ID A0QPD6_MYCS2 Unreviewed; 387 AA.
AC A0QPD6;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN OrderedLocusNames=MSMEG_0361 {ECO:0000313|EMBL:ABK70873.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK70873.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK70873.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:4YYF}
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 26-387, AND DISULFIDE BONDS.
RA Tan K., Hatzos-Skintges C., Clancy S., Joachimiak A.;
RT "The crystal structure of a glycosyl hydrolase of GH3 family member from
RT [Mycobacterium smegmatis str. MC2 155.";
RL Submitted (MAR-2015) to the PDB data bank.
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; CP000480; ABK70873.1; -; Genomic_DNA.
DR RefSeq; WP_011726879.1; NZ_SIJM01000018.1.
DR RefSeq; YP_884774.1; NC_008596.1.
DR PDB; 4YYF; X-ray; 1.92 A; A/B/C=26-387.
DR PDBsum; 4YYF; -.
DR AlphaFoldDB; A0QPD6; -.
DR SMR; A0QPD6; -.
DR STRING; 246196.MSMEG_0361; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR PaxDb; 246196-MSMEI_0354; -.
DR GeneID; 66738548; -.
DR KEGG; msm:MSMEG_0361; -.
DR PATRIC; fig|246196.19.peg.358; -.
DR eggNOG; COG1472; Bacteria.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000000757; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4YYF};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABK70873.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000757};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..387
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010263020"
FT DOMAIN 64..376
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT REGION 24..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 56..386
FT /evidence="ECO:0007829|PDB:4YYF"
SQ SEQUENCE 387 AA; 39155 MW; 8A412D9200347417 CRC64;
MASPRLLATF VALSGLLLAC SPAAPPDAGP STGPSGSPDM QPMATTAPLP EAPATCDLAA
LPARDKLAQL LTVGVTDAAD ARAVVADHHV GGIMIGSWTD LSMLTDGSLG DIAASAAPLP
LAVSVDEEGG RVSRLASLIG SQPSARELAR TKTADEVYGI ALDRGRKMRD LGVTVDFAPV
VDVTDAAADT VIGDRSFGSD PAVVTEYAGA YARGLRDAGV LPVLKHFPGH GHASGDSHTG
GVTTPPLDVL MGDDLVPYRT LTGQAPVAVM VGHMQVPGLT GSDPASLSPA AYNLLRSGGY
GGPGFGGLVY TDDLSSMGAI NQRYGVADAV LRALQAGADN ALWITTAEVP AVLDRLEQAL
ASGELNQGAV DASLQRNAAV KGPLRCG
//
