ID A0A1J0A4K2_9ENTE Unreviewed; 477 AA.
AC A0A1J0A4K2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:APB30846.1};
GN ORFNames=BHY08_02780 {ECO:0000313|EMBL:APB30846.1};
OS Vagococcus teuberi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=519472 {ECO:0000313|EMBL:APB30846.1, ECO:0000313|Proteomes:UP000191200};
RN [1] {ECO:0000313|EMBL:APB30846.1, ECO:0000313|Proteomes:UP000191200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21459 {ECO:0000313|EMBL:APB30846.1,
RC ECO:0000313|Proteomes:UP000191200};
RA Wullschleger S., Seifert C., Baumgartner S., Lacroix C., Bonfoh B.,
RA Stevens M.J., Meile L.;
RT "Vagococcus teuberi sp. nov., isolated from the Malian artisanal sour milk
RT fene.";
RL Submitted (SEP-2016) 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; CP017267; APB30846.1; -; Genomic_DNA.
DR RefSeq; WP_071456421.1; NZ_CP017267.1.
DR AlphaFoldDB; A0A1J0A4K2; -.
DR STRING; 519472.BHY08_02780; -.
DR KEGG; vte:BHY08_02780; -.
DR OrthoDB; 1637462at2; -.
DR Proteomes; UP000191200; 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|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU004468};
KW Hydrolase {ECO:0000256|RuleBase:RU004468};
KW Reference proteome {ECO:0000313|Proteomes:UP000191200}.
FT ACT_SITE 372
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 477 AA; 54695 MW; BBCD3B469AFB3455 CRC64;
MGFRQDFLWG GATAANQCEG AYREDGRGLA NVDLAPVGKD RAAVITGEMK MFEFDEHHFY
PAKEAIDMYH RYKEDIALFA EMGFKTYRLS IAWSRIFPKG DENEPNEAGL KYYEDLFKEC
KKYGIEPLVT ITHFDCPMHL VEKYGAWRSR ELVGFYENLC HVIFNRYKGL VKYWLTFNEI
NMILHAPFMG AGLYFEEGEN KEQIKYQAAH HELLASAIAT KIAHEVDPEN KVGCMLAAGA
NYAYTSKPED VWASRKADRE NYFFIDVQSR GEYPSYALKE MERKGITLPI QEGDLELLKE
HTVDFVSFSY YSSRLQSTDP AVNEQTSGNI FESLKNPYLE SSEWGWQIDP LGLRITLNDL
YDRYQKPLFI VENGLGAVDT PDENGYVADD YRIEYLAEHI KAMRDAVEID GVDLLGYTTW
GCIDLVSAGT GEMKKRYGFI YVDRDNEGNG TLNRSKKKSF DWYKKVIATN GEDLSNS
//
