ID A0A087ACW9_9BIFI Unreviewed; 477 AA.
AC A0A087ACW9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=6-phospho-beta-glucosidase BglA {ECO:0000313|EMBL:KFI56619.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:KFI56619.1};
GN ORFNames=BCAL_0218 {ECO:0000313|EMBL:KFI56619.1};
OS Bifidobacterium callitrichos DSM 23973.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437609 {ECO:0000313|EMBL:KFI56619.1, ECO:0000313|Proteomes:UP000029072};
RN [1] {ECO:0000313|EMBL:KFI56619.1, ECO:0000313|Proteomes:UP000029072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23973 {ECO:0000313|EMBL:KFI56619.1,
RC ECO:0000313|Proteomes:UP000029072};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFI56619.1}.
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DR EMBL; JGYS01000001; KFI56619.1; -; Genomic_DNA.
DR RefSeq; WP_043163661.1; NZ_JGYS01000001.1.
DR AlphaFoldDB; A0A087ACW9; -.
DR STRING; 1437609.BCAL_0218; -.
DR eggNOG; COG2723; Bacteria.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000029072; Unassembled WGS sequence.
DR GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
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:SF348; 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, ECO:0000313|EMBL:KFI56619.1};
KW Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:KFI56619.1}.
FT ACT_SITE 375
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 477 AA; 54647 MW; A5F590A41E838187 CRC64;
MGFPDNFLWG GAVAAHQLEG AWNEDGRGPS ICDVLTGGAA GVARRITDGV IDGLNYPNHR
GIDYYHTFRE DDALFQEMGF KCFRTSISWS RIFPNGDDEE PNEAGLKFYE ELFSDYRAKG
MEPVVTLSHF EMPLHLAKMG GFTNRKVVDC FVRFATTVME RYKDLVTYWL TFNEVDNQMN
MHTPIFPYTN SGIIPNPDDD PHTVERKVWQ AIHNEFVAAA LAVKKGREIN PDFRIGCMLS
FVPIYPETCR PDDVMLAQTE MRNRYLFGDV YVHGEYPRYL RKRWEREGID IAMEPGDLEI
IREGTVDFVS LSYYMSVAVS SQGSRLDVME HGLDGLVPNP YIKATDWGWQ IDPVGLRYSL
CEMYERWNKP LFIVENGVGM YETPDSDGYI ADDSRIEYLR SHIAEVKKAI DLDGVPVMGY
TVWGCIDVVS FTTGEMKKRY GLIYVDADDE GHGTFERRRK KSFGWYKKVI ESNGEEL
//
