Strain |
Pseudomonas aeruginosa PAO1 (Stover et al., 2000)
GCF_000006765.1|latest |
Locus Tag |
PA4872
|
Name |
|
Replicon | chromosome |
Genomic location | 5469115 - 5469978 (- strand) |
Transposon Mutants | 2 transposon mutants in PAO1 |
Transposon Mutants in orthologs | 2 transposon mutants in orthologs |
RefSeq | NP_253559.1 |
GI | 15600065 |
Affymetrix | PA4872_at |
Entrez | 878100 |
GenBank | AAG08257.1 |
INSDC | AAG08257.1 |
NCBI Locus Tag | PA4872 |
protein_id(GenBank) | gb|AAG08257.1|AE004900_11|gnl|PseudoCAP|PA4872 |
TIGR | NTL03PA04873 |
UniParc | UPI00000C5E4E |
UniProtKB Acc | Q9HUU1 |
UniProtKB ID | OADC_PSEAE |
UniRef100 | UniRef100_B7V1T5 |
UniRef50 | UniRef50_A6VCY0 |
UniRef90 | UniRef90_A6VCY0 |
Feature Type | CDS |
Coding Frame | 1 |
Product Name |
oxaloacetate decarboxylase
|
Synonyms | |
Evidence for Translation |
Identified using nanoflow high-pressure liquid chromatography (HPLC) in conjunction with microelectrospray ionization on LTQ XL mass spectrometer (PMID:24291602).
|
Charge (pH 7) | -7.98 |
Kyte-Doolittle Hydrophobicity Value | 0.121 |
Molecular Weight (kDa) | 31.3 |
Isoelectric Point (pI) | 5.38 |
Individual Mappings | |
Additional evidence for subcellular localization |
Accession | Header | Accession Date | Compound | Source | Resolution | Method | Percent Identity |
3B8I | LYASE | 11/01/07 | Crystal Structure of Oxaloacetate Decarboxylase from Pseudomonas Aeruginosa (PA4872) in complex with oxalate and Mg2+. | Pseudomonas aeruginosa | 1.9 | X-RAY DIFFRACTION | 100.0 |
Results |
Common
Found in both pathogen and nonpathogenic strains
Hits to this gene were found in 265 genera
|
Pseudomonas Ortholog Database | View orthologs at Pseudomonas Ortholog Database |
Pseudomonas Ortholog Group |
POG004500 (519 members) |
Putative Inparalogs | None Found |
STRING database | Search for predicted protein-protein interactions using:
Search term: PA4872
Search term: oxaloacetate decarboxylase
|
Structure and function of PA4872 from Pseudomonas aeruginosa, a novel class of oxaloacetate decarboxylase from the PEP mutase/isocitrate lyase superfamily.
Narayanan BC, Niu W, Han Y, Zou J, Mariano PS, Dunaway-Mariano D, Herzberg O
Biochemistry 2008 Jan 8;47(1):167-82
PubMed ID: 18081320
|