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Database: UniProt
Entry: A0A1S9A8D7_9BURK
LinkDB: A0A1S9A8D7_9BURK
Original site: A0A1S9A8D7_9BURK 
ID   A0A1S9A8D7_9BURK        Unreviewed;       823 AA.
AC   A0A1S9A8D7;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
DE   AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00030512};
DE   AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000256|ARBA:ARBA00033000};
GN   ORFNames=B0920_20605 {ECO:0000313|EMBL:OON59689.1};
OS   Massilia sp. KIM.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1955422 {ECO:0000313|EMBL:OON59689.1, ECO:0000313|Proteomes:UP000190838};
RN   [1] {ECO:0000313|EMBL:OON59689.1, ECO:0000313|Proteomes:UP000190838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM {ECO:0000313|EMBL:OON59689.1,
RC   ECO:0000313|Proteomes:UP000190838};
RA   Vikram S., Kabwe M.H., Bezuidt O., Govender N., Makhalanyane T.P.;
RT   "Genome sequence of Massilia sp. KIM isolated from grassland biome soil in
RT   South Africa.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OON59689.1}.
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DR   EMBL; MVAD01000003; OON59689.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9A8D7; -.
DR   STRING; 1955422.B0920_20605; -.
DR   OrthoDB; 9763537at2; -.
DR   Proteomes; UP000190838; Unassembled WGS sequence.
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:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02847; E_set_Chitobiase_C; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR004866; CHB/HEX_N_dom.
DR   InterPro; IPR004867; CHB_C_dom.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR015882; HEX_bac_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR   Pfam; PF03173; CHB_HEX; 1.
DR   Pfam; PF03174; CHB_HEX_C; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SMART; SM01081; CHB_HEX; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190838}.
FT   DOMAIN          14..156
FT                   /note="Chitobiase/beta-hexosaminidases N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01081"
FT   ACT_SITE        493
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   823 AA;  89756 MW;  9B9DBE50E7059B27 CRC64;
     MKPIPEPSSR PGAAPVAVSW ECLTNTARDD RFRARLVLAN VSDAAIAPGW RLYFNTARKP
     LAASATPGYA IEHLNGDLCR LGMPDGGPWL PGQRHVIDYD CLHWAISVTD APLGFHLVTA
     EGEAIDLGDP RIAPFARPEQ RMRTSYDLLP TEDAARRHRR NAGLRQLPED EIGRITPRPV
     HARLGGATCR LSPGAPLVHD ASLGREAALL SAMLAALPDG PPGEAGVELR LGAVALEDPS
     EEAYELEIGA RRVCVRGRSA HGVFNGLQTL AQLLGPDGSL PLGQVLDAPR FAYRGMMLDV
     ARHFSSVATV LRLLDCMAAY KLNRFHFHLT DDEGWRLAIA ALPELTAIGS RRGVGASCLP
     PSYGSGARIE GSAGTGFYSA EEFVAILRHA HARHIEVIPE FNMPGHARAA VVAMRARYER
     LLAAGDRAGA EEYLLSDPDD RSEYESVQLW HDNVICIALP SVDRFIDTVV GEVCALYREA
     GAPLRVIHTG GDEVPAGAWL GSPLCRAKME REGWTRIDQL HDDFVARCRA ILARHGLGFA
     GWEETALVEV TGEGMRPNPR FAGPDFHAYV WNNAWGSGQE DCAYRLANAG YRVVLANAAN
     LYFDLAYAKH PEEPGYYWAG FVETRHAFAF CPLDVRVTAD LDPLGRPLDP RVLAAMQPLD
     AAGKERIAGL QGQLWGENAV DAGRIDYLAL PRLIALAERA WSPDPGWQHV ADEAQRAAAI
     ERDWNEFANR LARRELPRLD RAPEPYRYRL PPPGVALQDG AAHANVALPG LALHYTVDGS
     EPSASGPRYQ APVPLAPGSR FRIASFDTRG RRSRIVSLIL DTP
//
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