ID E8UQT9_THEBF Unreviewed; 464 AA. AC E8UQT9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 43. DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ADV80509.1}; DE EC=3.2.1.86 {ECO:0000313|EMBL:ADV80509.1}; GN OrderedLocusNames=Thebr_1990 {ECO:0000313|EMBL:ADV80509.1}; OS Thermoanaerobacter brockii subsp. finnii (strain ATCC 43586 / DSM 3389 / OS AKO-1) (Thermoanaerobacter finnii). OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=509193 {ECO:0000313|EMBL:ADV80509.1, ECO:0000313|Proteomes:UP000002062}; RN [1] {ECO:0000313|EMBL:ADV80509.1, ECO:0000313|Proteomes:UP000002062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43586 / DSM 3389 / AKO-1 RC {ECO:0000313|Proteomes:UP000002062}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Hemme C.L., Woyke T.; RT "Complete sequence of Thermoanaerobacter brockii finnii Ako-1."; RL Submitted (JAN-2011) 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002466; ADV80509.1; -; Genomic_DNA. DR RefSeq; WP_009051876.1; NC_014964.1. DR AlphaFoldDB; E8UQT9; -. DR KEGG; tbo:Thebr_1990; -. DR HOGENOM; CLU_001859_0_1_9; -. DR Proteomes; UP000002062; 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; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1. DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 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. PE 3: Inferred from homology; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ADV80509.1}; KW Hydrolase {ECO:0000313|EMBL:ADV80509.1}. FT ACT_SITE 367 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055" SQ SEQUENCE 464 AA; 54611 MW; 87D0F74A20FD091E CRC64; MAKEYKFPEG FWWGSATSAV QIEGAANEDG KGMNVWDYWY KNEPNRFFDR VGPQVTSDFY HRYKDDIKLM KELGHNSFRF SISWSRLIPG GVGEVNKKAV EFYNSVIDEL IKNDIEPFVT LFHFDMPIEM QNMGGFENRK VVEYFAEYAK TCFELFGDRV KRWITFNEPI VPVLGGYLYN FHYPDIVDFK RAVQFAYGTV LASARAIEEF KKLQIERAKI GIVLNLSPVY PRSNHPADLK AAEIADLFYN RSFLDPTVKG EYPKELVELL KTYNHLPEYS DSDLELIKNN TVEYLGVNYY QPIRVKAKEN MPNPYGVFTP NWFYDEYIMP GRRMNPYRGW EIYERGIYDI MINLRDNYGN IGSFISENGM GVEGEERFIK DGIIQDDYRI EFIKEHLKWL HKAIEEGCNV KGYHLWTFMD NWSFLNAYKN RYGLVSVDLK TQKRTIKKSG YWYKELSENN GFVD //