ID   Q0RSF2_FRAAA            Unreviewed;       537 AA.
AC   Q0RSF2;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   OrderedLocusNames=FRAAL0843 {ECO:0000313|EMBL:CAJ59511.1};
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ59511.1, ECO:0000313|Proteomes:UP000000657};
RN   [1] {ECO:0000313|EMBL:CAJ59511.1, ECO:0000313|Proteomes:UP000000657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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DR   EMBL; CT573213; CAJ59511.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0RSF2; -.
DR   STRING; 326424.FRAAL0843; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   KEGG; fal:FRAAL0843; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_008392_0_1_11; -.
DR   Proteomes; UP000000657; Chromosome.
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   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR30480:SF15; BETA-HEXOSAMINIDASE LPQI; 1.
DR   PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:CAJ59511.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAJ59511.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000657}.
FT   DOMAIN          183..473
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   REGION          87..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..537
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  53734 MW;  E6BE61BEDD0C02F3 CRC64;
     MAVAREGEVA SEVEVASEVE VASEVEVAVF GLSRRASAPG IRHRRWYLPI PDWLYGLGEV
     VPFRLLLPAL LATVLGLVVV VARAHGSPGD GDATRATATR PTLAPDPSGS GLPAGLPTGL
     DADLDALGAL SGESGGSSAS DGTGGRPGPT APAATVADRF AASGARPGPT ASCAPARAAA
     MSIEQQAGQV MMIGVPVTNV RSAIALIRQS RLGGVFLAGR STQSAAGLRD DLRAVQDAAR
     RDVGVGAHIA VDQEGGQVQT LQGPGFGTIP SAVEQGRWDA ATLRSRTAAW AGVLAGAGVT
     LDLAPVADTV AAGTARSNPP IGAYGRNFGT AASAVAGDIG VVVPAMQDSG LLATAKHFPG
     LGRVHQNTDT SAAAVDDAAT TTDPNLEPFR VAVSTGTAAV MVSLARYPKL DPATPAAFSA
     PVVTGLLHDQ LGFRGVIVSD DLGSAVAVQS VPVGERAVRF VAAGGDLVLS VRGADAAPMT
     AALAAEAHRS PVFARRLADA ATAVLASKQR QGLLDCPAAA PTPAPAPAPT PTPVPTR
//