ID A0A011RP69_9LACT Unreviewed; 477 AA.
AC A0A011RP69;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:EXJ23723.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:EXJ23723.1};
GN ORFNames=ADIAL_0838 {ECO:0000313|EMBL:EXJ23723.1};
OS Alkalibacterium sp. AK22.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ23723.1, ECO:0000313|Proteomes:UP000020164};
RN [1] {ECO:0000313|EMBL:EXJ23723.1, ECO:0000313|Proteomes:UP000020164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164};
RA Singh A., Pinnaka A.K.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ23723.1}.
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DR EMBL; JANL01000019; EXJ23723.1; -; Genomic_DNA.
DR RefSeq; WP_034300392.1; NZ_JANL01000019.1.
DR AlphaFoldDB; A0A011RP69; -.
DR STRING; 1229520.ADIAL_0838; -.
DR PATRIC; fig|1229520.3.peg.835; -.
DR eggNOG; COG2723; Bacteria.
DR OrthoDB; 1637462at2; -.
DR Proteomes; UP000020164; Unassembled WGS sequence.
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:EXJ23723.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020164}.
FT ACT_SITE 372
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 477 AA; 54447 MW; 5DDE6C37ED00DB85 CRC64;
MSFRKDFLWG GATAANQLEG GYDEDGRGLA NVDVAPVGED RHAIISGDKK HLDFDGEHFY
PAKKAIDHYH RYKEDIALFA EMGFKTYRLS IGWTRIFPKG DEKEPNEAGL KFYEDLFKEC
KKHGIEPLVT ITHFDCPMHL IKEYGGWRNR KMVDFYANLT RTLFTRYKGL VKYWLTFNEI
NIILHAPFMG AGIVFEEGEN KKQVLYQAAH HELVSSAMAT KIAREVDPNI QIGCMLAAGK
TYPNSPRPAD VLAAQQADRQ NYFFIDVQSR GEYPAYALKE LEREGVEIPF KEGDKELLKE
YTVDFISFSY YSSRVAAANP ENQDETSGNI FSSVKNPYLE ASEWGWQIDP LGLRITMNDI
YDRYQKPLFI VENGLGAIDT PDASGYVEDD YRIDYLSSHI AAMKEAVELD GVDLMGYTSW
GCIDLVSAGT GEMKKRYGYI YVDRDNYGNG TLERTPKKSF YWYKKVIETN GEDLSNN
//
