ID   A0A1C2GMF4_9SPHI        Unreviewed;       766 AA.
AC   A0A1C2GMF4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=BEL04_14365 {ECO:0000313|EMBL:OCX52628.1};
OS   Mucilaginibacter sp. PPCGB 2223.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1886027 {ECO:0000313|EMBL:OCX52628.1, ECO:0000313|Proteomes:UP000095113};
RN   [1] {ECO:0000313|EMBL:OCX52628.1, ECO:0000313|Proteomes:UP000095113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PPCGB 2223 {ECO:0000313|EMBL:OCX52628.1,
RC   ECO:0000313|Proteomes:UP000095113};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:OCX52628.1}.
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DR   EMBL; MDJS01000002; OCX52628.1; -; Genomic_DNA.
DR   RefSeq; WP_066005052.1; NZ_MDJS01000002.1.
DR   AlphaFoldDB; A0A1C2GMF4; -.
DR   STRING; 1886027.BEL04_14365; -.
DR   OrthoDB; 1006965at2; -.
DR   Proteomes; UP000095113; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095113};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..766
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008662125"
FT   DOMAIN          625..763
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
FT   ACT_SITE        332
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   766 AA;  84768 MW;  0AF3B714826E1DDA CRC64;
     MLKHFLLALT FFGFSAAYAQ DAAPNLNIIP APVSLKKSDG VFILNQETLI QADTPANRAV
     GVFTSALLST RGLRKQVTLT DNSVTTHVIK FTSAGADALP AEGYHISITP QQITVTGKGA
     GLFYAVQTLI QLLPATNAAV AKVPCVDIDD YPRFGYRGLH LDVSRHFFGV DFVKKYIDLM
     AQYKLNTFHW HLTDDQGWRI EIKKYPKLTE VGSQREQTMI GNYHDFNPQQ FDNTPYGGYY
     TQDQVRDVVK YAAERYITVL PEIEMPGHSV AAIAAYPELG CYGNKQVKVQ GTWGGFDDIY
     CPTDYTFNFM QDVLTEVMGL FPSKYIHIGG DEVSKTAWKQ SVFCQDLIKK LKLKDEEGLQ
     SYFIQRIEKF VNSKGRSIIG WDEILQGGLA PNATVMSWRG ESGGIAAAQQ HHNVIMTPGS
     GGVYFDHAQG KTSQEPVGIG GYAPLQKTYS YNPVPVSLTT DQQKYIMGVQ ANVWTEYIAT
     DNKVEYMLLP RLLALSEIAW TPLANKNYKD FSETRVPVHL AKIDAAGLNY RVSTAIGAPD
     TIITGNKYTF TLKSPVAGAK IYYTIDGYTP RETDLEYTGP VTVQVPDNMS RVFQTIVITP
     SGKRSAVTRA VINNKPALAP VTYSGTADGL KYRLFNGTFE NTDKIDGGAE IDTGIVKNFN
     TNVFRKNGIH DFGVIYNGFI RIDNDGRYSF STSSGDGSVL LIDDQLVVDN DGKHSAFEQG
     GDVLLQKGYH KFTLKYFFAS AGNSLHVYMT IPGKPKGELP PDMMFN
//