ID   K8E296_CARML            Unreviewed;       481 AA.
AC   K8E296;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 2.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Aryl-phospho-beta-D-glucosidase BglH {ECO:0000313|EMBL:CCO10015.2};
DE            EC=3.2.1.86 {ECO:0000313|EMBL:CCO10015.2};
GN   Name=bglH {ECO:0000313|EMBL:CCO10015.2};
GN   ORFNames=BN424_538 {ECO:0000313|EMBL:CCO10015.2};
OS   Carnobacterium maltaromaticum LMA28.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1234679 {ECO:0000313|EMBL:CCO10015.2, ECO:0000313|Proteomes:UP000000212};
RN   [1] {ECO:0000313|Proteomes:UP000000212}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMA28 {ECO:0000313|Proteomes:UP000000212};
RX   PubMed=23405327; DOI=10.1128/genomeA.00115-12;
RA   Cailliez-Grimal C., Chaillou S., Anba-Mondoloni J., Loux V., Afzal M.I.,
RA   Rahman A., Kergourlay G., Champomier-Verges M.C., Zagorec M., Dalgaard P.,
RA   Leisner J.J., Prevost H., Revol-Junelles A.M., Borges F.;
RT   "Complete Chromosome Sequence of Carnobacterium maltaromaticum LMA 28.";
RL   Genome Announc. 1:0-0(2013).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; HE999757; CCO10015.2; -; Genomic_DNA.
DR   RefSeq; WP_015075504.1; NC_019425.2.
DR   AlphaFoldDB; K8E296; -.
DR   STRING; 1234679.BN424_538; -.
DR   KEGG; cml:BN424_538; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_0_2_9; -.
DR   OrthoDB; 1637462at2; -.
DR   Proteomes; UP000000212; 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|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU004468};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:CCO10015.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000212}.
FT   ACT_SITE        379
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   481 AA;  54682 MW;  909A0C0655AABDCC CRC64;
     MTTTKSIFPK NFLWGGATAA NQLEGGYLED GRGLSVADAL PGGKERFKIV AQPDFDFEID
     ETKYVYPNHN GIDHYHRYQE DIALFAKMGF KVYRLSIAWS RIFPKGDETT PNEAGLAFYD
     KIFDECLKYG IEPVVTISHY EMPLHLAKEY GGWGNRKLID FYERYAQVVL ERYHAKVKYW
     MTFNEINSAL HFPVMSQGLT MKSGAADKQT IYQGLHHQFV ASSKATKIAH ELDPNLQVGC
     MIIYATTYAY DSNPVNHLEA LEYNQRFNFY CADVQAKGEY PHYAKRIWEK NNVTLDIQPG
     DLEILKAHPV DYIGFSYYMS TVVTTDADKL AQSSGNLLSG VSNPFLEASE WGWQIDPLGL
     RLALNELYGR YQKPLFIVEN GLGAYDTPDE NHYVADDYRI DYLRSHISAM GEAIEDGVDL
     MGYTPWGCID LVSASTGEMS KRYGFIYVDL DDNGQGTGNR YEKKSFNWYK KVIDTNGSDL
     A
//