ID W1SH81_9BACI Unreviewed; 687 AA.
AC W1SH81;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=BAVI_11734 {ECO:0000313|EMBL:ETI68577.1};
OS Neobacillus vireti LMG 21834.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI68577.1, ECO:0000313|Proteomes:UP000018877};
RN [1] {ECO:0000313|EMBL:ETI68577.1, ECO:0000313|Proteomes:UP000018877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI68577.1,
RC ECO:0000313|Proteomes:UP000018877};
RX PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT potent source and sink for nitric and nitrous oxide under high nitrate
RT conditions.";
RL Environ. Microbiol. 16:3196-3210(2014).
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:ETI68577.1}.
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DR EMBL; ALAN01000065; ETI68577.1; -; Genomic_DNA.
DR RefSeq; WP_024028534.1; NZ_ALAN01000065.1.
DR AlphaFoldDB; W1SH81; -.
DR STRING; 220686.AA980_19070; -.
DR PATRIC; fig|1131730.3.peg.2443; -.
DR eggNOG; COG1472; Bacteria.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000018877; 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 PRINTS; PR00133; GLHYDRLASE3.
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:UP000018877};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..687
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038675075"
FT DOMAIN 145..479
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 522..677
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 687 AA; 73737 MW; ECE2DF971CFE4923 CRC64;
MRKFLKTLIT SCLGFALLLT GIPHSGATAA SAIKDVVIDL NVPQVTREVK DNQIDLNALN
VYDDGHFMLA SEHLTWKSSN KNVASVKDGA VTLSGHNGKT FISVSDGKYN DRISIQFKGN
QGEILVEKEK GSRYSIIGKA IKQMTIEEKV GQMLMPDFRT WKGQNVTVMN DEIVQLVKKY
HLGGVILFRE NTETAAQTTK LVSAYQDAAE KYGLLISIDQ EGGIVTRLQS GTDFPGSMAL
GASRSEELAE KVGKAIGEEL NAVGINMNFG PVLDTNNNPD NPVIGVRSFG EDPALVAKLG
NAYIKGLHET GTAATAKHFP GHGDTATDSH LGLPEVPHDI DRLKKVELYP FQQAMDAGID
AVMSAHVTFP KIDNTKAISK KDGTEIAVPG TLSHKVLTGL MREDMGFKGV IVTDAMNMQA
IADHFGPVDA AIRAVKAGTD IVLMPVGLES VANGLYDAVK SGDISVDRLD QSVERILTLK
LNRGIVKAEV EKSLDEKVSN AEKTWRSAEH LQIEKEAAAK SITLVKNSGV LPLKAGVNDK
IVVVGSSAPT LLAEVQKHHK NVTMINTAAP LTGANLTEAK TAKYIIVGTN TSTVSGRLPS
ASLMKLANQM IDETDASVIG VGIRNPYDIM AYPKVDAYLT QYGTKDVSFE AAVNTIFGVN
KPSAKLPVTI FNQDGSVLYG FDHGLGF
//
