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Q9AQI0

- HMGA_PSEOC

UniProt

Q9AQI0 - HMGA_PSEOC

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
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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

    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.

    Q9AQI0-1 [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: 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