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Database: UniProt
Entry: A0A108T226_9BACE
LinkDB: A0A108T226_9BACE
Original site: A0A108T226_9BACE 
ID   A0A108T226_9BACE        Unreviewed;       814 AA.
AC   A0A108T226;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=F2Y81_08880 {ECO:0000313|EMBL:KAA5420174.1};
OS   Bacteroides cellulosilyticus.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=246787 {ECO:0000313|EMBL:KAA5420174.1, ECO:0000313|Proteomes:UP000448877};
RN   [1] {ECO:0000313|EMBL:KAA5420174.1, ECO:0000313|Proteomes:UP000448877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIOML-A6 {ECO:0000313|EMBL:KAA5420174.1,
RC   ECO:0000313|Proteomes:UP000448877};
RX   PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA   Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA   Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA   Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA   Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA   Xavier R.J., Alm E.J.;
RT   "A library of human gut bacterial isolates paired with longitudinal
RT   multiomics data enables mechanistic microbiome research.";
RL   Nat. Med. 25:1442-1452(2019).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285}.
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:KAA5420174.1}.
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DR   EMBL; VVYV01000011; KAA5420174.1; -; Genomic_DNA.
DR   RefSeq; WP_007215528.1; NZ_VVYV01000011.1.
DR   AlphaFoldDB; A0A108T226; -.
DR   STRING; 246787.BcellWH2_04347; -.
DR   eggNOG; COG3525; Bacteria.
DR   Proteomes; UP000448877; 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; IPR026876; Fn3_assoc_repeat.
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; 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   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KAA5420174.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..814
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030020042"
FT   DOMAIN          644..779
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   ACT_SITE        345
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   814 AA;  91667 MW;  D5E4CC291AB4F19D CRC64;
     MKKGLSALLL ASLLCASSGC QQNQKEVVNE YNIVPMPNQM TPQEGRFLLS NKVSVVTAGC
     TPEVQAIADS LIAQIQLTSG ISLKTSSQEN PEQPDIRFVT EEGMPKEGYK LSIAPNEITL
     SASHPNGFFY GVQTMYQLLP PAIYGKATVK RANWSLPAVE VEDAPRFPYR GLMLDVCRHF
     STTDYIYKFI DMLAMHKMNT FHFHLTDDQG WRIEIKKYPK LQEVGSKRKE TLIDYYFVNW
     PQIFDGKEHG GYYTQEEIKD IVAYAASKYI TVIPEIEMPG HAIAALASYP ELSCRPDTTY
     EVTGTWGVFE EVFCPKEETF QFLEGVLDEV MELFPSSYIH IGGDECPKDA WMKCAHCQGL
     IKKLGLKDDT TPNAIDGKKH TKEEKLQSYF ITRMEKYLNS KGRNIIGWDE ILEGGLAPNA
     TVMSWRGVEG GITAAKAGHD AIMTPSPYAY LDQYQEEPET APTTIGGYQT LKKTYSYNPV
     PDDADELVKK HIIGVQGNIW NEYMQSDERR DYQAFPRAVA LAETGWTQNN RKNWNSFRSR
     MVEDFERMDA MNVKACRNFF DVNINTHVYD GTLKAVLETF YPDAKIRYTT DGSAPTAKSE
     LYTQPFTWEG YIDLQAAAFK NGKMLGKVNG KKLYANLISG KQYTTTPHWG WMSGDIFGEN
     DILGADTTTL GLTNGKRGNI ASFTPWVAFS LNEKNNNELV FSVDLEKPAT ISKVIFGTLY
     NPAFRVLPAS AARVEVSTNG KEFKEVAQTS YTREYPEHGR KMFTDVLEFT PTEARYIKVT
     LKSGGTLRNG IDCRKDSPGD IIPSDLYVDE IEVY
//
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