ID   RRAAH_METCA             Reviewed;         161 AA.
AC   Q607E7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=MCA1813;
OS   Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylococcus.
OX   NCBI_TaxID=243233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX   PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA   Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA   Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA   Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA   Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA   Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA   Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA   Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT   "Genomic insights into methanotrophy: the complete genome sequence of
RT   Methylococcus capsulatus (Bath).";
RL   PLoS Biol. 2:1616-1628(2004).
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; AE017282; AAU92150.1; -; Genomic_DNA.
DR   RefSeq; WP_010961066.1; NC_002977.6.
DR   AlphaFoldDB; Q607E7; -.
DR   SMR; Q607E7; -.
DR   STRING; 243233.MCA1813; -.
DR   PRIDE; Q607E7; -.
DR   EnsemblBacteria; AAU92150; AAU92150; MCA1813.
DR   KEGG; mca:MCA1813; -.
DR   eggNOG; COG0684; Bacteria.
DR   HOGENOM; CLU_072626_4_0_6; -.
DR   OMA; RSCDTQF; -.
DR   OrthoDB; 1614890at2; -.
DR   Proteomes; UP000006821; 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..161
FT                   /note="Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase"
FT                   /id="PRO_0000209619"
FT   BINDING         77..80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   161 AA;  17640 MW;  FD55C26B92E1A37F CRC64;
     MEFTTAGLCD QFHGTHPLQI VEPLFRPFGA VSRFHGRITT LKVFEDSVLI RETLAQEVDG
     RVLVIDGGAS HRCALLGGNL ARLAADNGWQ GIIVYGCVRD SVELGTVPIG IRALHTHPLD
     SHKRGGGDRD CLITFASVNF RTDHYLYADE DGIVVSEEKL I