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Database: UniProt
Entry: C0PY24_SALPC
LinkDB: C0PY24_SALPC
Original site: C0PY24_SALPC 
ID   C0PY24_SALPC            Unreviewed;       477 AA.
AC   C0PY24;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ACN47198.1};
GN   Name=bglA {ECO:0000313|EMBL:ACN47198.1};
GN   OrderedLocusNames=SPC_3111 {ECO:0000313|EMBL:ACN47198.1};
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213 {ECO:0000313|EMBL:ACN47198.1, ECO:0000313|Proteomes:UP000001599};
RN   [1] {ECO:0000313|EMBL:ACN47198.1, ECO:0000313|Proteomes:UP000001599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594 {ECO:0000313|EMBL:ACN47198.1,
RC   ECO:0000313|Proteomes:UP000001599};
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; CP000857; ACN47198.1; -; Genomic_DNA.
DR   RefSeq; WP_001230139.1; NC_012125.1.
DR   AlphaFoldDB; C0PY24; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; sei:SPC_3111; -.
DR   HOGENOM; CLU_001859_0_2_6; -.
DR   OMA; HGSNDFY; -.
DR   Proteomes; UP000001599; 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; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF122; 6-PHOSPHO-BETA-GLUCOSIDASE ASCB-RELATED; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU004468};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468}.
FT   ACT_SITE        375
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   477 AA;  55059 MW;  C521E6585D46351D CRC64;
     MRKLTLPKDF LWGGAVAAHQ VEGGWNKDGK GPSICDVLTG GAHGVPREIT QNVVAGKYYP
     NHEAVDFYGH YKEDIRLFAE MGFKCFRTSI AWTRIFPNGD ESQPNEAGLK FYDDMFDELL
     KYNIEPVITL SHFEMPLHLV QHYGGWTNRK VVDFFVRFAE VVFERYKHKV KYWMTFNEIN
     NQRNWRAPLF GYCCSGVVYT EHENPEETMY QVLHHQFVAS ALAVKAARRI NPQMKVGCML
     AMVALYPFSC KPEDVMFAQE SMRERYVFTD VQLRGYYPSY VLNEWERRGF NIKMDDGDLE
     VLREGTCDYL GFSYYMTNAV KAEGGSGDAI SGFEGSVPNP YVKASDWGWQ IDPVGLRYSL
     CELYERYQKP LFIVENGFGA YDKVEEDGGI NDDYRIDYLR AHIEEMKKAV TYDGVDLMGY
     TPWGCIDCVS FTTGQYSKRY GFIYVNKHDD GTGDMSRSRK KSFNWYKEVI ASNGEKL
//
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