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RRAAH_HALHL
ID   RRAAH_HALHL             Reviewed;         164 AA.
AC   A1WU91;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Hhal_0465;
OS   Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS   halophila (strain DSM 244 / SL1)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=349124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA   Richardson P.;
RT   "Complete sequence of Halorhodospira halophila SL1.";
RL   Submitted (DEC-2006) 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; CP000544; ABM61253.1; -; Genomic_DNA.
DR   RefSeq; WP_011813276.1; NC_008789.1.
DR   AlphaFoldDB; A1WU91; -.
DR   SMR; A1WU91; -.
DR   STRING; 349124.Hhal_0465; -.
DR   EnsemblBacteria; ABM61253; ABM61253; Hhal_0465.
DR   KEGG; hha:Hhal_0465; -.
DR   eggNOG; COG0684; Bacteria.
DR   HOGENOM; CLU_072626_4_0_6; -.
DR   OMA; YADWNGV; -.
DR   OrthoDB; 1614890at2; -.
DR   Proteomes; UP000000647; 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..164
FT                   /note="Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase"
FT                   /id="PRO_1000013845"
FT   BINDING         79..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   164 AA;  17360 MW;  28E3CA810A2890A1 CRC64;
     MALLTTDLCD AYADEPGAQL RAMNPMLIGY GGRARFGGPV TTLKLFEDNV RVRELLSAPG
     DGGVLVVDGG GSMRCALLGD RLAELGRENG WSGAIIYGCV RDSAELAQID FGVQALNTHP
     LKSQKKGLGE RDVSVTFAGV TIQSGDWLYA DEDGVVVASR ELTL
 
 
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