ID A8FIT4_BACP2 Unreviewed; 442 AA. AC A8FIT4; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 04-NOV-2026, entry version 93. DE RecName: Full=6-phospho-beta-glucosidase {ECO:0000256|ARBA:ARBA00066487}; DE EC=3.2.1.86 {ECO:0000256|ARBA:ARBA00066487}; GN OrderedLocusNames=BPUM_3503 {ECO:0000313|EMBL:ABV64151.1}; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV64151.1, ECO:0000313|Proteomes:UP000001355}; RN [1] {ECO:0000313|EMBL:ABV64151.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV64151.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y., RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., RA Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(2007). RN [2] {ECO:0000313|EMBL:ABV64151.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV64151.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=23812891; DOI=10.1007/s00792-013-0559-z; RA Tirumalai M.R., Fox G.E.; RT "An ICEBs1-like element may be associated with the extreme radiation and RT desiccation resistance of Bacillus pumilus SAFR-032 spores."; RL Extremophiles 17:767-774(2013). RN [3] {ECO:0000313|EMBL:ABV64151.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV64151.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=23799069; RA Tirumalai M.R., Rastogi R., Zamani N., O'Bryant Williams E., Allen S., RA Diouf F., Kwende S., Weinstock G.M., Venkateswaran K.J., Fox G.E.; RT "Candidate genes that may be responsible for the unusual resistances RT exhibited by Bacillus pumilus SAFR-032 spores."; RL PLoS ONE 8:E66012-E66012(2013). CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000256|RuleBase:RU361152}; CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. CC {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}. 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; CP000813; ABV64151.1; -; Genomic_DNA. DR RefSeq; WP_012011705.1; NC_009848.4. DR AlphaFoldDB; A8FIT4; -. DR STRING; 315750.BPUM_3503; -. DR PaxDb; 315750-BPUM_3503; -. DR GeneID; 5622792; -. DR KEGG; bpu:BPUM_3503; -. DR eggNOG; COG1486; Bacteria. DR HOGENOM; CLU_045951_0_1_9; -. DR OMA; AAHMPEC; -. DR OrthoDB; 9808275at2; -. DR Proteomes; UP000001355; Chromosome. DR GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd05296; GH4_P_beta_glucosidase; 1. DR FunFam; 3.40.50.720:FF:000163; 6-phospho-beta-glucosidase; 1. DR FunFam; 3.90.110.10:FF:000008; 6-phospho-beta-glucosidase; 1. DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR019802; GlycHydrolase_4_CS. DR InterPro; IPR001088; Glyco_hydro_4. DR InterPro; IPR022616; Glyco_hydro_4_C. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR32092:SF5; 6-PHOSPHO-BETA-GLUCOSIDASE; 1. DR PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1. DR Pfam; PF02056; Glyco_hydro_4; 1. DR Pfam; PF11975; Glyco_hydro_4C; 1. DR PRINTS; PR00732; GLHYDRLASE4. DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277}; KW Cobalt {ECO:0000256|PIRSR:PIRSR601088-3}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361152}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361152}; KW Iron {ECO:0000256|PIRSR:PIRSR601088-3}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR601088-3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR601088-3}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU361152}; KW Nickel {ECO:0000256|PIRSR:PIRSR601088-3}; KW Reference proteome {ECO:0000313|Proteomes:UP000001355}. FT DOMAIN 197..412 FT /note="Glycosyl hydrolase family 4 C-terminal" FT /evidence="ECO:0000259|Pfam:PF11975" FT BINDING 96 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2" FT BINDING 150 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2" FT BINDING 172 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3" FT BINDING 202 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3" FT SITE 112 FT /note="Increases basicity of active site Tyr" FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4" SQ SEQUENCE 442 AA; 49007 MW; 80D0204A699F15DB CRC64; MKEGIKIVTI GGGSSYTPEL VEGFIKRYHE LPVKELWLVD IEAGQEKLNI VGALAKRMVE KAGLPIEVHL TLDRREALKD ADFVTTQFRV GLLEARAKDE RIPLKYGVIG QETNGPGGLF KGLRTIPVIL DIVKDMEELC PDAWLVNFTN PAGMVTEAVL RYTNLKKVVG LCNVPIGIKM GIAKALEVDV ERIEVQFAGL NHMVYGLDVY LDGVSIMDQV LDELGNPNSQ WSMKNIEAKN WEPSFVKGLG VIPCPYHRYY YKTKDMLEEE QKAAQEKGTR AEVVLQVEHE LFELYKDPDL SIKPPQLEKR GGAYYSDAAC NLISSIYNDK HDIQPVNTVN RGAIASIPAD SAVEVNCIIT KDGPKPIATG DLPVAVRGLV QQIKSFERVA AEAAVTGDYE TALVAMTINP LVPSDEIAKQ ILDEMLEAHR EYLPQFFKSV KA //