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Database: UniProt/TrEMBL
Entry: A0A0T9MD81_YERIN
LinkDB: A0A0T9MD81_YERIN
Original site: A0A0T9MD81_YERIN 
ID   A0A0T9MD81_YERIN        Unreviewed;       465 AA.
AC   A0A0T9MD81;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Cryptic 6-phospho-beta-glucosidase {ECO:0000313|EMBL:CNF98421.1};
DE            EC=3.2.1.86 {ECO:0000313|EMBL:CNF98421.1};
GN   Name=ascB_2 {ECO:0000313|EMBL:CNF98421.1};
GN   ORFNames=ERS008530_02638 {ECO:0000313|EMBL:CNF98421.1};
OS   Yersinia intermedia.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=631 {ECO:0000313|EMBL:CNF98421.1, ECO:0000313|Proteomes:UP000038750};
RN   [1] {ECO:0000313|EMBL:CNF98421.1, ECO:0000313|Proteomes:UP000038750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR165/97 {ECO:0000313|EMBL:CNF98421.1,
RC   ECO:0000313|Proteomes:UP000038750};
RA   Murphy D.;
RL   Submitted (MAR-2015) 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; CPZJ01000010; CNF98421.1; -; Genomic_DNA.
DR   RefSeq; WP_042568366.1; NZ_NHOH01000017.1.
DR   AlphaFoldDB; A0A0T9MD81; -.
DR   STRING; 631.CH53_488; -.
DR   KEGG; yin:CH53_488; -.
DR   eggNOG; COG2723; Bacteria.
DR   OrthoDB; 9765195at2; -.
DR   Proteomes; UP000038750; 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:SF122; 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:CNF98421.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:CNF98421.1}.
FT   ACT_SITE        362
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   465 AA;  53087 MW;  307361DFFF789145 CRC64;
     MKHAFPDNFL WGGAIAANQV EGAYLTEGKG LSTSDLQPHG IFGDIIPRVS GDSYVKDVAI
     DFYHRYPEDI ALFAEMGFKC LRISIAWTRI FPQGDEQQPN EAGLAFYDRV FDEMAKYNIT
     PLVTLSHYEM PYGLVKNYGG WGNRKTIGFF EHYARTVFQR YQHKVKLWLT FNEINMSLHA
     PFTGVGLEQE SSKSAVYQAI HHQLVASAKA VAALHEIIPD GRIGNMLLGG LMYPLTCKPA
     DVLETLQQNR EWLFFGDVQV RGYYPSYMAR YFKQHGISVE ITAEDKLALK QTVDFISFSY
     YMSGCVTADE ELNRKARGNI LSMVQNPHLA SSEWGWQIDP EGLRILLNEL WDRYQKPLFI
     VENGLGAKDK PDVNGHIEDD YRIEYLNDHL VQVSEAIEDG VEVMGYTSWG PIDLVSASKA
     ELSKRYGFIY VDRDDNGKGT LARRRKKSFY WYRDVIQSNG EILKR
//
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