ID   A0A1G6RN73_9BACT        Unreviewed;       845 AA.
AC   A0A1G6RN73;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
DE   AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00030512};
DE   AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000256|ARBA:ARBA00033000};
GN   ORFNames=SAMN04488104_101368 {ECO:0000313|EMBL:SDD05843.1};
OS   Algoriphagus faecimaris.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=686796 {ECO:0000313|EMBL:SDD05843.1, ECO:0000313|Proteomes:UP000199060};
RN   [1] {ECO:0000313|Proteomes:UP000199060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23095 {ECO:0000313|Proteomes:UP000199060};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC         residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC         Evidence={ECO:0000256|ARBA:ARBA00001231};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNAC01000013; SDD05843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6RN73; -.
DR   STRING; 686796.SAMN04488104_101368; -.
DR   OrthoDB; 9763537at2; -.
DR   Proteomes; UP000199060; 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:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR004866; CHB/HEX_N_dom.
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; IPR014756; Ig_E-set.
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   PRINTS; PR00738; GLHYDRLASE20.
DR   SMART; SM01081; CHB_HEX; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          25..171
FT                   /note="Chitobiase/beta-hexosaminidases N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01081"
FT   ACT_SITE        520
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   845 AA;  96361 MW;  3E1EEE026AFA173C CRC64;
     MRVIVLFTVI FLLFSCNPSE DLQAGELSVE WKLLENELTP RSSHKAAFIL RNHTMKEIEE
     GWKLYFNTIF VSVSPEVSDD RFQIRHLAGD FFVLEGRGQK TPMIREGEKL EVTYASNNPF
     LKNSHAPEGL IFQERDGTFQ EVSSYEKSAL ELKELIAVFG STEVFIPTAE AIYEMNEEVF
     LLDKEHVPPF LPIPKSWEYL GEPLLIKNAG IGVLGDKAFE KAAKMVTKQI QLGYKPENDR
     SIKPLQIRIA KKEGIPSEGY HLEIRDRRVL ILASDERGAF YGVQSFLALL PPGFWEQPSN
     EILLPQIEID DAPDFGYRGL FLDVARNFIP KESIFKILDL MSFYKLNTFH FNLANDEGWR
     IEIKGLSELT DFGSKRGFSI DESTMLWPFY GSGAATNNGL GSGFYSVADF QEILRYADER
     MIEVIPEIGV PAHSRAAIRA MEKRYQHWIG KGNEEEANRY RLADPQDSST YLSAQNFRDN
     TIAVCRESVY DFYEKVVSEI KSIYDEAGVP LKTWHTGGDE IPSGVWESSP LCDSFLVDQS
     HSSQHSLEKY FRLRVSEILA KYGLNTAGWE EIGLEEEEGE VVPVKKYATK GWSLYAWNAV
     PGWGSEDRAY KLANAGYPVV ISSSANFYFD LAYNWDPREP GHTWSGVADM YQAWKAVPHK
     MYLSHDQTID GKTWPWEEKQ IDFEKLTEQG KKNILGVQGQ LWTETIRSVE MVEYYLFPKM
     LGLVERAWNG DPEWSEAAEV KDMLKKRGQE WNIFSNVVGQ NELPRLATIF GGVNARVPAP
     GLKKIAQEIW ANVENPGLEI RWTDDGTVPS YKSKLYTEPL SYRPGLRFRA FNKKGKGGHV
     SMMEE
//