ID A0A0F6B6E4_SALT1 Unreviewed; 477 AA.
AC A0A0F6B6E4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=6-phospho-beta-glucosidase A {ECO:0000313|EMBL:ACY90091.1};
GN Name=bglA {ECO:0000313|EMBL:ACY90091.1};
GN OrderedLocusNames=STM14_3684 {ECO:0000313|EMBL:ACY90091.1};
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858 {ECO:0000313|EMBL:ACY90091.1, ECO:0000313|Proteomes:UP000002695};
RN [1] {ECO:0000313|EMBL:ACY90091.1, ECO:0000313|Proteomes:UP000002695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262 {ECO:0000313|Proteomes:UP000002695};
RX PubMed=19897643; DOI=10.1128/JB.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; CP001363; ACY90091.1; -; Genomic_DNA.
DR RefSeq; WP_001230141.1; NZ_CP043402.1.
DR AlphaFoldDB; A0A0F6B6E4; -.
DR KEGG; seo:STM14_3684; -.
DR PATRIC; fig|588858.6.peg.3392; -.
DR HOGENOM; CLU_001859_0_2_6; -.
DR OMA; HGSNDFY; -.
DR BioCyc; SENT588858:STM14_RS16310-MONOMER; -.
DR Proteomes; UP000002695; 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; 55103 MW; 70C443A8095261DB 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 NIKMEDGDLE
VLREGTCDYL GFSYYMTNAV KAEGGSGDAI SGFEGSVPNP YVKASDWGWQ IDPVGLRYSL
CELYERYQKP LFIVENGFGA YDKVEEDGSI NDDYRIDYLR AHIEEMKKAV TYDGVDLMGY
TPWGCIDCVS FTTGQYSKRY GFIYVNKHDD GTGDMSRSRK KSFNWYKEVI ASNGEKL
//