RRAAH_PSEA7
ID RRAAH_PSEA7 Reviewed; 162 AA.
AC A6V753;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=4.1.1.112;
DE AltName: Full=Regulator of ribonuclease activity homolog;
DE AltName: Full=RraA-like protein;
GN OrderedLocusNames=PSPA7_3534;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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 common
CC pyruvate enolate transition state formed following C-C bond cleavage in
CC the retro-aldol and decarboxylation reactions (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate;
CC Xref=Rhea:RHEA:22748, ChEBI:CHEBI:15361, ChEBI:CHEBI:58276;
CC EC=4.1.3.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16526; EC=4.1.1.112;
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}.
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DR EMBL; CP000744; ABR81960.1; -; Genomic_DNA.
DR RefSeq; WP_003152917.1; NC_009656.1.
DR AlphaFoldDB; A6V753; -.
DR SMR; A6V753; -.
DR EnsemblBacteria; ABR81960; ABR81960; PSPA7_3534.
DR KEGG; pap:PSPA7_3534; -.
DR HOGENOM; CLU_072626_4_0_6; -.
DR OMA; YADWNGV; -.
DR OrthoDB; 1614890at2; -.
DR Proteomes; UP000001582; Chromosome.
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 Lyase; Metal-binding.
FT CHAIN 1..162
FT /note="Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase"
FT /id="PRO_1000013856"
FT BINDING 75..78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 162 AA; 17362 MW; 4F8F1B628344D0AE CRC64;
MHYVTPDLCD AYPELVQVVE PMFSNFGGRD AFGGEIVTIK CFEDNSLVKE QVDKDGKGKV
LVVDGGGSLR RALLGDMLAE KAAKNGWEGI VVYGCIRDVD VIAQTELGVQ ALASHPMKTD
KRGIGDLNVV VTFGGVTFRP GEFVYADNNG IIVSPQALNM PG
