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
//