ID A0A0H2Z271_ECOK1 Unreviewed; 479 AA.
AC A0A0H2Z271;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=6-phospho-beta-glucosidase BglA {ECO:0000313|EMBL:ABJ02331.1};
GN Name=bglA {ECO:0000313|EMBL:ABJ02331.1};
GN ORFNames=APECO1_3626 {ECO:0000313|EMBL:ABJ02331.1};
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955 {ECO:0000313|EMBL:ABJ02331.1, ECO:0000313|Proteomes:UP000008216};
RN [1] {ECO:0000313|EMBL:ABJ02331.1, ECO:0000313|Proteomes:UP000008216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APEC O1 {ECO:0000313|EMBL:ABJ02331.1};
RX PubMed=17293413; DOI=10.1128/JB.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT shares strong similarities with human extraintestinal pathogenic E. coli
RT genomes.";
RL J. Bacteriol. 189:3228-3236(2007).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; CP000468; ABJ02331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H2Z271; -.
DR KEGG; ecv:APECO1_3626; -.
DR HOGENOM; CLU_001859_0_2_6; -.
DR Proteomes; UP000008216; 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:UP000008216}.
FT ACT_SITE 377
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 479 AA; 55238 MW; D7131431AD85CF06 CRC64;
MIVKKLTLPK DFLWGGAVAA HQVEGGWNKG GKGPSICDVL TGGAHGVPRE ITKEVVPGKY
YPNHEAVDFY GHYKEDIKLF AEMGFKCFRT SIAWTRIFPK GDEAQPNEEG LKFYDDMIDE
LLKYNIEPVI TLSHFEMPLH LVQQYGSWTN RKVVDFFVRF AEVVFERYKH KVKYWMTFNE
INNQRNWRAP LFGYCCSGVV YTEHENPEET MYQVLHHQFV ASALAVKAAH RINPEMKVGC
MLAMVPLYPY SCNPDDVMFA QESMRERYVF TDVQLRGYYP SYVLNEWERR GFNIKMEDGD
LDVLREGTCD YLGFSYYMTN AVKAEGGTGD AISGFEGSVP NPYVKASDWG WQIDPVGLRY
ALCELYERYQ KPLFIVENGF GAYDKVEDDG SINDDYRIDY LRAHIEEMKK AVTYDGVDLM
GYTPWGCIDC VSFTTGQYSK RYGFIYVNKH DDGTGDMSRS RKKSFNWYKE VIASNGENL
//
