ID   B1JYR7_BURO0            Unreviewed;       828 AA.
AC   B1JYR7;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
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   OrderedLocusNames=Bcenmc03_2831 {ECO:0000313|EMBL:ACA91990.1};
OS   Burkholderia orbicola (strain MC0-3).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex;
OC   Burkholderia orbicola.
OX   NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA91990.1, ECO:0000313|Proteomes:UP000002169};
RN   [1] {ECO:0000313|Proteomes:UP000002169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3.";
RL   Submitted (FEB-2008) 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}.
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DR   EMBL; CP000958; ACA91990.1; -; Genomic_DNA.
DR   RefSeq; WP_012329254.1; NC_010508.1.
DR   AlphaFoldDB; B1JYR7; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   GeneID; 83049615; -.
DR   KEGG; bcm:Bcenmc03_2831; -.
DR   HOGENOM; CLU_007082_4_1_4; -.
DR   Proteomes; UP000002169; Chromosome 1.
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   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   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; 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; 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; 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   Glycosidase {ECO:0000313|EMBL:ACA91990.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACA91990.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..828
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002763831"
FT   DOMAIN          54..217
FT                   /note="Chitobiase/beta-hexosaminidases N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01081"
FT   REGION          199..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        541
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   828 AA;  90097 MW;  6F96D0FC724C44D8 CRC64;
     MKRTLPSLIA GLLIAVLSPA AISALPASAA AGATAGSAQA AAAQAASLAT QLSNGLALRV
     AVDNNHAAAA GVPCADLGAD GAACATGRLI LQNRGHQAIA DGGWKLYLHS IRRLLRIDRP
     GFALRRLTGD LYELTPQPGS VRLAPGERIE LPFVAEYWLL RYSDVIPRPY VVVDGAPPAV
     LRYNDTDNEL RYVESLPADA QNNSTGNAPP VAARPDPGRA LPSVKRELPL PGTLELRGVE
     LALPDLPDAQ VAALHERATT LGLDGAGVPV RGFVAPRRLP ADIATPGGYR LAIGPRGVLI
     EGYDRAGLYY GVQTLYSLAP AGGGPIPAML VEDAPRFTHR GMHVDLARNF KQPATLRRLI
     DQMSAYKLNR LHLHLSDDEG WRIEIPGLPE LTEIGSRRCH DPSETRCLLP QLGSGPDNRS
     GGGYLTRDDY VALVRYAAAR FVQIIPEIDM PAHARAAVVT MEARYRRLHA AGREQEASAY
     RLLDPQDTTN LTTVQFYDRR SDLNPCVPGA LNFASKVIRE IAAMHADAQA PLQTWHYGGD
     EAKNIFLGGG FQALNGTDPN KGRIDLAAQD KPWARSPACT ALLQRGEIKS IDELPTRFAK
     QVSAAVNANG IGTMAAWQDG IKHANGPQDF STRHVMVSLW DTIFWGASDS ARDLSGKGYQ
     TVLALPDYLY FDFPYTLNPR ERGYYWGSHA TDEYKVFSLA PENLPQNAEV MGDRDGNPFE
     VTGTGPAPRI EGMQGQAWGE VMRNDTFLEY MTYPRLLALA ERAWHRADWE LPYAAGMRFK
     RGDTHHVDIA ALQRDWAGFA TLLTQRELPK LERAGVGYRK PTFTLTNP
//