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Database: UniProt
Entry: A0A069D416_9BACE
LinkDB: A0A069D416_9BACE
Original site: A0A069D416_9BACE 
ID   A0A069D416_9BACE        Unreviewed;       866 AA.
AC   A0A069D416;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=JCM15093_27 {ECO:0000313|EMBL:GAK34954.1};
OS   Bacteroides graminisolvens DSM 19988 = JCM 15093.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1121097 {ECO:0000313|EMBL:GAK34954.1, ECO:0000313|Proteomes:UP000027601};
RN   [1] {ECO:0000313|EMBL:GAK34954.1, ECO:0000313|Proteomes:UP000027601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15093 {ECO:0000313|EMBL:GAK34954.1,
RC   ECO:0000313|Proteomes:UP000027601};
RX   PubMed=25736980;
RA   Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA   Hattori M., Ohkuma M.;
RT   "Distribution and evolution of nitrogen fixation genes in the phylum
RT   bacteroidetes.";
RL   Microbes Environ. 30:44-50(2015).
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}.
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:GAK34954.1}.
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DR   EMBL; BAJS01000001; GAK34954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A069D416; -.
DR   STRING; 1121097.GCA_000428125_00497; -.
DR   eggNOG; COG1472; Bacteria.
DR   eggNOG; COG1680; Bacteria.
DR   Proteomes; UP000027601; 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; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 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; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
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   PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027601}.
FT   DOMAIN          1..227
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          463..836
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   866 AA;  95991 MW;  A0A9276CE3579349 CRC64;
     MVLGCIQDDR LIYEYGQEMA RQCRELGVQV NFAPVADVNI NPQNPVINVR SFGENPLLVA
     DKVIAYASGL ESGRVLSVAK HFPGHGDTDV DSHKALPVLP FTRERLDSVE LYPFRKLIHA
     GLGGVMVGHL QVPVFEPVGK LPSSLSRNVV YTLLTEKMAF KGLIFTDALA MKGVSSAQKV
     CLQALKAGND VVLAPRDVKK EIDYVVEAVK KGEFSEEEID ERCRKVLLFK YAMGLNRKPV
     VRLSGLERRI NTPHTRDLIR RLNLAAVTVL NNEKGVLPIH PDVKKVAVLT VGKAKELEAF
     TNELKKYVEV HTFELGKQMP DSLQQKLRDS LSAYRRIIVP VNEIRLAPYQ SFFAKFTPQV
     PVVYAFFTPA KLMLQIHRAI SNASSVVLGH TDSDEVQEQI AALLFGKAAA NGRLSAGIGG
     LFRAGAGLTV TTSTPYHFVP EEYGMRSEVL QSIDTIAMRG IHAGAYPGCE IVVLKNGRTM
     YNKSFGTFTY EDEKAVSTND IYDLASLSKT TGTLLAVMKL YDNGRFNLSD PIGDYLPFLK
     GTNKAKITIR ELLLHQSGLP SGLVFYQDAI DKKSYKGSLF KGSKDALHTV QIGPKTFAQP
     GFRFKEGLTS AVGGGDYTLH VADSLWLHKS FRDVMLKKIA DAPLKGKKYV YSCLNFILLQ
     QLVEQLAGVP MDEFLTHEFY RPMNLSRTAY LPLRYFRKEN IVPSSVDRFL RKETLQGFVH
     DESAAFLGGI SGNAGLFSTA YEVSQVYQML LNGGEYEGQR YLSKETCQLF TTETSKISRR
     GLGFDKPDAE DVGSSPCAPS APASVYGHTG FTGTCAWTDP DNGLVYVFLS NRTYPDAWVN
     KLSNLEIREH IQETLYRALM QPAPVE
//
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