ID RRAAH_CUPTR Reviewed; 165 AA. AC B3R2J3; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 1. DT 12-SEP-2018, entry version 62. DE RecName: Full=Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase; DE Short=HMG aldolase; DE EC=4.1.3.17; DE AltName: Full=Oxaloacetate decarboxylase; DE Short=OAA decarboxylase; DE EC=4.1.1.3; DE AltName: Full=Regulator of ribonuclease activity homolog; DE AltName: Full=RraA-like protein; GN OrderedLocusNames=RALTA_A1769; OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CIP 107171 / OS LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=977880; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17343 / BCRC 17206 / CIP 107171 / LMG 19424 / R1; RX PubMed=18490699; DOI=10.1101/gr.076448.108; RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., RA Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., RA Batut J., Medigue C., Masson-Boivin C.; RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and RT comparative genomics of rhizobia."; RL Genome Res. 18:1472-1483(2008). CC -!- FUNCTION: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2- CC oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a CC secondary oxaloacetate (OAA) decarboxylase activity due to the CC common pyruvate enolate transition state formed following C-C bond CC cleavage in the retro-aldol and decarboxylation reactions (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 4-hydroxy-4-methyl-2-oxoglutarate = 2 CC pyruvate. CC -!- CATALYTIC ACTIVITY: Oxaloacetate = pyruvate + CO(2). CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250}; CC Note=Divalent metal cation. {ECO:0000250}; CC -!- SUBUNIT: Homotrimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class II aldolase/RraA-like family. CC {ECO:0000305}. 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; CU633749; CAQ69711.1; -; Genomic_DNA. DR RefSeq; WP_012353031.1; NC_010528.1. DR ProteinModelPortal; B3R2J3; -. DR SMR; B3R2J3; -. DR STRING; 977880.RALTA_A1769; -. DR EnsemblBacteria; CAQ69711; CAQ69711; RALTA_A1769. DR GeneID; 29761907; -. DR KEGG; cti:RALTA_A1769; -. DR eggNOG; ENOG4108YYX; Bacteria. DR eggNOG; COG0684; LUCA. DR HOGENOM; HOG000252803; -. DR KO; K02553; -. DR OMA; RSCDTQF; -. DR BioCyc; CTAI977880:RALTA_RS08525-MONOMER; -. DR Proteomes; UP000001692; Chromosome 1. DR GO; GO:0047443; F:4-hydroxy-4-methyl-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0008428; F:ribonuclease inhibitor activity; IEA:InterPro. DR GO; GO:0051252; P:regulation of RNA metabolic process; IEA:InterPro. DR CDD; cd16841; RraA_family; 1. DR InterPro; IPR010203; RraA. DR InterPro; IPR005493; RraA/RraA-like. DR InterPro; IPR036704; RraA/RraA-like_sf. DR Pfam; PF03737; RraA-like; 1. DR SUPFAM; SSF89562; SSF89562; 1. DR TIGRFAMs; TIGR01935; NOT-MenG; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Metal-binding; Reference proteome. FT CHAIN 1 165 Putative 4-hydroxy-4-methyl-2- FT oxoglutarate aldolase. FT /FTId=PRO_1000125597. FT REGION 80 83 Substrate binding. {ECO:0000250}. FT METAL 103 103 Divalent metal cation. {ECO:0000250}. FT BINDING 102 102 Substrate. {ECO:0000250}. SQ SEQUENCE 165 AA; 17532 MW; 5E44558C80B85792 CRC64; MKPVTTDLCD AHEDRLAEGT LRVMAPVFRA FGKQPAFAGP AATLKVFEDN SLVRATLESP GRGRVLVIDG GGSLRCALVG GNLGLLAEKN GWVGIVVNGC IRDTAELDVC DIGIRALAAH PQKSQKRNVG ESEVTVQMPG AVVRPGNWIY VDVDGILVAD DKLER //