HMGA_PSEOC
ID HMGA_PSEOC Reviewed; 227 AA.
AC Q9AQI0;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase;
DE Short=HMG/CHA aldolase;
DE EC=4.1.3.16 {ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032};
DE EC=4.1.3.17 {ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032};
DE AltName: Full=4-hydroxy-2-oxoglutarate aldolase;
DE AltName: Full=Oxaloacetate decarboxylase;
DE Short=OAA decarboxylase;
DE EC=4.1.1.112 {ECO:0000269|PubMed:2229032};
GN Name=proA {ECO:0000312|EMBL:BAB21456.3};
OS Pseudomonas straminea.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=47882;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-22, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=NGJ1 {ECO:0000312|EMBL:BAB21456.3};
RX PubMed=11826967; DOI=10.1271/bbb.65.2701;
RA Maruyama K., Miwa M., Tsujii N., Nagai T., Tomita N., Harada T.,
RA Sobajima H., Sugisaki H.;
RT "Cloning, sequencing, and expression of the gene encoding 4-hydroxy-4-
RT methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae NGJ1.";
RL Biosci. Biotechnol. Biochem. 65:2701-2709(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
RX PubMed=2229032; DOI=10.1093/oxfordjournals.jbchem.a123201;
RA Maruyama K.;
RT "Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase
RT from Pseudomonas ochraceae grown on phthalate.";
RL J. Biochem. 108:327-333(1990).
RN [3]
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2229033; DOI=10.1093/oxfordjournals.jbchem.a123202;
RA Maruyama K.;
RT "Activation of Pseudomonas ochraceae 4-hydroxy-4-methyl-2-oxoglutarate
RT aldolase by inorganic phosphate.";
RL J. Biochem. 108:334-340(1990).
RN [4]
RP ACTIVITY REGULATION.
RX PubMed=1794988; DOI=10.1093/oxfordjournals.jbchem.a123699;
RA Maruyama K.;
RT "Chemical modification of Pseudomonas ochraceae 4-hydroxy-4-methyl-2-
RT oxoglutarate aldolase by diethyl pyrocarbonate.";
RL J. Biochem. 110:976-981(1991).
CC -!- FUNCTION: Catalyzes the last step of the bacterial protocatechuate 4,5-
CC cleavage pathway. Has a broad substrate specificity and catalyzes the
CC aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate, 4-hydroxy-2-
CC oxoglutarate and 4-carboxy-4-hydroxy-2-oxoadipate, and the
CC decarboxylation of oxaloacetate. Preferentially cleaves the L-isomer of
CC 4-carboxy-4-hydroxy-2-oxoadipate, and has lower activity towards 4-
CC hydroxy-4-methyl-2-oxoglutarate and 4-Hydroxy-2-oxoglutarate. Does not
CC cleave 4-hydroxy-2-oxovalerate, citrate, 4-hydroxy-2-oxobutyrate, 2-
CC oxoglutarate or fructose-1,6-bisphosphate.
CC {ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4S)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC Xref=Rhea:RHEA:35639, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:71685; EC=4.1.3.16;
CC Evidence={ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC Xref=Rhea:RHEA:30687, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:62213; EC=4.1.3.16;
CC Evidence={ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032};
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:11826967,
CC ECO:0000269|PubMed:2229032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate +
CC pyruvate; Xref=Rhea:RHEA:28935, ChEBI:CHEBI:15361, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:58075; EC=4.1.3.17;
CC Evidence={ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032};
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:2229032};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032};
CC Note=Divalent metal cations. Probably Mg(2+).
CC {ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032};
CC -!- ACTIVITY REGULATION: Cleavage of 4-carboxy-4-hydroxy-2-oxoadipate, and
CC to a lesser extent 4-hydroxy-4-methyl-2-oxoglutarate, is inhibited by
CC lysine modification caused by diethyl pyrocarbonate. Decarboxylation of
CC oxaloacetate is unaffected by diethyl pyrocarbonate. Inhibited by
CC BeCl(2), CaCl(2), NiCl(2), BaCl(2), HgCl(2), SrSO(4), CrCl(3) and
CC FeCl(3). Partially inhibited by p-chloromercuribenzoate and N-
CC ethylmaleimide. Activated by inorganic phosphate, arsenate, phosphorous
CC acid, acetyl phosphate, thiamine diphosphate, ADP, ATP and diphosphate.
CC {ECO:0000269|PubMed:1794988, ECO:0000269|PubMed:2229032,
CC ECO:0000269|PubMed:2229033}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.044 mM for DL-4-carboxy-4-hydroxy-2-oxoadipate
CC {ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
CC ECO:0000269|PubMed:2229033};
CC KM=0.019 mM for L-4-carboxy-4-hydroxy-2-oxoadipate
CC {ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
CC ECO:0000269|PubMed:2229033};
CC KM=0.15 mM for D-4-carboxy-4-hydroxy-2-oxoadipate
CC {ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
CC ECO:0000269|PubMed:2229033};
CC KM=1.25 mM for DL-4-hydroxy-4-methyl-2-oxoglutarate
CC {ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
CC ECO:0000269|PubMed:2229033};
CC KM=0.24 mM for DL-4-hydroxy-2-oxoglutarate
CC {ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
CC ECO:0000269|PubMed:2229033};
CC KM=0.50 mM for oxaloacetate {ECO:0000269|PubMed:11826967,
CC ECO:0000269|PubMed:2229032, ECO:0000269|PubMed:2229033};
CC Vmax=1250 umol/min/mg enzyme with DL-4-carboxy-4-hydroxy-2-oxoadipate
CC as substrate {ECO:0000269|PubMed:11826967,
CC ECO:0000269|PubMed:2229032, ECO:0000269|PubMed:2229033};
CC Vmax=1220 umol/min/mg enzyme with L-4-carboxy-4-hydroxy-2-oxoadipate
CC as substrate {ECO:0000269|PubMed:11826967,
CC ECO:0000269|PubMed:2229032, ECO:0000269|PubMed:2229033};
CC Vmax=67.6 umol/min/mg enzyme with D-4-carboxy-4-hydroxy-2-oxoadipate
CC as substrate {ECO:0000269|PubMed:11826967,
CC ECO:0000269|PubMed:2229032, ECO:0000269|PubMed:2229033};
CC Vmax=213 umol/min/mg enzyme with DL-4-hydroxy-4-methyl-2-oxoglutarate
CC as substrate {ECO:0000269|PubMed:11826967,
CC ECO:0000269|PubMed:2229032, ECO:0000269|PubMed:2229033};
CC Vmax=1.3 umol/min/mg enzyme with DL-4-hydroxy-2-oxoglutarate as
CC substrate {ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
CC ECO:0000269|PubMed:2229033};
CC Vmax=20.8 umol/min/mg enzyme with oxaloacetate as substrate
CC {ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
CC ECO:0000269|PubMed:2229033};
CC pH dependence:
CC Optimum pH varies depending on the substrate used and phosphate
CC concentration. In the absence of inorganic phosphate pH optima are
CC 6.6 for L-4-carboxy-4-hydroxy-2-oxoadipate, 8.0 for D-4-carboxy-4-
CC hydroxy-2-oxoadipate, 6.7 and 8.0 for DL-4-carboxy-4-hydroxy-2-
CC oxoadipate, 8.3 for DL-4-hydroxy-4-methyl-2-oxoglutarate, 9.3 for DL-
CC 4-hydroxy-2-oxoglutarate and 8.8 for oxaloacetate. In the presence of
CC 3 mM inorganic phosphate pH optima are more alkaline: 8.2 for L-4-
CC carboxy-4-hydroxy-2-oxoadipate, 8.6 for D-4-carboxy-4-hydroxy-2-
CC oxoadipate, 8.2 for DL-4-carboxy-4-hydroxy-2-oxoadipate, 8.9 for DL-
CC 4-hydroxy-4-methyl-2-oxoglutarate, 9.4 for DL-4-hydroxy-2-
CC oxoglutarate and 8.9 for oxaloacetate. Stable at pH 6.0 to pH 9.5.
CC {ECO:0000269|PubMed:11826967, ECO:0000269|PubMed:2229032,
CC ECO:0000269|PubMed:2229033};
CC Temperature dependence:
CC Retains 50% of maximum activity after incubation at 54 degrees
CC Celsius for 10 minutes. {ECO:0000269|PubMed:11826967,
CC ECO:0000269|PubMed:2229032, ECO:0000269|PubMed:2229033};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:2229032}.
CC -!- INDUCTION: By growth on aromatic carboxylates such as phthalate,
CC terephthalate, m-hydroxybenzoate and p-hydroxybenzoate.
CC {ECO:0000269|PubMed:2229032}.
CC -!- SIMILARITY: Belongs to the LigK/PcmE family. {ECO:0000305}.
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DR EMBL; AB050935; BAB21456.3; -; Genomic_DNA.
DR AlphaFoldDB; Q9AQI0; -.
DR SMR; Q9AQI0; -.
DR BioCyc; MetaCyc:MON-3244; -.
DR GO; GO:0106009; F:(4S)-4-hydroxy-2-oxoglutarate aldolase activity; IEA:RHEA.
DR GO; GO:0008700; F:4-hydroxy-2-oxoglutarate aldolase activity; IDA:UniProtKB.
DR GO; GO:0047443; F:4-hydroxy-4-methyl-2-oxoglutarate aldolase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IDA:UniProtKB.
DR CDD; cd16841; RraA_family; 1.
DR InterPro; IPR014165; LigK_PcmE.
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; TIGR02798; ligK_PcmE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..227
FT /note="4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-
FT carboxy-4-hydroxy-2-oxoadipate aldolase"
FT /id="PRO_0000403973"
FT BINDING 97..100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A5W059"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A5W059"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A5W059"
SQ 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
