERGVRVLPEF
     DAPAHVGEGW QDTGLTVCFK AEPWTKFCVE PPCGQLNPTK EELYDYLEDI YVEMAEAFES
     TDMFHMGGDE VSERCWNSSE EIQNFMIQNR WNLDKSSFLK LWNYFQKNAQ DRAYKAFGKR
     LPLILWTSTL TDYTHVEKFL DKDEYIIQVW TTGADPQIQG LLQKGYRLIM SNYDALYFDC
     GFGAWVGSGN NWCSPYIGGQ KVYGNSPAVM ALSYRDQILG GEVALWSEQS DPATLDGRLW
     PRAAAFAERM WAEPSTAWQD AEHRMLHVRE RLVRMGIQAE SLEPEWCYQN QGLCYG
//