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

Cofactori

Mg2+2 PublicationsNote: 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
  1. Vmax=1250 µmol/min/mg enzyme with DL-4-carboxy-4-hydroxy-2-oxoadipate as substrate3 Publications
  2. Vmax=1220 µmol/min/mg enzyme with L-4-carboxy-4-hydroxy-2-oxoadipate as substrate3 Publications
  3. Vmax=67.6 µmol/min/mg enzyme with D-4-carboxy-4-hydroxy-2-oxoadipate as substrate3 Publications
  4. Vmax=213 µmol/min/mg enzyme with DL-4-hydroxy-4-methyl-2-oxoglutarate as substrate3 Publications
  5. Vmax=1.3 µmol/min/mg enzyme with DL-4-hydroxy-2-oxoglutarate as substrate3 Publications
  6. 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)DescriptionActionsGraphical viewLength
Binding sitei119SubstrateBy similarity1
Metal bindingi120MagnesiumBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • 3,4-dihydroxybenzoate catabolic process Source: UniProtKB

Keywordsi

Molecular functionLyase
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3244.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase (EC:4.1.3.162 Publications, EC:4.1.3.172 Publications)
Short name:
HMG/CHA aldolase
Alternative name(s):
4-hydroxy-2-oxoglutarate aldolase
Oxaloacetate decarboxylase (EC:4.1.1.31 Publication)
Short name:
OAA decarboxylase
Gene namesi
Name:proAImported
OrganismiPseudomonas straminea
Taxonomic identifieri47882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004039731 – 2274-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolaseAdd BLAST227

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.
SMRiQ9AQI0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni97 – 100Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the LigK/PcmE family.Curated

Family and domain databases

CDDicd16841. RraA_family. 1 hit.
Gene3Di3.50.30.40. 1 hit.
InterProiView protein in InterPro
IPR014165. LigK_PcmE.
IPR005493. RraA/RraA-like.
PfamiView protein in Pfam
PF03737. RraA-like. 1 hit.
SUPFAMiSSF89562. SSF89562. 1 hit.
TIGRFAMsiTIGR02798. ligK_PcmE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9AQI0-1 [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:
EMBLi
GenBanki
DDBJi
Links Updated
AB050935 Genomic DNA. Translation: BAB21456.3.

Similar proteinsi

Entry informationi

Entry nameiHMGA_PSEOC
AccessioniPrimary (citable) accession number: Q9AQI0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: June 1, 2001
Last modified: August 30, 2017
This is version 49 of the entry and version 1 of the sequence. See 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