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4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase (HMG/CHA aldolase) (EC 4.1.3.16) (EC 4.1.3.17) (4-hydroxy-2-oxoglutarate aldolase) (Oxaloacetate decarboxylase) (OAA decarboxylase) (EC 4.1.1.3)

 HMGA_PSEOC              Reviewed;         227 AA.
Q9AQI0;
08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
12-SEP-2018, entry version 52.
RecName: Full=4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase;
Short=HMG/CHA aldolase;
EC=4.1.3.16 {ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032};
EC=4.1.3.17 {ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032};
AltName: Full=4-hydroxy-2-oxoglutarate aldolase;
AltName: Full=Oxaloacetate decarboxylase;
Short=OAA decarboxylase;
EC=4.1.1.3 {ECO:0000269|PubMed:2229032};
Name=proA {ECO:0000312|EMBL:BAB21456.3};
Pseudomonas straminea.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=47882;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-22, FUNCTION,
CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=NGJ1 {ECO:0000312|EMBL:BAB21456.3};
PubMed=11826967; DOI=10.1271/bbb.65.2701;
Maruyama K., Miwa M., Tsujii N., Nagai T., Tomita N., Harada T.,
Sobajima H., Sugisaki H.;
"Cloning, sequencing, and expression of the gene encoding 4-hydroxy-4-
methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae NGJ1.";
Biosci. Biotechnol. Biochem. 65:2701-2709(2001).
[2]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
PubMed=2229032; DOI=10.1093/oxfordjournals.jbchem.a123201;
Maruyama K.;
"Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate
aldolase from Pseudomonas ochraceae grown on phthalate.";
J. Biochem. 108:327-333(1990).
[3]
ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=2229033;
Maruyama K.;
"Activation of Pseudomonas ochraceae 4-hydroxy-4-methyl-2-oxoglutarate
aldolase by inorganic phosphate.";
J. Biochem. 108:334-340(1990).
[4]
ACTIVITY REGULATION.
PubMed=1794988; DOI=10.1093/oxfordjournals.jbchem.a123699;
Maruyama K.;
"Chemical modification of Pseudomonas ochraceae 4-hydroxy-4-methyl-2-
oxoglutarate aldolase by diethyl pyrocarbonate.";
J. Biochem. 110:976-981(1991).
-!- FUNCTION: Catalyzes the last step of the bacterial protocatechuate
4,5-cleavage pathway. Has a broad substrate specificity and
catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate,
4-hydroxy-2-oxoglutarate and 4-carboxy-4-hydroxy-2-oxoadipate, and
the decarboxylation of oxaloacetate. Preferentially cleaves the L-
isomer of 4-carboxy-4-hydroxy-2-oxoadipate, and has lower activity
towards 4-hydroxy-4-methyl-2-oxoglutarate and 4-Hydroxy-2-
oxoglutarate. Does not cleave 4-hydroxy-2-oxovalerate, citrate, 4-
hydroxy-2-oxobutyrate, 2-oxoglutarate or fructose-1,6-
bisphosphate. {ECO:0000269|PubMed:11826967,
ECO:0000269|PubMed:2229032}.
-!- CATALYTIC ACTIVITY: 4-hydroxy-2-oxoglutarate = pyruvate +
glyoxylate. {ECO:0000269|PubMed:11826967,
ECO:0000269|PubMed:2229032}.
-!- CATALYTIC ACTIVITY: 4-hydroxy-4-methyl-2-oxoglutarate = 2
pyruvate. {ECO:0000269|PubMed:11826967,
ECO:0000269|PubMed:2229032}.
-!- CATALYTIC ACTIVITY: 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate =
oxaloacetate + pyruvate. {ECO:0000269|PubMed:11826967,
ECO:0000269|PubMed:2229032}.
-!- CATALYTIC ACTIVITY: Oxaloacetate = pyruvate + CO(2).
{ECO:0000269|PubMed:2229032}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11826967,
ECO:0000269|PubMed:2229032};
Note=Divalent metal cations. Probably Mg(2+).
{ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032};
-!- ACTIVITY REGULATION: Cleavage of 4-carboxy-4-hydroxy-2-oxoadipate,
and to a lesser extent 4-hydroxy-4-methyl-2-oxoglutarate, is
inhibited by lysine modification caused by diethyl pyrocarbonate.
Decarboxylation of oxaloacetate is unaffected by diethyl
pyrocarbonate. Inhibited by BeCl(2), CaCl(2), NiCl(2), BaCl(2),
HgCl(2), SrSO(4), CrCl(3) and FeCl(3). Partially inhibited by p-
chloromercuribenzoate and N-ethylmaleimide. Activated by inorganic
phosphate, arsenate, phosphorous acid, acetyl phosphate, thiamine
diphosphate, ADP, ATP and diphosphate.
{ECO:0000269|PubMed:1794988, ECO:0000269|PubMed:2229032,
ECO:0000269|PubMed:2229033}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.044 mM for DL-4-carboxy-4-hydroxy-2-oxoadipate
{ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
ECO:0000269|PubMed:2229033};
KM=0.019 mM for L-4-carboxy-4-hydroxy-2-oxoadipate
{ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
ECO:0000269|PubMed:2229033};
KM=0.15 mM for D-4-carboxy-4-hydroxy-2-oxoadipate
{ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
ECO:0000269|PubMed:2229033};
KM=1.25 mM for DL-4-hydroxy-4-methyl-2-oxoglutarate
{ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
ECO:0000269|PubMed:2229033};
KM=0.24 mM for DL-4-hydroxy-2-oxoglutarate
{ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
ECO:0000269|PubMed:2229033};
KM=0.50 mM for oxaloacetate {ECO:0000269|PubMed:11826967,
ECO:0000269|PubMed:2229032, ECO:0000269|PubMed:2229033};
Vmax=1250 umol/min/mg enzyme with DL-4-carboxy-4-hydroxy-2-
oxoadipate as substrate {ECO:0000269|PubMed:11826967,
ECO:0000269|PubMed:2229032, ECO:0000269|PubMed:2229033};
Vmax=1220 umol/min/mg enzyme with L-4-carboxy-4-hydroxy-2-
oxoadipate as substrate {ECO:0000269|PubMed:11826967,
ECO:0000269|PubMed:2229032, ECO:0000269|PubMed:2229033};
Vmax=67.6 umol/min/mg enzyme with D-4-carboxy-4-hydroxy-2-
oxoadipate as substrate {ECO:0000269|PubMed:11826967,
ECO:0000269|PubMed:2229032, ECO:0000269|PubMed:2229033};
Vmax=213 umol/min/mg enzyme with DL-4-hydroxy-4-methyl-2-
oxoglutarate as substrate {ECO:0000269|PubMed:11826967,
ECO:0000269|PubMed:2229032, ECO:0000269|PubMed:2229033};
Vmax=1.3 umol/min/mg enzyme with DL-4-hydroxy-2-oxoglutarate as
substrate {ECO:0000269|PubMed:11826967,
ECO:0000269|PubMed:2229032, ECO:0000269|PubMed:2229033};
Vmax=20.8 umol/min/mg enzyme with oxaloacetate as substrate
{ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
ECO:0000269|PubMed:2229033};
pH dependence:
Optimum pH varies depending on the substrate used and phosphate
concentration. In the absence of inorganic phosphate pH optima
are 6.6 for L-4-carboxy-4-hydroxy-2-oxoadipate, 8.0 for D-4-
carboxy-4-hydroxy-2-oxoadipate, 6.7 and 8.0 for DL-4-carboxy-4-
hydroxy-2-oxoadipate, 8.3 for DL-4-hydroxy-4-methyl-2-
oxoglutarate, 9.3 for DL-4-hydroxy-2-oxoglutarate and 8.8 for
oxaloacetate. In the presence of 3 mM inorganic phosphate pH
optima are more alkaline: 8.2 for L-4-carboxy-4-hydroxy-2-
oxoadipate, 8.6 for D-4-carboxy-4-hydroxy-2-oxoadipate, 8.2 for
DL-4-carboxy-4-hydroxy-2-oxoadipate, 8.9 for DL-4-hydroxy-4-
methyl-2-oxoglutarate, 9.4 for DL-4-hydroxy-2-oxoglutarate and
8.9 for oxaloacetate. Stable at pH 6.0 to pH 9.5.
{ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
ECO:0000269|PubMed:2229033};
Temperature dependence:
Retains 50% of maximum activity after incubation at 54 degrees
Celsius for 10 minutes. {ECO:0000269|PubMed:11826967,
ECO:0000269|PubMed:2229032, ECO:0000269|PubMed:2229033};
-!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:2229032}.
-!- INDUCTION: By growth on aromatic carboxylates such as phthalate,
terephthalate, m-hydroxybenzoate and p-hydroxybenzoate.
{ECO:0000269|PubMed:2229032}.
-!- SIMILARITY: Belongs to the LigK/PcmE family. {ECO:0000305}.
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EMBL; AB050935; BAB21456.3; -; Genomic_DNA.
ProteinModelPortal; Q9AQI0; -.
SMR; Q9AQI0; -.
BioCyc; MetaCyc:MONOMER-3244; -.
GO; GO:0008700; F:4-hydroxy-2-oxoglutarate aldolase activity; IDA:UniProtKB.
GO; GO:0047443; F:4-hydroxy-4-methyl-2-oxoglutarate aldolase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008948; F:oxaloacetate decarboxylase activity; IDA:UniProtKB.
GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IDA:UniProtKB.
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;
Direct protein sequencing; Lyase; Magnesium; Metal-binding.
CHAIN 1 227 4-hydroxy-4-methyl-2-oxoglutarate
aldolase/4-carboxy-4-hydroxy-2-oxoadipate
aldolase.
/FTId=PRO_0000403973.
REGION 97 100 Substrate binding.
{ECO:0000250|UniProtKB:A5W059}.
METAL 120 120 Magnesium.
{ECO:0000250|UniProtKB:A5W059}.
BINDING 119 119 Substrate.
{ECO:0000250|UniProtKB:A5W059}.
SEQUENCE 227 AA; 24068 MW; F56501D5BDD0262F CRC64;
MYELGVVYRN IQRADRAAAD GLAALGSATV HEAMGRVGLL KPYMRPIYAG KQVSGTAVTV
LLQPGDNWMM HVAAEQIQPG DIVVAAVTAE CTDGYFGDLL ATSFQARGAR ALIIDAGVRD
VKTLQEMDFP VWSKAISSKG TIKATLGSVN IPIVCAGMLV TPGDVIVADD DGVVCVPAAR
AVEVLAAAQK RESFEGEKRA KLASGVLGLD MYKMREPLEK AGLKYID


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