RRAAH_ALKHC
ID RRAAH_ALKHC Reviewed; 210 AA.
AC Q9KBI9;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=BH1938;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB05657.1; -; Genomic_DNA.
DR PIR; B83892; B83892.
DR AlphaFoldDB; Q9KBI9; -.
DR SMR; Q9KBI9; -.
DR STRING; 272558.10174556; -.
DR EnsemblBacteria; BAB05657; BAB05657; BAB05657.
DR KEGG; bha:BH1938; -.
DR eggNOG; COG0684; Bacteria.
DR HOGENOM; CLU_072626_3_2_9; -.
DR OMA; MKLCGPA; -.
DR Proteomes; UP000001258; 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 CDD; cd16841; RraA_family; 1.
DR InterPro; IPR005493; RraA/RraA-like.
DR InterPro; IPR036704; RraA/RraA-like_sf.
DR Pfam; PF03737; RraA-like; 1.
DR SUPFAM; SSF89562; SSF89562; 1.
PE 3: Inferred from homology;
KW Lyase; Metal-binding; Reference proteome.
FT CHAIN 1..210
FT /note="Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase"
FT /id="PRO_0000209655"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 210 AA; 22154 MW; 7A96BCCBFEBCC50E CRC64;
MSQAEIDFIT QFRTIPTTCI SDALDGLTNL TSTIKPLNEN DQVVGPARTV QVASGDNLAV
LKAMYEASPG DVIVIDAKGD CTRAIAGDFV LGMAKTLGIA GFVVDGAIRD IRASKALNFP
IFCRGTTIAA SKKTGIGNIN VPISCGGVPI RPGDLIVGDA DGVTVIPKGQ EENVLQKAKK
KQADDEARER AISDNVMAIR AYLEKMIHPS
