RRAAH_THET8
ID RRAAH_THET8 Reviewed; 164 AA.
AC Q5SIP7; P83846;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=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;
GN OrderedLocusNames=TTHA1322;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND COFACTOR.
RX PubMed=24359411; DOI=10.1021/bi401486g;
RA Mazurkewich S., Wang W., Seah S.Y.;
RT "Biochemical and structural analysis of RraA proteins to decipher their
RT relationships with 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-
RT oxoadipate aldolases.";
RL Biochemistry 53:542-553(2014).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT.
RX PubMed=15502308; DOI=10.1107/s0907444904021146;
RA Rehse P.H., Kuroishi C., Tahirov T.H.;
RT "Structure of the RNA-processing inhibitor RraA from Thermus
RT thermophilis.";
RL Acta Crystallogr. D 60:1997-2002(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.
CC {ECO:0000269|PubMed:24359411}.
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; Evidence={ECO:0000269|PubMed:24359411};
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 Evidence={ECO:0000269|PubMed:24359411};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:24359411};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:24359411};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:24359411};
CC Note=Divalent metal cation. Has preference for nickel and cobalt ions
CC for the HMG aldolase activity. Has preference for zinc ions for the OAA
CC decarboxylase activity. {ECO:0000269|PubMed:24359411};
CC -!- ACTIVITY REGULATION: Competitively inhibited by oxalate, a pyruvate
CC enolate analog. {ECO:0000269|PubMed:24359411}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=150.7 uM for 4-hydroxy-4-methyl-2-oxoglutarate
CC {ECO:0000269|PubMed:24359411};
CC KM=211.4 uM for oxaloacetate {ECO:0000269|PubMed:24359411};
CC Note=kcat is 0.356 sec(-1) with 4-hydroxy-4-methyl-2-oxoglutarate as
CC substrate and 1.06 sec(-1) with oxaloacetate as substrate.;
CC -!- SUBUNIT: Homotrimer. {ECO:0000305|PubMed:15502308}.
CC -!- SIMILARITY: Belongs to the class II aldolase/RraA-like family.
CC {ECO:0000305}.
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DR EMBL; AP008226; BAD71145.1; -; Genomic_DNA.
DR RefSeq; WP_011228595.1; NC_006461.1.
DR RefSeq; YP_144588.1; NC_006461.1.
DR PDB; 1J3L; X-ray; 2.30 A; A/B/C/D/E/F=1-164.
DR PDBsum; 1J3L; -.
DR AlphaFoldDB; Q5SIP7; -.
DR SMR; Q5SIP7; -.
DR STRING; 300852.55772704; -.
DR EnsemblBacteria; BAD71145; BAD71145; BAD71145.
DR GeneID; 3168568; -.
DR KEGG; ttj:TTHA1322; -.
DR eggNOG; COG0684; Bacteria.
DR HOGENOM; CLU_072626_4_0_0; -.
DR OMA; RSCDTQF; -.
DR PhylomeDB; Q5SIP7; -.
DR EvolutionaryTrace; Q5SIP7; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; Lyase; Metal-binding; Reference proteome.
FT CHAIN 1..164
FT /note="4-hydroxy-4-methyl-2-oxoglutarate aldolase"
FT /id="PRO_1000013877"
FT BINDING 74..77
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 26..39
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1J3L"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1J3L"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:1J3L"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:1J3L"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:1J3L"
SQ SEQUENCE 164 AA; 17345 MW; 84F94FD9FDD952FA CRC64;
MEARTTDLSD LYPEGEALPM VFKSFGGRAR FAGRVRTLRV FEDNALVRKV LEEEGAGQVL
FVDGGGSLRT ALLGGNLARL AWEKGWAGVV VHGAVRDTEE LREVPIGLLA LAATPKKSAK
EGKGEVDVPL KVLGVEVLPG SFLLADEDGL LLLPEPPSGV RSGG
