ID   RRAAH_MYCLB             Reviewed;         157 AA.
AC   B8ZTT3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, 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=MLBr00066;
OS   Mycobacterium leprae (strain Br4923).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=561304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Br4923;
RX   PubMed=19881526; DOI=10.1038/ng.477;
RA   Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA   Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA   Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA   Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA   Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA   Rougemont J., Brennan P.J., Cole S.T.;
RT   "Comparative genomic and phylogeographic analysis of Mycobacterium
RT   leprae.";
RL   Nat. Genet. 41:1282-1289(2009).
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; FM211192; CAR70159.1; -; Genomic_DNA.
DR   RefSeq; WP_010907499.1; NC_011896.1.
DR   AlphaFoldDB; B8ZTT3; -.
DR   SMR; B8ZTT3; -.
DR   EnsemblBacteria; CAR70159; CAR70159; MLBr00066.
DR   KEGG; mlb:MLBr00066; -.
DR   HOGENOM; CLU_072626_4_0_11; -.
DR   OMA; RSCDTQF; -.
DR   OrthoDB; 1614890at2; -.
DR   Proteomes; UP000006900; 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..157
FT                   /note="Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase"
FT                   /id="PRO_1000135496"
FT   BINDING         78..81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   157 AA;  16193 MW;  F2191ACE6382EE53 CRC64;
     MIVSFRPTAD LVDSIGVDVR SCDLQFRQFG GCSEFAGPIS TVRCFQDNAL LKSVLSQTSA
     GGVLVVDGAG SLHTALVGDV IAELAHSNGW AGLIVNGAVR DAAALRGIDI GIKALGTNPR
     KSTKIGTGER HVEVNLGGVT FVPGEVVYSD DDGIVVV