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Database: UniProt
Entry: L0EF27_THECK
LinkDB: L0EF27_THECK
Original site: L0EF27_THECK 
ID   L0EF27_THECK            Unreviewed;       590 AA.
AC   L0EF27;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   OrderedLocusNames=Theco_1623 {ECO:0000313|EMBL:AGA57760.1};
OS   Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Thermobacillus.
OX   NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA57760.1, ECO:0000313|Proteomes:UP000010795};
RN   [1] {ECO:0000313|Proteomes:UP000010795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18247 / JCM 13945 / KWC4
RC   {ECO:0000313|Proteomes:UP000010795};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA   Woyke T.;
RT   "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL   Submitted (JAN-2012) 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 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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DR   EMBL; CP003255; AGA57760.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0EF27; -.
DR   STRING; 717605.Theco_1623; -.
DR   KEGG; tco:Theco_1623; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_008392_5_3_9; -.
DR   Proteomes; UP000010795; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGA57760.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010795}.
FT   DOMAIN          21..342
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
SQ   SEQUENCE   590 AA;  63184 MW;  309202EED1403CF8 CRC64;
     MSKAGAWRGT GEGVNLAGWS LRDKIGQMVM AGFDGKAPTD EIRALIRERK LGGVIYFRRN
     AGSVAEVARL SAALRELAAE ATKVPLWIAV DQEGGMVARL DQGVTVMPGH MALGATRSAK
     WARETAYASG AQLMRLGVNL NFAPCLDVNN NPANPVIGVR SFGERPELAA ELGIAAIRGY
     REAGVVACAK HFPGHGDTVA DSHRELPTVP HDRKRLEEVE LLPFRLAAAA GADAIMTAHV
     RFPALEPDGL PATLSPRILR GLLRDEWGYD GVVFTDCLEM KAIAGTVGVA RGAVMAVKAG
     ADVVLVSHTP ALQKAALDAL YEAVEAGEIA EARIDESVRR IAGLKARQSA AVPVGPVPAA
     RSDAGTGPDD FDFGGEAAAL AREVCRRSVT LVRNERGALP LRRDVPTFVV WPEVRQGTEV
     DEALARELTL GRALAPYLSR VKEFRIGTVP GEDEVRETLA EIDRALEDIR ERAAVRGEPG
     SDRTLLQVVV GTYNAAFAAG QTELVNHLLA CEGVRVTAAA LRNPYDFLAF PEVHAYAACY
     ENTPCMMEAL AEVLAGETEA RGRLPVTLSE RYPFGHGISG FRKERDGEET
//
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