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Q9AQI0 (HMGA_PSEOC) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
4-hydroxy-4-methyl-2-oxoglutarate aldolase
Alternative name(s):
4-hydroxy-2-oxoglutarate aldolase
EC=4.1.1.3
EC=4.1.3.-
EC=4.1.3.16
EC=4.1.3.17
Gene names
Name:proA
OrganismPseudomonas straminea
Taxonomic identifier47882 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in protocatechuate degradation. 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. Ref.1 Ref.2

Catalytic activity

4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate. Ref.1 Ref.2

2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate. Ref.1 Ref.2

4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate. Ref.1 Ref.2

Oxaloacetate = pyruvate + CO2. Ref.1 Ref.2

Cofactor

Divalent metal cations. Probably Mg2+. Ref.1 Ref.2

Enzyme 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 BeCl2, CaCl2, NiCl2, BaCl2, HgCl2, SrSO4, CrCl3 and FeCl3. Partially inhibited by p-chloromercuribenzoate and N-ethylmaleimide. Activated by inorganic phosphate, arsenate, phosphorous acid, acetyl phosphate, thiamine diphosphate, ADP, ATP and diphosphate. Ref.2 Ref.3 Ref.4

Subunit structure

Homohexamer. Ref.2

Induction

By growth on aromatic carboxylates such as phthalate, terephthalate, m-hydroxybenzoate and p-hydroxybenzoate. Ref.2 Ref.3 Ref.4

Sequence similarities

Belongs to the LigK/PcmE family.

Biophysicochemical properties

Kinetic parameters:

KM=0.044 mM for DL-4-carboxy-4-hydroxy-2-oxoadipate Ref.1 Ref.2 Ref.3

KM=0.019 mM for L-4-carboxy-4-hydroxy-2-oxoadipate Ref.1

KM=0.15 mM for D-4-carboxy-4-hydroxy-2-oxoadipate Ref.1

KM=1.25 mM for DL-4-hydroxy-4-methyl-2-oxoglutarate Ref.1

KM=0.24 mM for DL-4-hydroxy-2-oxoglutarate Ref.1

KM=0.50 mM for oxaloacetate Ref.1

Vmax=1250 µmol/min/mg enzyme with DL-4-carboxy-4-hydroxy-2-oxoadipate as substrate Ref.1

Vmax=1220 µmol/min/mg enzyme with L-4-carboxy-4-hydroxy-2-oxoadipate as substrate

Vmax=67.6 µmol/min/mg enzyme with D-4-carboxy-4-hydroxy-2-oxoadipate as substrate

Vmax=213 µmol/min/mg enzyme with DL-4-hydroxy-4-methyl-2-oxoglutarate as substrate Ref.1

Vmax=1.3 µmol/min/mg enzyme with DL-4-hydroxy-2-oxoglutarate as substrate Ref.1

Vmax=20.8 µmol/min/mg enzyme with oxaloacetate as substrate

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. Ref.3

Temperature dependence:

Retains 50% of maximum activity after incubation at 54 degrees Celsius for 10 minutes. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2272274-hydroxy-4-methyl-2-oxoglutarate aldolase
PRO_0000403973

Regions

Region99 – 1002Substrate binding By similarity

Sites

Metal binding1201Magnesium By similarity
Binding site1191Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9AQI0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F56501D5BDD0262F

FASTA22724,068
        10         20         30         40         50         60 
MYELGVVYRN IQRADRAAAD GLAALGSATV HEAMGRVGLL KPYMRPIYAG KQVSGTAVTV 

        70         80         90        100        110        120 
LLQPGDNWMM HVAAEQIQPG DIVVAAVTAE CTDGYFGDLL ATSFQARGAR ALIIDAGVRD 

       130        140        150        160        170        180 
VKTLQEMDFP VWSKAISSKG TIKATLGSVN IPIVCAGMLV TPGDVIVADD DGVVCVPAAR 

       190        200        210        220 
AVEVLAAAQK RESFEGEKRA KLASGVLGLD MYKMREPLEK AGLKYID 

« Hide

References

[1]"Cloning, sequencing, and expression of the gene encoding 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae NGJ1."
Maruyama K., Miwa M., Tsujii N., Nagai T., Tomita N., Harada T., Sobajima H., Sugisaki H.
Biosci. Biotechnol. Biochem. 65:2701-2709(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-22, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: NGJ1.
[2]"Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae grown on phthalate."
Maruyama K.
J. Biochem. 108:327-333(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION.
[3]"Activation of Pseudomonas ochraceae 4-hydroxy-4-methyl-2-oxoglutarate aldolase by inorganic phosphate."
Maruyama K.
J. Biochem. 108:334-340(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]"Chemical modification of Pseudomonas ochraceae 4-hydroxy-4-methyl-2-oxoglutarate aldolase by diethyl pyrocarbonate."
Maruyama K.
J. Biochem. 110:976-981(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB050935 Genomic DNA. Translation: BAB21456.3.

3D structure databases

ProteinModelPortalQ9AQI0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3244.
RETL1328306-WGS:GSTH-4402-MONOMER.
RETL1328306-WGS:GSTH-4408-MONOMER.

Family and domain databases

Gene3D3.50.30.40. 1 hit.
InterProIPR014165. LigK_PcmE.
IPR005493. RNase_E_inh/diMeMenaQ_MeTrfase.
[Graphical view]
PfamPF03737. Methyltransf_6. 1 hit.
[Graphical view]
SUPFAMSSF89562. SSF89562. 1 hit.
TIGRFAMsTIGR02798. ligK_PcmE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHMGA_PSEOC
AccessionPrimary (citable) accession number: Q9AQI0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families