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Database: UniProt/TrEMBL
Entry: A0A0F6B6E4_SALT1
LinkDB: A0A0F6B6E4_SALT1
Original site: A0A0F6B6E4_SALT1 
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
//
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