ID   RRAAH_COREF             Reviewed;         170 AA.
AC   Q8FQY0;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2003, sequence version 2.
DT   03-AUG-2022, entry version 92.
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=CE0987;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC17797.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000035; BAC17797.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_035109947.1; NZ_GG700688.1.
DR   AlphaFoldDB; Q8FQY0; -.
DR   SMR; Q8FQY0; -.
DR   STRING; 196164.23492825; -.
DR   EnsemblBacteria; BAC17797; BAC17797; BAC17797.
DR   KEGG; cef:CE0987; -.
DR   eggNOG; COG0684; Bacteria.
DR   HOGENOM; CLU_072626_4_0_11; -.
DR   Proteomes; UP000001409; 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..170
FT                   /note="Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase"
FT                   /id="PRO_0000209608"
FT   BINDING         81..84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   170 AA;  17719 MW;  7696EAE1E320198A CRC64;
     MTDTHGTFIP TADLVDIIGD DVRSCDTQFR NLGGRTDFHG TITTVKCFQD NALLKSILGE
     DNPGGVLVID GDASLHTALV GDIIAGLGRD HGWSGVVVNG AIRDSAVIGE MEFGCKALGT
     NPRKSSKTGA GERDVVVSFG GVDFTPGHYL YADSDGIVVT ENPVKAPASN