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Database: UniProt
Entry: A0A069D1H2_9BACE
LinkDB: A0A069D1H2_9BACE
Original site: A0A069D1H2_9BACE 
ID   A0A069D1H2_9BACE        Unreviewed;       810 AA.
AC   A0A069D1H2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=JCM15093_1449 {ECO:0000313|EMBL:GAK36292.1};
OS   Bacteroides graminisolvens DSM 19988 = JCM 15093.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1121097 {ECO:0000313|EMBL:GAK36292.1, ECO:0000313|Proteomes:UP000027601};
RN   [1] {ECO:0000313|EMBL:GAK36292.1, ECO:0000313|Proteomes:UP000027601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15093 {ECO:0000313|EMBL:GAK36292.1,
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   -!- 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:GAK36292.1}.
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DR   EMBL; BAJS01000006; GAK36292.1; -; Genomic_DNA.
DR   RefSeq; WP_024996242.1; NZ_BAJS01000006.1.
DR   AlphaFoldDB; A0A069D1H2; -.
DR   STRING; 1121097.GCA_000428125_00813; -.
DR   eggNOG; COG3525; Bacteria.
DR   OrthoDB; 1090159at2; -.
DR   Proteomes; UP000027601; 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; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027601}.
FT   DOMAIN          641..775
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   ACT_SITE        341
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   810 AA;  90830 MW;  145699A312B99A4E CRC64;
     MKRGFFILLL IVSFISPGCG QSKEAVNEYQ LIPYPNGLTP QKGSFKLTNG LPVVVQCPEA
     QCVADSFITR LKQCALMNLK VETKGTPGQP AIYFQKQEGL HKEGYKLSVS GKQITVKAST
     ANGFFYAVQT LYQLLPPAIY KRDVTPGLTW SIPAVEIEDE PRFAYRGLML DVCRHFSPVG
     YIYRFIDMLA YHKMNVFHWH LTDDQGWRIE IKKYPKLIEI GSKRPETLIG YYFENYPQLF
     DGKEHQGYYT QKQIKEIVAY AASKHITVIP EIEMPGHALA ALASYPELSC RPDTTYGVST
     KWGIFNEVFC PKEETFAFLE GVLDEVMALF PSPYIHIGGD ECPKTEWKNC AHCQALIKEL
     GLTDDSEPNK VDGKKHSKEE KLQSYFITRM EKYLNAKGRN IIGWDEILEG GLAPNATVMS
     WRGVEGGLTA AKAGHNAIMT PGAYMYLDQY QENPEIAPTT IGGYATLKKV YGYNPVPDDA
     DALVKKHIIG LQGNIWTEYI PTTDRRDYQA FPRALAIAET AWTQNGRKNW NSFRQRVESD
     FARMDIIGVK ACRNFFDVNI QTRGNGKNGL NVTLETDVPN AEIHYTTNGT EPTNQSTRYT
     QPFLLHGNLS LKAATFRNGK RLGSITSKPL YGNLISGHSF TVTPGAGWMT GDIWDENHVL
     GSDKQTFGLT NGKRGYRQSY TPWVSFGMNE SCKEVIFTTD LGKTESISKV VFGTLHNPAY
     KALPAGKAVV EISTDGVNYQ KVAEETFRRQ LPGNGRKAFT DEVIFAASDA RYVRLTIQNG
     GTLRNGIDYR KDNGPATIQA NLYLDEIEVY
//
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