ID A0A0S6U206_CLOBO Unreviewed; 308 AA. AC A0A0S6U206; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 12-OCT-2022, entry version 23. DE SubName: Full=Fructose-1,6-bisphosphate aldolase, class II {ECO:0000313|EMBL:GAE00620.1}; GN ORFNames=CBO05C_0310 {ECO:0000313|EMBL:GAE00620.1}; OS Clostridium botulinum B str. Osaka05. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1407017 {ECO:0000313|EMBL:GAE00620.1}; RN [1] {ECO:0000313|EMBL:GAE00620.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Osaka05 {ECO:0000313|EMBL:GAE00620.1}; RA Sakaguchi Y., Hosomi K., Uchiyama J., Ogura Y., Sakaguchi M., Kohda T., RA Mukamoto M., Misawa N., Matsuzaki S., Hayashi T., Kozaki S.; RT "Draft genome sequence of Clostridium botulinum type B strain Osaka05."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR001359-3}; CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other CC provides a structural contribution. {ECO:0000256|PIRSR:PIRSR001359-3}; 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; DF384213; GAE00620.1; -; Genomic_DNA. DR RefSeq; WP_030032947.1; NZ_DF384213.1. DR EnsemblBacteria; GAE00620; GAE00620; CBO05C_0310. DR HOGENOM; CLU_040088_0_0_9; -. DR Proteomes; UP000054164; Unassembled WGS sequence. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:InterPro. DR CDD; cd00947; TBP_aldolase_IIB; 1. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000771; FBA_II. DR InterPro; IPR011289; Fruc_bis_ald_class-2. DR Pfam; PF01116; F_bP_aldolase; 1. DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1. DR TIGRFAMs; TIGR00167; cbbA; 1. DR TIGRFAMs; TIGR01859; fruc_bis_ald; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3}; KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}. FT ACT_SITE 82 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1" FT BINDING 83 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT BINDING 104 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT BINDING 134 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT BINDING 178 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT BINDING 179 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2" FT BINDING 209 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT BINDING 210..212 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2" FT BINDING 252..255 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2" SQ SEQUENCE 308 AA; 33059 MW; D26149B9AE5D57B7 CRC64; MALVTTKEMF KKAYEGKYAI GAFNINNMEI LQGVVNAAKA ANSAVILQVS AGALKYAGPK YLKAMVDAAI ADTGIDVALH LDHGASLDVV KLAIDSGFTS VMFDGSHYDY EENVAKTKEV VEYAHSHGVV VEAELGVLAG VEDDVQSDVH IYTDPEQAVD FVNRTGVDSL AIAIGTSHGA YKFAGEAQLR FDILEEIQSK LPGYPIVLHG ASSVDPESVD TCNKYGGEIK GAKGVPADML RKASSMAVCK INMDTDLRLA MTAGIRKVLS EDPKQFDPRK YLGEGRARIE KIVEDKIKDV LGSTDSLK //