ID   A0A1H0HGF3_9BACI        Unreviewed;       700 AA.
AC   A0A1H0HGF3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=SAMN04488053_10891 {ECO:0000313|EMBL:SDO18180.1};
OS   Alkalicoccus daliensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalicoccus.
OX   NCBI_TaxID=745820 {ECO:0000313|EMBL:SDO18180.1, ECO:0000313|Proteomes:UP000198778};
RN   [1] {ECO:0000313|Proteomes:UP000198778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10369 {ECO:0000313|Proteomes:UP000198778};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNIL01000008; SDO18180.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0HGF3; -.
DR   STRING; 745820.SAMN04488053_10891; -.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000198778; 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; IPR003343; Big_2.
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; PF02368; Big_2; 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:UP000198778};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..700
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011719060"
FT   DOMAIN          57..109
FT                   /note="BIG2"
FT                   /evidence="ECO:0000259|Pfam:PF02368"
FT   DOMAIN          157..489
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          532..700
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
SQ   SEQUENCE   700 AA;  75941 MW;  89526E33ACC52C26 CRC64;
     MKFKKSLLAS VLFLSPVFAA AQPAFAEGTQ GSEDLVLYQN IPEVEAELTE EGIDLRTLQI
     HEEGHYTEAT EELEWKSSNQ NVAAVNENGE VTFSGQRGKT FITVTNGEHT DRIGLQMKAD
     ASKKTGKGKP PNSIEVKKES GERYQVVDRA LASLSEDEKI GQMMMPDFRH FEGEEVTEML
     PEIEDLVEEY HLGGVILFAE NVVETEQTSR LVDDYQEAAE KFGLLVTIDQ EGGIVTRLQT
     GTHLPGNMAL GATRSPALAE MAGDVIGAEL SALGINTNLA PVVDVNNNPD NPVIGVRSFG
     EDPDLVAEMG MNYIAGLQQN GVAATAKHFP GHGDTAVDSH LGLPEVPHDM ERLKEVELYP
     FQQAMDHGID AIMTAHVTFP QIDGSKAISQ KDGTEISIPA TLSRTVLTDL MRDEMGYEGV
     VMTDAMNMNA ITDHFGPVDA SIRAINAGAD IILMPVGLEE VFSGVREALS SGEIQQEEID
     QSVKRILTLK MERGIFKTEE TLNQEEKAEN ALQVIGAEAH KAVEQEIADR SITMVKNEDV
     LPISMESDEE IVVVGTSFIG SLAGALQNYH ENVTTITLSS GQTALTSSQQ ELIEEAGQVI
     IGSYTFNVAG RSPENAAMQV FHQILDLKED VIGVGIRNPY DIMGYQDVDG YLTQYGFRDA
     SFAATASVIF GENNPTGALP VTIPDHENGV LYPFGTGLSY
//