ID A0A1M3HRH5_9SPHI Unreviewed; 868 AA.
AC A0A1M3HRH5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BGO55_31145 {ECO:0000313|EMBL:OJW61327.1};
OS Sphingobacteriales bacterium 50-39.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895841 {ECO:0000313|EMBL:OJW61327.1, ECO:0000313|Proteomes:UP000184242};
RN [1] {ECO:0000313|EMBL:OJW61327.1, ECO:0000313|Proteomes:UP000184242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=50-39 {ECO:0000313|EMBL:OJW61327.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJW61327.1}.
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DR EMBL; MKTZ01000001; OJW61327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3HRH5; -.
DR STRING; 1895841.BGO55_31145; -.
DR Proteomes; UP000184242; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..868
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013019221"
FT DOMAIN 34..190
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT ACT_SITE 530
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 868 AA; 96091 MW; 32F0CC8DDECAC6BB CRC64;
MKRIFIFCLL AGCSVGLAAQ VPAGGAGMRA GMADRLAIRW TCVKNIYEMP NRSVSRLTLM
NKGNGAFPLS GWGIYFNSNR SIDPHSVIGG QIEHINGDLY CLRLQASDGV RRGLKPGGTL
PITFTSSDLS INISDAPIGF YLVWDDRPAQ GHTIHDYQVD RIDDPMLGAL TPGMEYQRNM
GFRQMDTAKV SRVYPTPLWY RDSGSAFLLD GKTPVVADAG FEGEAAYLST ALAGVIGRRP
VVKGGASGKA IILRHVDEAE GQGWADSSAY RMEITDKHIL ISASAPVGIF YGIQSFLSAL
PAGVWRGAQS SVMIPGLVVA DRPRFAVRAL MLDVARNFRS EEEVRRVLDL MALCKLNVLH
LHLCDDEGWR LEIPSLPELT EVGAYRGLET GGRVCLPPSF GSGPLAGMGA GSGYYSKASF
ISLLRYARER HIEVVPEIEC PGHARAAIKA MDARYKKYAR QGNMEEARRY LLRDTMDRSV
YESAQMWRDN VIAVALPSVY RWFDKVIGEV CAMYKEAGAP LRTIHLGGDE LPAGVWEQSP
ACRALMEQDR SLASPGDARW YFYNRLDSLV KRRGLVMSGW EEVALRKVTE GGKTKVVPDS
AWKERDSRVH VWNNMIGGGD EDLPYRLANA GYKVILSCVS NNYYDMASNK SFDERGYHWG
GFLDVDKPYA FMPYDYYRNA REDYTGGPVA AGYFRDKELL TEEGKKNILG IEGLLWAENL
PTDERMEYML LPKLLGTAER AWAPDPMWAM ETDSAVTARL YAAAWNGFMN VVGQRLLPRL
SYMNGGYAYR IPVPGVSIEG GLVRANLPMP GFMVRYTTDG SVPGASSRQY DGPVAERKLI
RLRTFDVRGR GGRTVDADNR VSADDTAK
//
