ID Q8A798_BACTN Unreviewed; 776 AA.
AC Q8A798;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN OrderedLocusNames=BT_1627 {ECO:0000313|EMBL:AAO76734.1};
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186 {ECO:0000313|EMBL:AAO76734.1, ECO:0000313|Proteomes:UP000001414};
RN [1] {ECO:0000313|EMBL:AAO76734.1, ECO:0000313|Proteomes:UP000001414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2] {ECO:0000313|EMBL:AAO76734.1, ECO:0000313|Proteomes:UP000001414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; AE015928; AAO76734.1; -; Genomic_DNA.
DR RefSeq; NP_810540.1; NC_004663.1.
DR RefSeq; WP_011107900.1; NC_004663.1.
DR AlphaFoldDB; Q8A798; -.
DR STRING; 226186.BT_1627; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR PaxDb; 226186-BT_1627; -.
DR EnsemblBacteria; AAO76734; AAO76734; BT_1627.
DR KEGG; bth:BT_1627; -.
DR PATRIC; fig|226186.12.peg.1665; -.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_007082_5_0_10; -.
DR InParanoid; Q8A798; -.
DR OrthoDB; 1090159at2; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IBA:GO_Central.
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 GO; GO:0030203; P:glycosaminoglycan metabolic process; IBA:GO_Central.
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; IPR026876; Fn3_assoc_repeat.
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; PF13287; Fn3_assoc; 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 PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001414};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..776
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004303164"
FT DOMAIN 30..159
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 163..517
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT DOMAIN 648..751
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|Pfam:PF00754"
FT ACT_SITE 346
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 776 AA; 87530 MW; EF5EEB31FC29EA07 CRC64;
MTRAILILLI GFLSSIVAGC SDTNLTHDIP LVPRPAQIVP GSGNYLFSGK TVFAVENEEQ
AEVARSFIAL FTRAAGFTPK LTVGDAEKGN VRFQTDATLK SEAYTLQVSP KEIIIEASDA
KGFFYALQTI RQLLPASIEK EEVSDKKVKW SIPAVSIQDE PRFGYRALLL DASRFFIPKE
NVLRIIDCMA MLKINTLHFH LTDDNGWRVE IKKYPRLTEV GAWRVDRTDL PFPARRNPEP
GEPTPVGGFY TQEEIKEMVA YAAERQIEVV PEIDMPAHSN SALAAYPHLA CPVVKEYIGV
LPGLGGRNSE IIYCAGNDSV YAFLQDVMDE ILELFPSRYI HIGGDEARKT YWEKCPLCQA
RMKKEKIANE EDLQGYFMNR MSEYVRSKGR EVIGWDELTN SSFLPDDAII LGWQGYGQAA
LKAAEKGHRF IMTPARIMYL IRYQGPQWFE PLTYFGNNTL KDVYDYEPVQ KDWKPEYADL
LMGVQACMWT EFCNKPEDVD YLVFPRLAAL AEVAWTQPEK KDWTSFLEGM DSFNEHLAAK
GIVYARSMYN IQHTVRPEDG ALKVKLECVR PDVEIRYTMD GSEPTAASPL YEQPLLVKEA
QTVNAATFAD GQQMGKTLTL PVHWNKATAK PLLGNKVNEA VLNNGVRGSL KQTDFEWCSW
GSSDRISFTV DLLQKEKMNT LTIGCITNYG MGVHKPKSIR VAVSDDNATY RDINELEYTP
EEIFREGTFI EDLSIDMRGT VARYVRVTTE GAGECPANHV RPGQESRVCF DELIIE
//