ID A0A0B0D6W6_9BACI Unreviewed; 697 AA.
AC A0A0B0D6W6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=LD39_11935 {ECO:0000313|EMBL:KHE70134.1};
OS Halobacillus sp. BBL2006.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=1543706 {ECO:0000313|EMBL:KHE70134.1, ECO:0000313|Proteomes:UP000030879};
RN [1] {ECO:0000313|EMBL:KHE70134.1, ECO:0000313|Proteomes:UP000030879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBL2006 {ECO:0000313|EMBL:KHE70134.1,
RC ECO:0000313|Proteomes:UP000030879};
RA Kirchner G., Treves D., Francis J.III.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BBL2006.";
RL Submitted (SEP-2014) 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 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:KHE70134.1}.
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DR EMBL; JRNX01000387; KHE70134.1; -; Genomic_DNA.
DR RefSeq; WP_035546768.1; NZ_JRNX01000387.1.
DR AlphaFoldDB; A0A0B0D6W6; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000030879; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR InterPro; IPR019800; Glyco_hydro_3_AS.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000030879};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..697
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038900970"
FT DOMAIN 152..486
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 529..697
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 697 AA; 76195 MW; 803EC43554861BEB CRC64;
MGRNSKKFIV SLLVLLMMLS QALFVPKQVE SEESDVSDLI LLQNVPEAST DIEGNVVTLQ
ALHIYKDGHF MKTDHNLSWK SSNKNVATVD EEGNVTISGH RGRTFISVSD GVHTDRIALD
YKVSHKKAAS PSLVKEKGER YDVIQKAIDG MTLEEKIGQM LMPDFRKWEG ENVTEMLPEI
EEQVQKYHLG GVILFRENVE TTEQTAKLVS DYKKASEKYG LLMAIDQEGG IVTRLQSGTD
MPGNMALGAT RSEEISHNVG HAIGEELDSL GINMNLAPVL DVNNNPDNPV IGVRSFGGDP
ELVANLGISY MKGLQEAGVA ATGKHFPGHG DTAVDSHLGL PEVPYDKERL KEVELYPFQQ
AMDAGIDAVM TAHVTFPKID DTKVISKKDG TKISLPATLS HKVLTGLMRE EMGHEGVIIT
DAMNMNAIAE HFGAVDAAIR AVKAGTDIVL MPVGLEEVAE GLINAVKSDE ITEERIEASV
ERVLTLKVHR GIIKSEQPES IDNKIQNAIE VVGSQEHKAV EREAAEKSIT LVKNDDVLPI
NADRNDHVVV VGRSFIESLG AAVRSHHENT SIIEMNSNYE FTDEQQAILD SADQIIVGTY
TYSVGTRAPE HPQMEMVQTL MRSMDAPVVA VGIRNPYDIM AYPEVDGYLA QYGFRDASFE
ATAAVIFGES EPSGKLPVTI PGEESGVLYP FGHGLTY
//
