(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BI24_GEOS0

ID   A0A0F6BI24_GEOS0        Unreviewed;       478 AA.
AC   A0A0F6BI24;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 21.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ADP73075.1};
DE            EC=3.2.1.86 {ECO:0000313|EMBL:ADP73075.1};
GN   OrderedLocusNames=GY4MC1_0226 {ECO:0000313|EMBL:ADP73075.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73075.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73075.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73075.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; CP002293; ADP73075.1; -; Genomic_DNA.
DR   RefSeq; WP_013399879.1; NC_014650.1.
DR   EnsemblBacteria; ADP73075; ADP73075; GY4MC1_0226.
DR   GeneID; 29237125; -.
DR   KEGG; gmc:GY4MC1_0226; -.
DR   KO; K01223; -.
DR   OMA; YEANHIA; -.
DR   OrthoDB; 654705at2; -.
DR   BioCyc; GSP581103:G1GOQ-269-MONOMER; -.
DR   Proteomes; UP000002034; 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   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; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BI24.
DR   SWISS-2DPAGE; A0A0F6BI24.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Glycosidase {ECO:0000256|RuleBase:RU004468,
KW   ECO:0000313|EMBL:ADP73075.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468,
KW   ECO:0000313|EMBL:ADP73075.1}.
FT   ACT_SITE    378    378       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU10055}.
SQ   SEQUENCE   478 AA;  55634 MW;  3CE303F02759C28C CRC64;
     MEHKQLRPFP DRFLWGSASA AYQVEGAWNE DGKGLSVWDV FAKQPGRTFK GTNGDVAVDH
     YHRYKEDVAL MAEMGLKAYR FSVAWSRVFP NEKGEINEKG LQFYDNLINE LLKHNIEPII
     TLYHWDVPQA LMDEYGAWES RQIIDDFHDY AVTLFQRFGD RVKYWVTLNE QNLFITFGYR
     LGLHPPGVKD AKRMYEANHI ANLANAKVIQ AFRHYVPDGK IGPSFAYSPM YPYDCRPENV
     LAWENAEEFQ NHWWMDVYVW GTYPQAAWNY LEQQGWAPTI KSGDMELLKA GKPDFMGVNY
     YRSQTVQYNP LDGVGEGVMN TTGKKGTSTE SGIPGLFKIV RNPHLEATNW DWEIDPVGLR
     IGLRRIANRY GLPVFITENG LGEFDKLEDG DIVNDDYRID YLRRHIQEIQ RAITDGVDVI
     GYCTWSFTDL LSWLNGYQKR YGFVYVNRDD ESEKDLRRIK KKSFYWYKQV IASNGKEL
//

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