HMGA_PSEP1
ID HMGA_PSEP1 Reviewed; 238 AA.
AC A5W059;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase;
DE Short=HMG/CHA aldolase;
DE EC=4.1.3.17 {ECO:0000269|PubMed:20843800};
DE AltName: Full=Oxaloacetate decarboxylase;
DE Short=OAA decarboxylase;
DE EC=4.1.1.112 {ECO:0000269|PubMed:20843800};
GN OrderedLocusNames=Pput_1361;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP PYRUVATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND MUTAGENESIS
RP OF ARG-123.
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RX PubMed=20843800; DOI=10.1074/jbc.m110.159509;
RA Wang W., Mazurkewich S., Kimber M.S., Seah S.Y.;
RT "Structural and kinetic characterization of 4-hydroxy-4-methyl-2-
RT oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase, a protocatechuate
RT degradation enzyme evolutionarily convergent with the HpaI and DmpG
RT pyruvate aldolases.";
RL J. Biol. Chem. 285:36608-36615(2010).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
CC -!- FUNCTION: Catalyzes the last step of the bacterial protocatechuate 4,5-
CC cleavage pathway. The preferred substrates of the enzyme are 2-keto-4-
CC hydroxy acids with a 4-carboxylate substitution. Catalyzes the
CC conversion of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) to pyruvate. Also
CC catalyzes the conversion of 4-carboxy-4-hydroxy-2-oxoadipic acid (CHA)
CC to pyruvate and oxaloacetate. {ECO:0000269|PubMed:20843800,
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:20843800,
CC ECO:0000269|PubMed:24359411};
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:20843800};
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:20843800};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20843800};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 mM for oxaloacetate (in presence of 1 mM of magnesium)
CC {ECO:0000269|PubMed:20843800};
CC KM=0.036 mM for oxaloacetate (in presence of 1 mM of manganese)
CC {ECO:0000269|PubMed:20843800};
CC KM=0.26 mM for 4-hydroxy-4-methyl-2-oxoglutarate (in presence of 1 mM
CC of magnesium) {ECO:0000269|PubMed:20843800};
CC KM=0.022 mM for 4-hydroxy-4-methyl-2-oxoglutarate (in presence of 1
CC mM of manganese) {ECO:0000269|PubMed:20843800};
CC KM=0.066 mM for 4-carboxy-4-hydroxy-2-oxoadipic acid or 2-hydroxy-4-
CC oxobutane-1,2,4-tricarboxylic (in presence of 1 mM of magnesium)
CC {ECO:0000269|PubMed:20843800};
CC KM=0.030 mM for 4-carboxy-4-hydroxy-2-oxoadipic acid or 2-hydroxy-4-
CC oxobutane-1,2,4-tricarboxylic (in presence of 1 mM of manganese)
CC {ECO:0000269|PubMed:20843800};
CC KM=0.15 mM for alpha-keto-gamma-hydroxyglutarate (in presence of 1 mM
CC of magnesium) {ECO:0000269|PubMed:20843800};
CC KM=0.071 mM for alpha-keto-gamma-hydroxyglutarate (in presence of 1
CC mM of manganese) {ECO:0000269|PubMed:20843800};
CC KM=25 mM for 4-hydroxy-2-oxopentanoate (in presence of 1 mM of
CC magnesium) {ECO:0000269|PubMed:20843800};
CC KM=8.8 mM for 4-hydroxy-2-oxopentanoate (in presence of 1 mM of
CC manganese) {ECO:0000269|PubMed:20843800};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:20843800}.
CC -!- SIMILARITY: Belongs to the LigK/PcmE family. {ECO:0000305}.
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DR EMBL; CP000712; ABQ77519.1; -; Genomic_DNA.
DR RefSeq; WP_012051536.1; NC_009512.1.
DR PDB; 3NOJ; X-ray; 1.82 A; A=1-238.
DR PDBsum; 3NOJ; -.
DR AlphaFoldDB; A5W059; -.
DR SMR; A5W059; -.
DR STRING; 351746.Pput_1361; -.
DR EnsemblBacteria; ABQ77519; ABQ77519; Pput_1361.
DR KEGG; ppf:Pput_1361; -.
DR eggNOG; COG0684; Bacteria.
DR HOGENOM; CLU_072626_3_2_6; -.
DR OMA; KFHSIVE; -.
DR OrthoDB; 1614890at2; -.
DR BRENDA; 4.1.3.17; 5092.
DR BRENDA; 4.1.3.B3; 5092.
DR SABIO-RK; A5W059; -.
DR EvolutionaryTrace; A5W059; -.
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 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 3D-structure; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..238
FT /note="4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-
FT carboxy-4-hydroxy-2-oxoadipate aldolase"
FT /id="PRO_0000418488"
FT BINDING 101..104
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20843800,
FT ECO:0007744|PDB:3NOJ"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20843800,
FT ECO:0007744|PDB:3NOJ"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20843800"
FT MUTAGEN 123
FT /note="R->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:20843800"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:3NOJ"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:3NOJ"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:3NOJ"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:3NOJ"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:3NOJ"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:3NOJ"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:3NOJ"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:3NOJ"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:3NOJ"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:3NOJ"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:3NOJ"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:3NOJ"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:3NOJ"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3NOJ"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3NOJ"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:3NOJ"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3NOJ"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3NOJ"
FT HELIX 185..208
FT /evidence="ECO:0007829|PDB:3NOJ"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:3NOJ"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:3NOJ"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:3NOJ"
SQ 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
