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4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase (HMG/CHA aldolase) (EC 4.1.3.17) (Oxaloacetate decarboxylase) (OAA decarboxylase) (EC 4.1.1.3)

 HMGA_PSEP1              Reviewed;         238 AA.
A5W059;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
10-JUL-2007, sequence version 1.
28-MAR-2018, entry version 61.
RecName: Full=4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase;
Short=HMG/CHA aldolase;
EC=4.1.3.17 {ECO:0000269|PubMed:20843800};
AltName: Full=Oxaloacetate decarboxylase;
Short=OAA decarboxylase;
EC=4.1.1.3 {ECO:0000269|PubMed:20843800};
OrderedLocusNames=Pput_1361;
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=351746;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
US DOE Joint Genome Institute;
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Parales R.,
Richardson P.;
"Complete sequence of Pseudomonas putida F1.";
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
[2]
X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
PYRUVATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND
MUTAGENESIS OF ARG-123.
STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
PubMed=20843800; DOI=10.1074/jbc.M110.159509;
Wang W., Mazurkewich S., Kimber M.S., Seah S.Y.;
"Structural and kinetic characterization of 4-hydroxy-4-methyl-2-
oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase, a
protocatechuate degradation enzyme evolutionarily convergent with the
HpaI and DmpG pyruvate aldolases.";
J. Biol. Chem. 285:36608-36615(2010).
[3]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=24359411; DOI=10.1021/bi401486g;
Mazurkewich S., Wang W., Seah S.Y.;
"Biochemical and structural analysis of RraA proteins to decipher
their relationships with 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-
4-hydroxy-2-oxoadipate aldolases.";
Biochemistry 53:542-553(2014).
-!- FUNCTION: Catalyzes the last step of the bacterial protocatechuate
4,5-cleavage pathway. The preferred substrates of the enzyme are
2-keto-4-hydroxy acids with a 4-carboxylate substitution.
Catalyzes the conversion of 4-hydroxy-4-methyl-2-oxoglutarate
(HMG) to pyruvate. Also catalyzes the conversion of 4-carboxy-4-
hydroxy-2-oxoadipic acid (CHA) to pyruvate and oxaloacetate.
{ECO:0000269|PubMed:20843800, ECO:0000269|PubMed:24359411}.
-!- CATALYTIC ACTIVITY: 4-hydroxy-4-methyl-2-oxoglutarate = 2
pyruvate. {ECO:0000269|PubMed:20843800,
ECO:0000269|PubMed:24359411}.
-!- CATALYTIC ACTIVITY: 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate =
oxaloacetate + pyruvate. {ECO:0000269|PubMed:20843800}.
-!- CATALYTIC ACTIVITY: Oxaloacetate = pyruvate + CO(2).
{ECO:0000269|PubMed:20843800}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:20843800};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.3 mM for oxaloacetate (in presence of 1 mM of magnesium)
{ECO:0000269|PubMed:20843800};
KM=0.036 mM for oxaloacetate (in presence of 1 mM of manganese)
{ECO:0000269|PubMed:20843800};
KM=0.26 mM for 4-hydroxy-4-methyl-2-oxoglutarate (in presence of
1 mM of magnesium) {ECO:0000269|PubMed:20843800};
KM=0.022 mM for 4-hydroxy-4-methyl-2-oxoglutarate (in presence
of 1 mM of manganese) {ECO:0000269|PubMed:20843800};
KM=0.066 mM for 4-carboxy-4-hydroxy-2-oxoadipic acid or 2-
hydroxy-4-oxobutane-1,2,4-tricarboxylic (in presence of 1 mM of
magnesium) {ECO:0000269|PubMed:20843800};
KM=0.030 mM for 4-carboxy-4-hydroxy-2-oxoadipic acid or 2-
hydroxy-4-oxobutane-1,2,4-tricarboxylic (in presence of 1 mM of
manganese) {ECO:0000269|PubMed:20843800};
KM=0.15 mM for alpha-keto-gamma-hydroxyglutarate (in presence of
1 mM of magnesium) {ECO:0000269|PubMed:20843800};
KM=0.071 mM for alpha-keto-gamma-hydroxyglutarate (in presence
of 1 mM of manganese) {ECO:0000269|PubMed:20843800};
KM=25 mM for 4-hydroxy-2-oxopentanoate (in presence of 1 mM of
magnesium) {ECO:0000269|PubMed:20843800};
KM=8.8 mM for 4-hydroxy-2-oxopentanoate (in presence of 1 mM of
manganese) {ECO:0000269|PubMed:20843800};
-!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:20843800}.
-!- SIMILARITY: Belongs to the LigK/PcmE family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP000712; ABQ77519.1; -; Genomic_DNA.
RefSeq; WP_012051536.1; NC_009512.1.
PDB; 3NOJ; X-ray; 1.82 A; A=1-238.
PDBsum; 3NOJ; -.
ProteinModelPortal; A5W059; -.
SMR; A5W059; -.
STRING; 351746.Pput_1361; -.
EnsemblBacteria; ABQ77519; ABQ77519; Pput_1361.
KEGG; ppf:Pput_1361; -.
eggNOG; ENOG4105JSC; Bacteria.
eggNOG; COG0684; LUCA.
HOGENOM; HOG000107599; -.
KO; K10218; -.
OMA; WCRGPSP; -.
BioCyc; PPUT351746:G1G90-1433-MONOMER; -.
BRENDA; 4.1.3.B3; 5092.
EvolutionaryTrace; A5W059; -.
Proteomes; UP000006553; Chromosome.
GO; GO:0047443; F:4-hydroxy-4-methyl-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
CDD; cd16841; RraA_family; 1.
InterPro; IPR014165; LigK_PcmE.
InterPro; IPR005493; RraA/RraA-like.
InterPro; IPR036704; RraA/RraA-like_sf.
Pfam; PF03737; RraA-like; 1.
SUPFAM; SSF89562; SSF89562; 1.
TIGRFAMs; TIGR02798; ligK_PcmE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Lyase; Magnesium; Metal-binding.
CHAIN 1 238 4-hydroxy-4-methyl-2-oxoglutarate
aldolase/4-carboxy-4-hydroxy-2-oxoadipate
aldolase.
/FTId=PRO_0000418488.
REGION 101 104 Substrate binding. {ECO:0000244|PDB:3NOJ,
ECO:0000269|PubMed:20843800}.
METAL 124 124 Magnesium. {ECO:0000269|PubMed:20843800}.
BINDING 123 123 Substrate. {ECO:0000244|PDB:3NOJ,
ECO:0000269|PubMed:20843800}.
MUTAGEN 123 123 R->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:20843800}.
TURN 3 6 {ECO:0000244|PDB:3NOJ}.
STRAND 9 11 {ECO:0000244|PDB:3NOJ}.
HELIX 20 29 {ECO:0000244|PDB:3NOJ}.
HELIX 31 37 {ECO:0000244|PDB:3NOJ}.
STRAND 49 54 {ECO:0000244|PDB:3NOJ}.
STRAND 57 66 {ECO:0000244|PDB:3NOJ}.
HELIX 73 78 {ECO:0000244|PDB:3NOJ}.
STRAND 85 93 {ECO:0000244|PDB:3NOJ}.
HELIX 102 110 {ECO:0000244|PDB:3NOJ}.
STRAND 115 122 {ECO:0000244|PDB:3NOJ}.
HELIX 125 131 {ECO:0000244|PDB:3NOJ}.
STRAND 134 140 {ECO:0000244|PDB:3NOJ}.
STRAND 152 155 {ECO:0000244|PDB:3NOJ}.
STRAND 157 159 {ECO:0000244|PDB:3NOJ}.
STRAND 162 164 {ECO:0000244|PDB:3NOJ}.
STRAND 169 173 {ECO:0000244|PDB:3NOJ}.
STRAND 176 180 {ECO:0000244|PDB:3NOJ}.
HELIX 182 184 {ECO:0000244|PDB:3NOJ}.
HELIX 185 208 {ECO:0000244|PDB:3NOJ}.
HELIX 212 215 {ECO:0000244|PDB:3NOJ}.
HELIX 219 225 {ECO:0000244|PDB:3NOJ}.
HELIX 233 235 {ECO:0000244|PDB:3NOJ}.
SEQUENCE 238 AA; 25448 MW; 6A44EB4A3C0CB48D CRC64;
MNTLIGKTGI VVRNIQRAEL DSIDALGRLG VATVHEAQNR KGLLSSKMRP IQQGTSLAGS
AVTVLVAPGD NWMFHVAVEQ CRPGDVLVVS PSSPCTDGYF GDLLATSLQA RGVRALIVDA
GVRDTQTLRD MGFAVWARAI NAQGTVKETL GSVNLPVICG GQLINPGDIV VADDDGVVVV
RRDECESTLV AAAERAGLEE EKRLRLAAGE LGLDIYKMRE RLEAKGLRYV DNIEDLEG


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