ID A8FDV5_BACP2 Unreviewed; 446 AA. AC A8FDV5; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 02-SEP-2026, entry version 88. DE SubName: Full=Alpha-galactosidase {ECO:0000313|EMBL:ABV62422.1}; GN OrderedLocusNames=BPUM_1750 {ECO:0000313|EMBL:ABV62422.1}; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV62422.1, ECO:0000313|Proteomes:UP000001355}; RN [1] {ECO:0000313|EMBL:ABV62422.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV62422.1, 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:ABV62422.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV62422.1, 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:ABV62422.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV62422.1, 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=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; 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; ABV62422.1; -; Genomic_DNA. DR RefSeq; WP_012010149.1; NC_009848.4. DR AlphaFoldDB; A8FDV5; -. DR STRING; 315750.BPUM_1750; -. DR PaxDb; 315750-BPUM_1750; -. DR GeneID; 5621011; -. DR KEGG; bpu:BPUM_1750; -. DR eggNOG; COG1486; Bacteria. DR HOGENOM; CLU_045951_1_1_9; -. DR OrthoDB; 9808275at2; -. DR Proteomes; UP000001355; Chromosome. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. 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; cd05297; GH4_alpha_glucosidase_galactosidase; 1. DR Gene3D; 3.90.1820.10; AglA-like glucosidase; 1. DR InterPro; IPR053715; GH4_Enzyme_sf. 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 NCBIfam; NF011657; PRK15076.1; 1. DR PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1. DR PANTHER; PTHR32092:SF6; ALPHA-GALACTOSIDASE; 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. 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 194..405 FT /note="Glycosyl hydrolase family 4 C-terminal" FT /evidence="ECO:0000259|Pfam:PF11975" FT BINDING 148 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2" FT BINDING 169 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3" FT BINDING 199 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3" FT SITE 110 FT /note="Increases basicity of active site Tyr" FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4" SQ SEQUENCE 446 AA; 50584 MW; 9B8F4AF126EB4136 CRC64; MSKITFIGAG STVFAKNILG DCLFVPALSD FEFALYDIDH KRLKESETML RHLKENYGAH VTITSYHNRK EALKDAKYVI NAIQVGGYRP STVIDFEIPK KYGLRQTIAD TVGIGGIFRF LRTFPVMLDL AKEMEEVCPN ALLLNYTNPM ATLTGAMLRY TPVQTVGLCH SVQVCTKDLF ESLEMDHEGI EEKIAGINHM AWLLEVKRDG KDLYPDIKRR AKEKQKSRHH DMVRFELMDK FGYYVTESSE HNAEYHPYFI KSRYPELIGQ FNIPLDEYPR RCEEQINNWN SMKHDLVSNT QITHTRSKEY GSRIIEAIET NVPFKFAGNV LNTGGLIHNL PEKACVEVPC VADRSGIMPC HVGEIPEQLA GLNRTNISSQ LMTIEAAISG KKEHVYQAAL LDPHTSAELS IDDIIKLCDE LIEAHSEMLP HFADPNQYAA STNLQK //