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Q9AQI0

- HMGA_PSEOC

UniProt

Q9AQI0 - HMGA_PSEOC

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Protein

4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase

Gene
proA
Organism
Pseudomonas straminea
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate.2 Publications
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate.2 Publications
4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate.2 Publications
Oxaloacetate = pyruvate + CO2.2 Publications

Cofactori

Divalent metal cations. Probably Mg2+.2 Publications

Enzyme regulationi

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.3 Publications

Kineticsi

  1. KM=0.044 mM for DL-4-carboxy-4-hydroxy-2-oxoadipate3 Publications
  2. KM=0.019 mM for L-4-carboxy-4-hydroxy-2-oxoadipate1 Publication
  3. KM=0.15 mM for D-4-carboxy-4-hydroxy-2-oxoadipate1 Publication
  4. KM=1.25 mM for DL-4-hydroxy-4-methyl-2-oxoglutarate1 Publication
  5. KM=0.24 mM for DL-4-hydroxy-2-oxoglutarate1 Publication
  6. KM=0.50 mM for oxaloacetate1 Publication

Vmax=1250 µmol/min/mg enzyme with DL-4-carboxy-4-hydroxy-2-oxoadipate as substrate1 Publication

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 substrate1 Publication

Vmax=1.3 µmol/min/mg enzyme with DL-4-hydroxy-2-oxoglutarate as substrate1 Publication

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

pH dependencei

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 9.5.1 Publication

Temperature dependencei

Retains 50% of maximum activity after incubation at 54 degrees Celsius for 10 minutes.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei119 – 1191Substrate By similarity
Metal bindingi120 – 1201Magnesium By similarity

GO - Molecular functioni

  1. 4-hydroxy-2-oxoglutarate aldolase activity Source: UniProtKB
  2. 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. oxaloacetate decarboxylase activity Source: UniProtKB

GO - Biological processi

  1. protocatechuate catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase (EC:4.1.3.16, EC:4.1.3.17)
Short name:
HMG/CHA aldolase
Alternative name(s):
4-hydroxy-2-oxoglutarate aldolase
Oxaloacetate decarboxylase (EC:4.1.1.3)
Short name:
OAA decarboxylase
Gene namesi
Name:proA
OrganismiPseudomonas straminea
Taxonomic identifieri47882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2272274-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolasePRO_0000403973Add
BLAST

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Homohexamer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9AQI0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 1004Substrate binding By similarity

Sequence similaritiesi

Belongs to the LigK/PcmE family.

Family and domain databases

Gene3Di3.50.30.40. 1 hit.
InterProiIPR014165. LigK_PcmE.
IPR005493. RNase_E_inh/diMeMenaQ_MeTrfase.
[Graphical view]
PfamiPF03737. Methyltransf_6. 1 hit.
[Graphical view]
SUPFAMiSSF89562. SSF89562. 1 hit.
TIGRFAMsiTIGR02798. ligK_PcmE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9AQI0-1 [UniParc]FASTAAdd to Basket

« Hide

MYELGVVYRN IQRADRAAAD GLAALGSATV HEAMGRVGLL KPYMRPIYAG    50
KQVSGTAVTV LLQPGDNWMM HVAAEQIQPG DIVVAAVTAE CTDGYFGDLL 100
ATSFQARGAR ALIIDAGVRD VKTLQEMDFP VWSKAISSKG TIKATLGSVN 150
IPIVCAGMLV TPGDVIVADD DGVVCVPAAR AVEVLAAAQK RESFEGEKRA 200
KLASGVLGLD MYKMREPLEK AGLKYID 227
Length:227
Mass (Da):24,068
Last modified:June 1, 2001 - v1
Checksum:iF56501D5BDD0262F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB050935 Genomic DNA. Translation: BAB21456.3.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB050935 Genomic DNA. Translation: BAB21456.3 .

3D structure databases

ProteinModelPortali Q9AQI0.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-3244.
RETL1328306-WGS:GSTH-4402-MONOMER.
RETL1328306-WGS:GSTH-4408-MONOMER.

Family and domain databases

Gene3Di 3.50.30.40. 1 hit.
InterProi IPR014165. LigK_PcmE.
IPR005493. RNase_E_inh/diMeMenaQ_MeTrfase.
[Graphical view ]
Pfami PF03737. Methyltransf_6. 1 hit.
[Graphical view ]
SUPFAMi SSF89562. SSF89562. 1 hit.
TIGRFAMsi TIGR02798. ligK_PcmE. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiHMGA_PSEOC
AccessioniPrimary (citable) accession number: Q9AQI0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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