ID D8MR09_ERWBE Unreviewed; 476 AA.
AC D8MR09;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Putative 6-phospho-beta-glucosidase {ECO:0000313|EMBL:CAX59266.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:CAX59266.1};
GN Name=ascB {ECO:0000313|EMBL:CAX59266.1};
GN OrderedLocusNames=EbC_17350 {ECO:0000313|EMBL:CAX59266.1};
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:CAX59266.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX59266.1,
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; CAX59266.1; -; Genomic_DNA.
DR RefSeq; WP_013201759.1; NC_014306.1.
DR AlphaFoldDB; D8MR09; -.
DR STRING; 634500.EbC_17350; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; ebi:EbC_17350; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_2_6; -.
DR Proteomes; UP000008793; Chromosome.
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:CAX59266.1};
KW Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:CAX59266.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793}.
FT ACT_SITE 374
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 476 AA; 53459 MW; 7D99FFF30F915F39 CRC64;
MSATQFPDGF LWGGALAANQ AEGASFEGGK GLTTVDVIPH GTHRLAVKVG LEKRVALRED
EFYPSHQAID FYHRYKDDIA LMAEMGFTVF RTSIAWSRIY PNGDELEPNE AGIAFYRDLF
NECKKHNIEP LVTLCHFDVP MHLVTEYGSW RNRKMVAFFA RYARTCFEAF DGLVKYWLTF
NEINILLASP FSGAGLVFEE GEDPSQVKYQ AAHHELVASA LATKIAHEVN AENQVGCMLA
GGNFYPRTCK PEDVWAALEK DRENLFFIDV QARGAYPSYT RRLFAEKGIS VKMEEGDGEL
LKNTVDFVSF SYYASRCASA DMNENNSSAA NVVKSLKNPH VQVSDWGWGI DPLGLRITMN
MMYDRYQKPL FLVENGLGAK DEITPEGEIV DDYRISYLRE HIKAMGEAIA DGIPVIGYTS
WGCIDLVSAS TGEMSKRYGF VYVDRDDQGQ GTLARTRKKS FYWYQKVIAS NGADLS
//
