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Database: UniProt/TrEMBL
Entry: A8FEX0_BACP2
LinkDB: A8FEX0_BACP2
Original site: A8FEX0_BACP2 
ID   A8FEX0_BACP2            Unreviewed;       468 AA.
AC   A8FEX0;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ABV62787.1};
GN   OrderedLocusNames=BPUM_2118 {ECO:0000313|EMBL:ABV62787.1};
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV62787.1, ECO:0000313|Proteomes:UP000001355};
RN   [1] {ECO:0000313|EMBL:ABV62787.1, ECO:0000313|Proteomes:UP000001355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV62787.1,
RC   ECO:0000313|Proteomes:UP000001355};
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(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; CP000813; ABV62787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8FEX0; -.
DR   STRING; 315750.BPUM_2118; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; bpu:BPUM_2118; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_0_1_9; -.
DR   Proteomes; UP000001355; 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; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295}.
FT   ACT_SITE        371
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   468 AA;  54431 MW;  6990558000C37759 CRC64;
     MSMENNKQSY TFPEGFWWGS SASATQTEGS VPGDGKGPNI WDHWFEQEPT RFFDGVGPNV
     TSQFYRKYKE DIRLMKEIGH NSFRLSISWS RLLPEGTGAV NEEAVSFYND VINELIAHDI
     EPFVNLYHFD MPMALQEKGG WVNRQVVDDY VSYAELCFQL FGDRVKKWFT HNEPIVPVEG
     GYMYSFHYPN EVDFQKAVQV GYHELLSNAK AIAAYKKLKQ DGKIGIILNL TPSYPRSQNP
     RDVEAAEMAD AFFNRSFLDP AVKGHFPEKL VEVLKKEGFM PSMQEGDLEL IQENTVDLLG
     INYYQPRRVK AKEHMPHPNA PFMPNHYFDA FDMPGRKMNV YRGWEIYEKG IYDILKKVQT
     DYDNIECFIS ENGMGVEGEE RFKDEEGMIH DDYRIDFIAE HLKWVHQAIK EGSNVKGYHL
     WTFMDNWSWS NAYKNRYGFV SVDLQEDGKR TIKKSGYWFQ SVSENNGF
//
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