ID A0A0S6U206_CLOBO Unreviewed; 308 AA. AC A0A0S6U206; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 29-SEP-2021, entry version 19. 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, ECO:0000313|Proteomes:UP000054164}; RN [1] {ECO:0000313|Proteomes:UP000054164} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Osaka05 {ECO:0000313|Proteomes:UP000054164}; RA Sakaguchi Y., Hosomi K., Uchiyama J., Ogura Y., Umeda K., Sakaguchi M., RA Kohda T., Mukamoto M., Misawa N., Matsuzaki S., Hayashi T., Kozaki S.; RT "Draft Genome Sequence of Clostridium botulinum Type B Strain Osaka05, RT Isolated from an Infant Patient with Botulism in Japan."; RL Genome Announc. 2:e01010-13(2014). 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 REGION 210..212 FT /note="Dihydroxyacetone phosphate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2" FT REGION 252..255 FT /note="Dihydroxyacetone phosphate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2" FT ACT_SITE 82 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1" FT METAL 83 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT METAL 104 FT /note="Zinc 2" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT METAL 134 FT /note="Zinc 2" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT METAL 178 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT METAL 209 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT BINDING 179 FT /note="Dihydroxyacetone phosphate; via amide nitrogen" 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 //