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Protein

Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase

Gene

PA1772

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions (By similarity).By similarity

Catalytic activityi

4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate.
Oxaloacetate = pyruvate + CO2.

Cofactori

a divalent metal cationBy similarityNote: Divalent metal cation.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei97SubstrateBy similarity1
Metal bindingi98Divalent metal cationBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
LigandMetal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase (EC:4.1.3.17)
Short name:
HMG aldolase
Alternative name(s):
Oxaloacetate decarboxylase (EC:4.1.1.3)
Short name:
OAA decarboxylase
Regulator of ribonuclease activity homolog
RraA-like protein
Gene namesi
Ordered Locus Names:PA1772
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA1772.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002096291 – 162Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolaseAdd BLAST162

Proteomic databases

PaxDbiQ9I2W7.
PRIDEiQ9I2W7.

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

STRINGi208964.PA1772.

Structurei

Secondary structure

1162
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 11Combined sources7
Turni13 – 15Combined sources3
Beta strandi32 – 40Combined sources9
Helixi46 – 52Combined sources7
Beta strandi59 – 64Combined sources6
Beta strandi69 – 73Combined sources5
Helixi76 – 84Combined sources9
Beta strandi89 – 96Combined sources8
Helixi99 – 102Combined sources4
Beta strandi105 – 114Combined sources10
Beta strandi126 – 128Combined sources3
Beta strandi131 – 133Combined sources3
Beta strandi136 – 138Combined sources3
Beta strandi142 – 146Combined sources5
Beta strandi151 – 156Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C8OX-ray1.90A/B1-162[»]
ProteinModelPortaliQ9I2W7.
SMRiQ9I2W7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9I2W7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni75 – 78Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the class II aldolase/RraA-like family.Curated

Phylogenomic databases

eggNOGiENOG4108YYX. Bacteria.
COG0684. LUCA.
HOGENOMiHOG000252803.
InParanoidiQ9I2W7.
KOiK02553.
OMAiRSCDTQF.
PhylomeDBiQ9I2W7.

Family and domain databases

CDDicd16841. RraA_family. 1 hit.
Gene3Di3.50.30.40. 1 hit.
InterProiView protein in InterPro
IPR010203. RraA.
IPR005493. RraA/RraA-like.
PfamiView protein in Pfam
PF03737. RraA-like. 1 hit.
SUPFAMiSSF89562. SSF89562. 1 hit.
TIGRFAMsiTIGR01935. NOT-MenG. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9I2W7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHYVTPDLCD AYPELVQVVE PMFSNFGGRD SFGGEIVTIK CFEDNSLVKE
60 70 80 90 100
QVDKDGKGKV LVVDGGGSLR RALLGDMLAE KAAKNGWEGI VVYGCIRDVD
110 120 130 140 150
VIAQTDLGVQ ALASHPLKTD KRGIGDLNVA VTFGGVTFRP GEFVYADNNG
160
IIVSPQALKM PE
Length:162
Mass (Da):17,404
Last modified:March 1, 2001 - v1
Checksum:i4F682F7A485DE1EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG05161.1.
PIRiB83423.
RefSeqiNP_250463.1. NC_002516.2.
WP_003087823.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG05161; AAG05161; PA1772.
GeneIDi880779.
KEGGipae:PA1772.
PATRICifig|208964.12.peg.1837.

Similar proteinsi

Entry informationi

Entry nameiRRAAH_PSEAE
AccessioniPrimary (citable) accession number: Q9I2W7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: March 1, 2001
Last modified: August 30, 2017
This is version 94 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families