ID Q6MSX3_MYCMS Unreviewed; 281 AA. AC Q6MSX3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 02-JUN-2021, entry version 98. DE SubName: Full=Fructose-bisphosphate aldolase class-II {ECO:0000313|EMBL:CAE77265.1}; DE EC=4.1.2.13 {ECO:0000313|EMBL:CAE77265.1}; GN Name=fbaA1 {ECO:0000313|EMBL:CAE77265.1}; GN OrderedLocusNames=MSC_0644 {ECO:0000313|EMBL:CAE77265.1}; OS Mycoplasma mycoides subsp. mycoides SC (strain PG1). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272632 {ECO:0000313|EMBL:CAE77265.1, ECO:0000313|Proteomes:UP000001016}; RN [1] {ECO:0000313|EMBL:CAE77265.1, ECO:0000313|Proteomes:UP000001016} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PG1 {ECO:0000313|EMBL:CAE77265.1, RC ECO:0000313|Proteomes:UP000001016}; RX PubMed=14762060; DOI=10.1101/gr.1673304; RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J., RA Johansson K.-E., Pettersson B., Uhlen M.; RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP)."; RL Genome Res. 14:221-227(2004). 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; BX293980; CAE77265.1; -; Genomic_DNA. DR RefSeq; NP_975623.1; NC_005364.2. DR STRING; 272632.MSC_0644; -. DR EnsemblBacteria; CAE77265; CAE77265; MSC_0644. DR KEGG; mmy:MSC_0644; -. DR PATRIC; fig|272632.4.peg.693; -. DR eggNOG; COG0191; Bacteria. DR HOGENOM; CLU_040088_1_0_14; -. DR OMA; NNMEIVQ; -. DR Proteomes; UP000001016; Chromosome. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic 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 Pfam; PF01116; F_bP_aldolase; 1. DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1. DR TIGRFAMs; TIGR00167; cbbA; 1. DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1. DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1. PE 4: Predicted; KW Lyase {ECO:0000313|EMBL:CAE77265.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3}; KW Reference proteome {ECO:0000313|Proteomes:UP000001016}; KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}. FT REGION 206..208 FT /note="Dihydroxyacetone phosphate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2" FT REGION 227..230 FT /note="Dihydroxyacetone phosphate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2" FT ACT_SITE 81 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1" FT METAL 82 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT METAL 103 FT /note="Zinc 2" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT METAL 133 FT /note="Zinc 2" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT METAL 177 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT METAL 205 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT BINDING 178 FT /note="Dihydroxyacetone phosphate; via amide nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2" SQ SEQUENCE 281 AA; 31153 MW; 31C59EA0F7C8784A CRC64; MKASLKDQLL KARQNHYAIG AFNFDNLEML KAIVEAAEES NSPIIAMITE SAAKYIGKEI VIASANAIIS NTKVPIVLHW DHGYDLNLIK WACDNEFSSV MLDASLDDFN TNVNKTLEIV NYAKSKNVEV ESEIGHVGGK EDDTDSNIDK YTSVDEAIKF VNLTQIDALA IAVGTSHGIF KTEPNLNFDR IKEIRDSINT PLVLHGSSGL SDTDLKKVIN SGICKINIGT DLKLVYANSL KQWFKENPTS YDARKFGRFA IEQMKNVIKQ KLEILGSINK A //