ID   B1MDE8_MYCA9            Unreviewed;       461 AA.
AC   B1MDE8;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Glycosyl hydrolase (Beta-glucosidase) {ECO:0000313|EMBL:CAM63269.1};
GN   OrderedLocusNames=MAB_3192c {ECO:0000313|EMBL:CAM63269.1};
OS   Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP
OS   104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948) (Mycobacterium
OS   abscessus).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacteroides; Mycobacteroides abscessus.
OX   NCBI_TaxID=561007 {ECO:0000313|EMBL:CAM63269.1, ECO:0000313|Proteomes:UP000007137};
RN   [1] {ECO:0000313|EMBL:CAM63269.1, ECO:0000313|Proteomes:UP000007137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 /
RC   TMC 1543 {ECO:0000313|Proteomes:UP000007137};
RX   PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA   Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA   Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA   Gaillard J.L.;
RT   "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT   Mycobacterium abscessus.";
RL   PLoS ONE 4:E5660-E5660(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000448};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; CU458896; CAM63269.1; -; Genomic_DNA.
DR   RefSeq; WP_005115973.1; NZ_MLCG01000003.1.
DR   AlphaFoldDB; B1MDE8; -.
DR   GeneID; 66968617; -.
DR   KEGG; mab:MAB_3192c; -.
DR   Proteomes; UP000007137; 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; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 2.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:CAM63269.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..461
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002768481"
SQ   SEQUENCE   461 AA;  50936 MW;  23723DAE22531A76 CRC64;
     MKWMNAVMAS AAVVALGLTA CSPRQEAPKE DAGWDRGFYW GTATAGYQVE GSAPDSNWRR
     YVERSAGKPV HPDESNLLAD GPVDPYKQAD DFRHRYAEDI ANAHAMGVNT FRFGLEWSRV
     MPEPGKWDEK ELAYYDSVVA TLRENGMTPM ITLMHWVYPG WVADSGGFMN NLPAFEEFAK
     AITKRYAGQG VLWVSINEPL AFGAMEVRTG AIKPDQFNGF LDRVADAHRA VYRAAHEADP
     EAKVTTNEAY IPPDVLAQFA GFGVKGIEGS FFDRVAGSLD YLGFDYYTGT AADNPASAQS
     MAARWNIKLQ PEDIYYVSRH YAQRYPGLPI YIVENGMVTD NGKPRADGVT RSQYLSDTVF
     WLQRAKADGI PIVGYNYWSL VDNYEWGSYR PRFGLYTVDA LGDPALKRVP TDAVATYTQI
     TRDAGTVPGY RPVIPAAKCS TTVGQDSCAP LDPNGPTVAL R
//