ID D8MWG2_ERWBE Unreviewed; 479 AA.
AC D8MWG2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=6-phospho-beta-glucosidase A (6-phospho-beta-glucosidase) {ECO:0000313|EMBL:CAX61169.1};
GN Name=bglA {ECO:0000313|EMBL:CAX61169.1};
GN OrderedLocusNames=EbC_36380 {ECO:0000313|EMBL:CAX61169.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX61169.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX61169.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(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; FP236843; CAX61169.1; -; Genomic_DNA.
DR RefSeq; WP_013203653.1; NC_014306.1.
DR AlphaFoldDB; D8MWG2; -.
DR STRING; 634500.EbC_36380; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; ebi:EbC_36380; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_2_6; -.
DR Proteomes; UP000008793; 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: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};
KW Hydrolase {ECO:0000256|RuleBase:RU004468};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793}.
FT ACT_SITE 377
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 479 AA; 54605 MW; 7DC6ECDB71964AF9 CRC64;
MSKHQQLPAD FLWGGAVAAH QVEGGWDQGG KGVSIADVLS GGAHGVDRVM TDGVLDGYSY
PNHQAVEFYS HYKDDIALFA EMGFKCFRTS IAWTRIFPNG DEQQPNEAGL QFYDDLFDEL
LKHNIEPVIT LSHFEMPYHL VKEYGGWLNR KVVDFFVRFS EVVLERYKNK VKYWMTFNEI
NNQRNWKYPL FGYCCSGVVF TDHPQPEQAM YQVLHHQFVA SAKVVSLGHN INPDLQIGCM
IAMVPLYPFS CHPDDVMLAQ EAMRERYLFG DVHMRGYYPS YILNEWARKG YHIEMENEDE
QVLREGCADY IGLSYYMSNA VQANAEGTGS AVSGFEGSVP NPHVKASDWG WQIDPVGLRY
SLAALYERYQ KPLFIVENGF GAIDKPEADG QINDDYRIAY LKAHIEQMKL AVFYDGVELM
GYTPWGCIDC VSFTTGQYSK RYGFIHVDKN DDGSGTLKRS KKKSFGWYQQ VIASQGEKL
//
