ID I0GT77_SELRL Unreviewed; 468 AA.
AC I0GT77;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Putative 6-phospho-beta-glucosidase {ECO:0000313|EMBL:BAL83964.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:BAL83964.1};
GN Name=bglA {ECO:0000313|EMBL:BAL83964.1};
GN OrderedLocusNames=SELR_22560 {ECO:0000313|EMBL:BAL83964.1};
OS Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / TAM6421).
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=927704 {ECO:0000313|EMBL:BAL83964.1, ECO:0000313|Proteomes:UP000007887};
RN [1] {ECO:0000313|EMBL:BAL83964.1, ECO:0000313|Proteomes:UP000007887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103574 / TAM6421 {ECO:0000313|Proteomes:UP000007887};
RA Oguchi A., Ankai A., Kaneko J., Yamada-Narita S., Fukui S., Takahashi M.,
RA Onodera T., Kojima S., Fushimi T., Abe N., Kamio Y., Yamazaki S.,
RA Fujita N.;
RT "Whole genome sequence of Selenomonas ruminantium subsp. lactilytica
RT TAM6421.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; AP012292; BAL83964.1; -; Genomic_DNA.
DR RefSeq; WP_014425391.1; NC_017068.1.
DR AlphaFoldDB; I0GT77; -.
DR KEGG; sri:SELR_22560; -.
DR PATRIC; fig|927704.6.peg.2336; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_2_9; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000007887; 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:SF122; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLH; 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:BAL83964.1}.
FT ACT_SITE 361
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 468 AA; 53435 MW; 6C243896F2AA5F2F CRC64;
MAFPKEFLWG GAVAANQCEG AYNEDGKGLD IQDIMPRGLK GAPTAEPTED NMKLVAIDFY
HRYKEDVKLF AEMGFKVFRT SIAWSRIFPN GDDAEPNEKG LQFYDDLFDE CHKYGIEPLV
TISHYETPLH LAKEYNGWVN HDLIGFYEKY VRVLFNRYKG KVKYWLTFNE INSVLHAPLM
SGGIMTPLSE LSKSDLYQAC HHELVASALA TKIGHEIDPE AKIGCMVLSM PTYPLTPNPD
DVIATMQANN LNDFFGDMHA RGVYPGYMKR YFRENGIEIK TTPEELALLK EHTVDFISFS
YYVSICESAS RKEEGSGNII QGVKNPYLKE SEWGWQIDPQ GIRYVLNRFY NRWQKPLFIV
ENGLGAKDEL VDDGQGGKTV NDDYRIAYLN DHLVQVEEAI EDGVPVMGYT TWGCIDLVSA
STAELAKRYG FIYVDRHDDG TGTLNRYKKK SFYWYKDIIE SNGEKLKK
//
