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Database: UniProt
Entry: G8RQM3_MYCRN
LinkDB: G8RQM3_MYCRN
Original site: G8RQM3_MYCRN 
ID   G8RQM3_MYCRN            Unreviewed;       433 AA.
AC   G8RQM3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   OrderedLocusNames=MycrhN_0798 {ECO:0000313|EMBL:AEV71429.1};
OS   Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV71429.1, ECO:0000313|Proteomes:UP000005442};
RN   [1] {ECO:0000313|EMBL:AEV71429.1, ECO:0000313|Proteomes:UP000005442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB3 {ECO:0000313|EMBL:AEV71429.1,
RC   ECO:0000313|Proteomes:UP000005442};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA   Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL   Submitted (DEC-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; CP003169; AEV71429.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8RQM3; -.
DR   STRING; 710685.MycrhN_0798; -.
DR   KEGG; mrh:MycrhN_0798; -.
DR   PATRIC; fig|710685.3.peg.804; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_008392_0_4_11; -.
DR   Proteomes; UP000005442; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEV71429.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005442};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        42..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          107..422
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   REGION          68..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          273..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   433 AA;  44756 MW;  B9953A9B3C120121 CRC64;
     MDIRISRSCV GVEATAPGNF FAMPSRGGSR KSLSERMQGS RWMTIAFAVL AVVVLAVVVV
     FVVKPRLSGS SSTAPSSQAS APSPPAPTAT IPPGCGDAEA VVNAMSTRDK LAQLLMVGVT
     GAEDARAVAA DHHVGGIMIG SWTDLSMLQD GSLREIAGSA GALPLAVSTD EEGGRVQRLS
     SIIGSQPPPR TLAATSSPDE VYSIALQRGR AMKELGITVD FAPVVDVTDA PDDTVIGDRS
     FGSNPEAVTA FAGAYARGLR DAGVLPVLKH FPGHGHGSGD SHTGGVSTPP LDQLQADDLI
     PYRTLTTDKP VAVMLGHLQV PGLTGTDPAS LSKPAYDLLR SGGYGGPPFT GLVYTDDLSS
     MAAINERYSV PDAVLRSLQA GADIALWITT DEVPAVLDSL EQAVNSGQLS MDRVNESAMR
     VADSKSATPN CGR
//
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