ID A0A1I0Q8V7_9BACT Unreviewed; 778 AA.
AC A0A1I0Q8V7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=SAMN05428988_3421 {ECO:0000313|EMBL:SEW23436.1};
OS Chitinophaga sp. YR573.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1881040 {ECO:0000313|EMBL:SEW23436.1, ECO:0000313|Proteomes:UP000198758};
RN [1] {ECO:0000313|EMBL:SEW23436.1, ECO:0000313|Proteomes:UP000198758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR573 {ECO:0000313|EMBL:SEW23436.1,
RC ECO:0000313|Proteomes:UP000198758};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOJF01000001; SEW23436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0Q8V7; -.
DR STRING; 1881040.SAMN05428988_3421; -.
DR OrthoDB; 726159at2; -.
DR Proteomes; UP000198758; 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; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.90.182.10; Toxin - Anthrax Protective Antigen;domain 1; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR Pfam; PF13290; CHB_HEX_C_1; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR PROSITE; PS51820; PA14; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 639..778
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT ACT_SITE 349
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 778 AA; 86744 MW; 3059158A32F47087 CRC64;
MKPGATKLQT PYQVNITSMR KLLLSTIAML SCLYGIAQLK TGDITIIPEP KLQKAVPGSF
VLNDHAIIHY EGKAGKTTAE LLQAFLKSNY NLILEISNAP LPKQPLHPVI NFIESTTGNP
EAYVMEVNAG TIFLKGDAAG LFYGLQTLHQ LLPVEKNTTI HVPGVHIEDE PRFAYRGLML
DVGRHFFPAS YIKQFIDVMA QYKFNRFHWH LTEDQGWRIE IKKYPRLQEI ASVRKETIVG
HHRYSSGYDG KPYGGYYTQN EIRDIVKYAA ARNITIIPEI EMPGHSQAVL AAYPSFGVTG
GPYAVRGTWG ISTDVLNPAN DSVFTFLEDV LTEVMDLFPS KYIHIGGDEC PKDQWKASPQ
VQALIQKLGL KDEHALQSYF IQRIEKFVNS KGRSIIGWDE ILEGGLAPNA TVMSWRGEEG
GIAAAKEKHD VIMSPNTYLY LDYYQGHPAT EPLNAGGYLP LSTVYNYEPL PASLTAEEQQ
YIKGVQANIW TEFIPDQAMV DYMTWPRAMA LSETAWSPAA KKNINRFLKK MPAELQRMEI
ENVNFRIPEP VGLESKITTG LSTVKLTAPV KGAAIYYTID GSQPGLKSKR YSQPIALQVP
ANSTVQLQCI VVTPSGRKSP LYSATYVNKD YLPAANVNPT IKGVRFSVSN KISLTQTKQI
PAKADSTGIV PNIEIRSFIN QGKVNFGVTF EGYVKIDTDG LYEFHVNADD GAVLYIDDSL
LIDNDGTHAL TDKAAFIPLR KGFHKIKTVY FNTGDLKWLD VFLFKDGEKV NLNPILFN
//
