ID A0A411WJF1_9GAMM Unreviewed; 478 AA.
AC A0A411WJF1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:QBH96312.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:QBH96312.1};
GN ORFNames=EKN56_07830 {ECO:0000313|EMBL:QBH96312.1};
OS Limnobaculum zhutongyuii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Limnobaculum.
OX NCBI_TaxID=2498113 {ECO:0000313|EMBL:QBH96312.1, ECO:0000313|Proteomes:UP000293154};
RN [1] {ECO:0000313|EMBL:QBH96312.1, ECO:0000313|Proteomes:UP000293154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF-458 {ECO:0000313|EMBL:QBH96312.1,
RC ECO:0000313|Proteomes:UP000293154};
RA Ge Y.;
RT "Pragia sp. nov. isolated from the gut tract of Carduelis flavirostris.";
RL Submitted (MAR-2019) 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; CP034752; QBH96312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411WJF1; -.
DR KEGG; prag:EKN56_07830; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000293154; 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|RuleBase:RU004468, ECO:0000313|EMBL:QBH96312.1};
KW Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:QBH96312.1}.
FT ACT_SITE 376
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 478 AA; 54964 MW; 615BEB3F9EFE86D8 CRC64;
MAQNGFPEGF LWGGAVAAHQ VEGGWNKGGK GVSIADVLSK GSHGVDRVMT DGVLPEYVYP
NHLGVDFYSR YKDDIALFAE MGFKCFRTSI AWTRIFPNGD EQTPNEAGLQ FYDHLFDELL
KHQIEPVITL SHFEMPYHLV KEYGGWHNRK VVDFFVRFSE VVMERYKSKV KYWITFNEIN
NQRNWKYPLF GYCNSGVIFT DYDNPEQSMY QVLHHQFIAS AQVVYRGHQI NPDFKIGSMI
HMMPLYPATC RPEDLVFAQE AMRQKYLFSD VQMRGTYPAY ILKEWARNNI TITTQPGDDE
ILRNGCADYL AISYYMSNIV SPEYTKSENA LTFFEGSKLN PYLQASEWGW QIDPVGLRYS
LSELYERYQK PLFIVENGFG AIDVQETDGS VNDDYRIEYL KAHIVEMEKA VAIDGVDLLG
YTPWGCIDCV SFTTGEYAKR YGFIYVDIND DGSGTLARSK KKSFDWYKNV IASNGAQR
//
