ID   ARBB_DICCH              Reviewed;         465 AA.
AC   P26206;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=6-phospho-beta-glucosidase;
DE            EC=3.2.1.86;
GN   Name=arbB;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1732212; DOI=10.1128/jb.174.3.765-777.1992;
RA   el Hassouni M., Henrissat B., Chippaux M., Barras F.;
RT   "Nucleotide sequences of the arb genes, which control beta-glucoside
RT   utilization in Erwinia chrysanthemi: comparison with the Escherichia coli
RT   bgl operon and evidence for a new beta-glycohydrolase family including
RT   enzymes from eubacteria, archeabacteria, and humans.";
RL   J. Bacteriol. 174:765-777(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose +
CC         D-glucose 6-phosphate; Xref=Rhea:RHEA:10772, ChEBI:CHEBI:4167,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:58312, ChEBI:CHEBI:61548; EC=3.2.1.86;
CC   -!- PATHWAY: Carbohydrate metabolism; beta-glucoside metabolism.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; M81772; AAA24815.1; -; Genomic_DNA.
DR   PIR; C42603; C42603.
DR   AlphaFoldDB; P26206; -.
DR   SMR; P26206; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   UniPathway; UPA00237; -.
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   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; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..465
FT                   /note="6-phospho-beta-glucosidase"
FT                   /id="PRO_0000063899"
FT   ACT_SITE        173
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        362
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   465 AA;  52983 MW;  B3D4E1C4AF0AC36B CRC64;
     MSNPFPAHFL WGGAIAANQV EGAYLTDGKG LSTSDLQPQG IFGEIVTRQP GDSGIKDVAI
     DFYHRYPQDI ALFAEMGFTC LRISIAWTRI FPQGDEAEPN EAGLAFYDRL FDELAKYGIQ
     PLVTLSHYEM PYGLVEKHGG WGNRLTIDCF ERYARTVFAR YRHKVKRWLT FNEINMSLHA
     PFTGVGLPPD SDKAAIYQAI HHQLVASARA VKACHDMIPD AQIGNMLLGA MLYPLTSKPE
     DVMESLHQNR EWLFFGDVQV RGAYPGYMHR YFREQGITLN ITAQDKQDLK ATVDFISFSY
     YMTGCVTTDE AQLEKTRGNI LNMVPNPYLE SSEWGWQIDP LGLRYLLNFL YDRYQKPLFI
     VENGLGAKDK IEENGDIYDD YRIRYLNDHL VQVGEAIDDG VEVLGYTCWG PIDLVSASKA
     EMSKRYGFIY VDRDDAGHGS LERRRKKSFY WYQSVIASHG KTLTR