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Database: UniProt
Entry: A0A085EGF8_9FLAO
LinkDB: A0A085EGF8_9FLAO
Original site: A0A085EGF8_9FLAO 
ID   A0A085EGF8_9FLAO        Unreviewed;       554 AA.
AC   A0A085EGF8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, 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=FEM08_29200 {ECO:0000313|EMBL:KFC58303.1};
OS   Flavobacterium gilvum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1492737 {ECO:0000313|EMBL:KFC58303.1, ECO:0000313|Proteomes:UP000028636};
RN   [1] {ECO:0000313|EMBL:KFC58303.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EM1308 {ECO:0000313|EMBL:KFC58303.1};
RA   Shin S.-K., Yi H.;
RT   "Genome Sequence of Flavobacterium sp. EM1308.";
RL   Submitted (MAY-2014) 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:KFC58303.1}.
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DR   EMBL; JNCP01000105; KFC58303.1; -; Genomic_DNA.
DR   RefSeq; WP_051877870.1; NZ_JNCP01000105.1.
DR   AlphaFoldDB; A0A085EGF8; -.
DR   STRING; 1492737.EM308_14215; -.
DR   KEGG; fgl:EM308_14215; -.
DR   PATRIC; fig|1492737.3.peg.2904; -.
DR   eggNOG; COG3525; Bacteria.
DR   OrthoDB; 9763537at2; -.
DR   Proteomes; UP000028636; 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   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   PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:KFC58303.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFC58303.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..554
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001788611"
FT   DOMAIN          21..145
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          149..513
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        345
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   554 AA;  63003 MW;  73F573958545AC3E CRC64;
     MVRSFFFALL LCSTLSFAQE VNIIPQPVQL TRNEGSFVIN SQTSLVVSSD KDKQTADYLN
     KYLSDHYGFK LPIVKKANKN FVTLKSGKST DGIKAEAYTL KSNGKGVEIN GNSEIGTFYG
     MQTLIQLLPV EKSTSLKIAS VDIKDEPRFA YRGAMLDVGR HFFPVAFVKK YIDYLALHKM
     NYFHWHLTED QGWRIEIKKY PKLTEIGSKR NGTIIGHAPG TGSDNTPEGG FYTQEEVKDI
     VKYASDRFIT VIPEIEMPGH SSAAIAAYPE LSCFPQEKTQ LSDKIISDKS KEELANGRTK
     LVQETWGVFT DVYAPTEYTF KFLQDVIDEV VTLFPSKYIH VGGDESPKDA WKRSEFCQNM
     IKEKGLKDEH ELQSYFIQRM EKYINSKGKT LIGWDEILEG GLAPNAIVMS WRGEKGGITA
     AKDKHQVIMT PGSHVYLDHS QTKNDKELTI GGFTNLEKIY SYEPVPKELT ADEAKYVMGA
     QGNVWTEYMQ TPAKVEYMIF PRLSALSEVL WSPKENRDWS QFQTKIETQK KRYTLWGANF
     FIEYQTVLTK PMNN
//
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