ID A0A0S6U206_CLOBO Unreviewed; 308 AA. AC A0A0S6U206; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 06-JUL-2016, entry version 5. 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; Clostridiales; 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., RA Sakaguchi M., Kohda T., Mukamoto M., Misawa N., Matsuzaki S., RA 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|SAAS:SAAS00613810}; CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase CC family. {ECO:0000256|SAAS:SAAS00591215}. 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 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 Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011289; Fruc_bis_ald_class-2. DR InterPro; IPR000771; Ketose_bisP_aldolase_II. 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054164}; KW Lyase {ECO:0000256|SAAS:SAAS00485079}; KW Metal-binding {ECO:0000256|SAAS:SAAS00485111}; KW Zinc {ECO:0000256|SAAS:SAAS00485107}. FT REGION 210 212 Dihydroxyacetone phosphate binding. FT {ECO:0000256|PIRSR:PIRSR001359-2}. FT REGION 252 255 Dihydroxyacetone phosphate binding. FT {ECO:0000256|PIRSR:PIRSR001359-2}. FT ACT_SITE 82 82 Proton donor. {ECO:0000256|PIRSR: FT PIRSR001359-1}. FT BINDING 179 179 Dihydroxyacetone phosphate; via amide FT nitrogen. {ECO:0000256|PIRSR:PIRSR001359- FT 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 //