ID   C3QMG4_9BACE            Unreviewed;      1003 AA.
AC   C3QMG4;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=BSCG_00073 {ECO:0000313|EMBL:EEO53148.1};
OS   Bacteroides sp. 2_2_4.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=469590 {ECO:0000313|EMBL:EEO53148.1};
RN   [1] {ECO:0000313|EMBL:EEO53148.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_2_4 {ECO:0000313|EMBL:EEO53148.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., Lander E.,
RA   Nusbaum C., Ilzarbe M., Galagan J., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. strain 2_2_4.";
RL   Submitted (DEC-2008) 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}.
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DR   EMBL; EQ973355; EEO53148.1; -; Genomic_DNA.
DR   RefSeq; WP_008774582.1; NZ_EQ973355.1.
DR   AlphaFoldDB; C3QMG4; -.
DR   HOGENOM; CLU_012120_0_0_10; -.
DR   Proteomes; UP000003969; 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   PRINTS; PR00133; GLHYDRLASE3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1003
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002931360"
FT   DOMAIN          57..368
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          602..985
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
FT   COILED          451..478
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1003 AA;  111763 MW;  E6836A6DFD917ECC CRC64;
     MKIIPSIVTL LFLIAAGTVS SPAQNATTVE PLLVYKALQD KDCRHWVDSV MDKLSFKEKV
     GQLFIYTIAP VDTKRNLELL REVIDTYKVG GLLFSGGKMQ NQVELTNRAQ RQAKVPLMIT
     FDGEWGLAMR LRGMPVFPRN MVLGCIRDNK LLYEYGREVA RQCRQIGVQV NFAPVADVNI
     NPENPVINTR SFGEDPIQVA DKVIAYASGL ESGGVLSVCK HFPGHGDTDV DSHKALPVLP
     FTRERLDSVE LYPFKEAIRA GLGGMMVGHL QVPVIEPIGG LPSSLSRNVV YDLLTDELAF
     KGLIFTDALA MKGVAGNGNV SLQALKAGND MVLSPRNLKE EIPAVLEAIE KGELTREDIE
     SKCRKVLTYK YVLGLKKKSY VQLSGLEQRI NSPQTRDLVR RLNLAAITVL NNKNHILPLH
     TDKEQTIALL EVGDPGETDA LAKQLSRYTS LARFSLRANQ TKEENQRLRD SLSTYKRIIV
     AVSEQRLAPY QPFFAKFVPE SPAIYLFFTP GKMMLQIQRA VAHASAVVLG HSYSSDVQRQ
     VADVLFAKAS ADGQLSASLG ELFPTGAGVT ITPKTPLHFV PEEYGLSSAH LKRIDSIALD
     GIHQGAYPGC QVVVLKNGHI MFDKAFGTYT GKGSPRVEST NIYDLASLSK TTGTLLAIMK
     LYDKGRFNLT DKISDHLPFL QRTDKKDITI QEILYHQSGL PSWIPFYQEA IDKDSYDGRL
     FSARKDIHHP VQIGTTTWAN PKFKFKSEYI SPVKTGDYTV QICDSLWLNR SFRKVIEEKI
     AEAPLKQKRY VYSDVGFILL GMLVEQLAGM PMEAYLQREF YEPMGLEHTG YLPLRRFAKS
     EIVPSNKDRF LRKETLQGFV HDEASAFFGG LAGNAGLFST ARDVARVYQM LLNGGEIDGQ
     RYLSKETCQL FTTETSKISR RGLGFDKPDA DDPKKGNCAP AAPAEVYGHT GFTGTCAWVD
     PVNELVYVFL SNRIYPDVTN RKLNQLHIRE RIQGAIYDAM KKK
//