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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.2 Publications

Catalytic activityi

4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate.2 Publications
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate.
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-oxoadipate3 Publications
  3. KM=0.15 mM for D-4-carboxy-4-hydroxy-2-oxoadipate3 Publications
  4. KM=1.25 mM for DL-4-hydroxy-4-methyl-2-oxoglutarate3 Publications
  5. KM=0.24 mM for DL-4-hydroxy-2-oxoglutarate3 Publications
  6. KM=0.50 mM for oxaloacetate3 Publications

Vmax=1250 µmol/min/mg enzyme with DL-4-carboxy-4-hydroxy-2-oxoadipate as substrate3 Publications

Vmax=1220 µmol/min/mg enzyme with L-4-carboxy-4-hydroxy-2-oxoadipate as substrate3 Publications

Vmax=67.6 µmol/min/mg enzyme with D-4-carboxy-4-hydroxy-2-oxoadipate as substrate3 Publications

Vmax=213 µmol/min/mg enzyme with DL-4-hydroxy-4-methyl-2-oxoglutarate as substrate3 Publications

Vmax=1.3 µmol/min/mg enzyme with DL-4-hydroxy-2-oxoglutarate as substrate3 Publications

Vmax=20.8 µmol/min/mg enzyme with oxaloacetate as substrate3 Publications

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 9.5.3 Publications

Temperature dependencei

Retains 50% of maximum activity after incubation at 54 degrees Celsius for 10 minutes.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei119 – 1191SubstrateBy similarity
Metal bindingi120 – 1201MagnesiumBy 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:proAImported
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.1 Publication

Interactioni

Subunit structurei

Homohexamer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9AQI0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the LigK/PcmE family.Curated

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYELGVVYRN IQRADRAAAD GLAALGSATV HEAMGRVGLL KPYMRPIYAG
60 70 80 90 100
KQVSGTAVTV LLQPGDNWMM HVAAEQIQPG DIVVAAVTAE CTDGYFGDLL
110 120 130 140 150
ATSFQARGAR ALIIDAGVRD VKTLQEMDFP VWSKAISSKG TIKATLGSVN
160 170 180 190 200
IPIVCAGMLV TPGDVIVADD DGVVCVPAAR AVEVLAAAQK RESFEGEKRA
210 220
KLASGVLGLD MYKMREPLEK AGLKYID
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: NGJ1Imported.
  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: October 1, 2014
This is version 40 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