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
//