ID L0IP57_9MYCO Unreviewed; 390 AA.
AC L0IP57;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
DE Flags: Precursor;
GN ORFNames=Mycsm_00187 {ECO:0000313|EMBL:AGB20648.1};
OS Mycobacterium sp. JS623.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB20648.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) 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; CP003078; AGB20648.1; -; Genomic_DNA.
DR RefSeq; WP_015304240.1; NC_019966.1.
DR AlphaFoldDB; L0IP57; -.
DR STRING; 212767.Mycsm_00187; -.
DR KEGG; msa:Mycsm_00187; -.
DR PATRIC; fig|710686.3.peg.185; -.
DR HOGENOM; CLU_008392_0_4_11; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000010844; 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; 3.20.20.300; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGB20648.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..390
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038871056"
FT DOMAIN 66..381
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
SQ SEQUENCE 390 AA; 39616 MW; 7F62391A3BE58056 CRC64;
MALPRRLCVL AALTTLMAAC SSPAPQPAPS ATTPAPTIAA TVAPAPAADP AAPACGDGPA
LLASMTTRDK LAQLLMVGVT GAADARAVVE NHHVGGIFIG SWTDLSMLSD GTIANIAETG
PLPLAVSVDE EGGRVARLSS LIGSQPSPRV LAASHTPEEV YNIALARGQA MRKLGITIDF
APVVDVTNAP DDTVIGDRSF GADPAAVTDY AGAYARGLRD AGLLPVLKHF PGHGHGSGDT
HTGSVVTPPL ADLQAGDLIP YRTLTTQGPV GVMVGHIEVP GLTGSDPASL SPAAYALLRS
GDYGGPGFTG PVFTDDLSSM QAISDRMGVA EAALRGLQAG ADIALWVTTD EVPAVLDRLE
KALAAGELTM PRVDASVLRM AAVKGRNPRC
//
