ID A0A174Q4F7_9BACE Unreviewed; 690 AA.
AC A0A174Q4F7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN Name=exo I_2 {ECO:0000313|EMBL:CUP68133.1};
GN Synonyms=exo I_1 {ECO:0000313|EMBL:CUO91388.1};
GN ORFNames=DW190_15165 {ECO:0000313|EMBL:RHH87657.1}, ERS852494_01079
GN {ECO:0000313|EMBL:CUO91388.1}, ERS852558_00766
GN {ECO:0000313|EMBL:CUP68133.1};
OS Bacteroides caccae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=47678 {ECO:0000313|EMBL:CUP68133.1, ECO:0000313|Proteomes:UP000095725};
RN [1] {ECO:0000313|Proteomes:UP000095657, ECO:0000313|Proteomes:UP000095725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5834880 {ECO:0000313|EMBL:CUO91388.1,
RC ECO:0000313|Proteomes:UP000095657}, and 2789STDY5834946
RC {ECO:0000313|EMBL:CUP68133.1, ECO:0000313|Proteomes:UP000095725};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RHH87657.1, ECO:0000313|Proteomes:UP000283512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM16-49B {ECO:0000313|EMBL:RHH87657.1,
RC ECO:0000313|Proteomes:UP000283512};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; CZAI01000002; CUO91388.1; -; Genomic_DNA.
DR EMBL; CZBL01000002; CUP68133.1; -; Genomic_DNA.
DR EMBL; QRKD01000016; RHH87657.1; -; Genomic_DNA.
DR RefSeq; WP_055170451.1; NZ_VVYO01000003.1.
DR AlphaFoldDB; A0A174Q4F7; -.
DR STRING; 47678.ERS852494_01079; -.
DR Proteomes; UP000095657; Unassembled WGS sequence.
DR Proteomes; UP000095725; Unassembled WGS sequence.
DR Proteomes; UP000283512; Unassembled WGS sequence.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06563; GH20_chitobiase-like; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:CUP68133.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CUP68133.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095657};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..690
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014252387"
FT DOMAIN 30..151
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 155..497
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT DOMAIN 579..681
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|Pfam:PF00754"
FT ACT_SITE 328
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 690 AA; 77557 MW; FBE49F5AAD550326 CRC64;
MNIRNRCTKV CLFLWVLGMC FAAHPLHAQS VIPVPLKIEQ GTGSFLLSEK TKLYTNIQGG
EARLLESYLQ ALPVHLKKGK KKDTQNVLSL LITEKSEQLP SPESYTLSVT PERILIRATS
GAGLFYGIQT LLQLSQPSGT GYSIASVEVQ DSPRFAYRGL MLDVSRHFFS KEFVKKQIDA
LAFYKINRLH LHLTDAAGWR IEIKKYPLLT EFAAWRTDAN WKTWWNGGRK YLRFDEPGAS
GGYYTQDDIR EIVEYARQHF ITIIPEIEMP AHSEEVLAAY PQLSCAGEPY KNADFCIGNE
ETFTFLENVL TEVMALFPSE YIHIGGDEAG MAAWKTCPKC QKRMKDEHLS HVDELQSYLI
HRIEKFLNDH GRRLLGWDEI LKGGLAPNAT VMSWRGEEGG ITAVTSGHRA IMTPGGYCYL
DSYQDAPYSQ PEAIGGYLPL KKVYSYNPVS TSLSAEQAKL VYGAQVNLFT EYVPTPEHVE
YMLYPRTLAL AEVAWSAPER KSWPDFYARA LKAVTDLQAK GYHTFDLKSE IGSRPESLQP
LTHLALGKKV IYNAPYNSSY AAQGDVTLTD GIRGDWTYGD GAWQGFISKN RLDVTVDMEN
ETTIHSVTAA FMQVVGAEVF LPASVVISVS DDGVNFTELK HQDFVVNKEE AIKFSDVSWE
GTVKGRYVRY QARAGKELGG WIFTDEIIVK
//
