ID   RRAAH_PSEF5             Reviewed;         163 AA.
AC   Q4KFJ3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=PFL_1871;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY91159.1; -; Genomic_DNA.
DR   RefSeq; WP_011060191.1; NC_004129.6.
DR   AlphaFoldDB; Q4KFJ3; -.
DR   SMR; Q4KFJ3; -.
DR   STRING; 220664.PFL_1871; -.
DR   PRIDE; Q4KFJ3; -.
DR   EnsemblBacteria; AAY91159; AAY91159; PFL_1871.
DR   GeneID; 57474888; -.
DR   KEGG; pfl:PFL_1871; -.
DR   PATRIC; fig|220664.5.peg.1906; -.
DR   eggNOG; COG0684; Bacteria.
DR   HOGENOM; CLU_072626_4_0_6; -.
DR   OMA; YADWNGV; -.
DR   OrthoDB; 1614890at2; -.
DR   Proteomes; UP000008540; 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; Reference proteome.
FT   CHAIN           1..163
FT                   /note="Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase"
FT                   /id="PRO_1000013859"
FT   BINDING         76..79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   163 AA;  17563 MW;  57C247CFD0C144EB CRC64;
     MNHYLTPDLC DAYPDLVQVV EPMFSNFGGR DSFGGEIVTI KCFEDNSLVK EQVELKGQGK
     VLVVDGGGSL RRALLGDMLA EKAAKNGWEG LVIYGCIRDV DVIAQTDLGV QALASHPMKT
     DKRGIGDLNV AVTFAGVTFR PGEYVYADNN GVIVSPSPLK MPE