Strain |
Pseudomonas aeruginosa PAO1 (Stover et al., 2000)
GCF_000006765.1|latest |
Locus Tag |
PA1587
|
Name |
lpd
Synonym: lpdA |
Replicon | chromosome |
Genomic location | 1728416 - 1729852 (+ strand) |
RefSeq | NP_250278.1 |
GI | 15596784 |
Affymetrix | PA1587_lpdG_at |
Entrez | 882090 |
GenBank | AAG04976.1 |
INSDC | AAG04976.1 |
NCBI Locus Tag | PA1587 |
protein_id(GenBank) | gb|AAG04976.1|AE004586_14|gnl|PseudoCAP|PA1587 |
TIGR | NTL03PA01588 |
UniParc | UPI00000C53F6 |
UniProtKB Acc | Q9I3D1 |
UniProtKB ID | DLDH2_PSEAE |
UniRef100 | UniRef100_Q9I3D1 |
UniRef50 | UniRef50_P14218 |
UniRef90 | UniRef90_P14218 |
Feature Type | CDS |
Coding Frame | 1 |
Product Name |
dihydrolipoamide dehydrogenase Lpd
|
Synonyms |
LPD-GLC, L-factor for glycine oxidation system dihydrolipoamide dehydrogenase (E3 subunit) |
Evidence for Translation |
Identified using nanoflow high-pressure liquid chromatography (HPLC) in conjunction with microelectrospray ionization on LTQ XL mass spectrometer (PMID:24291602).
Detected by MALDI-TOF/TOF (PMID:19333994).
Detected using LC-MS/MS (50.16 kDa, PMID:21751344)
|
Charge (pH 7) | -0.22 |
Kyte-Doolittle Hydrophobicity Value | 0.135 |
Molecular Weight (kDa) | 50.2 |
Isoelectric Point (pI) | 6.96 |
Individual Mappings | |
Additional evidence for subcellular localization |
Accession | Header | Accession Date | Compound | Source | Resolution | Method | Percent Identity |
5U8V | OXIDOREDUCTASE | 12/15/16 | Dihydrolipoamide dehydrogenase (LpdG) from Pseudomonas aeruginosa bound to NAD+ | Pseudomonas aeruginosa (strain UCBPP-PA14) | 1.45 | X-RAY DIFFRACTION | 100.0 |
5U8W | OXIDOREDUCTASE | 12/15/16 | Dihydrolipoamide dehydrogenase (LpdG) from Pseudomonas aeruginosa bound to NADH | Pseudomonas aeruginosa (strain UCBPP-PA14) | 1.79 | X-RAY DIFFRACTION | 100.0 |
5U8U | OXIDOREDUCTASE | 12/15/16 | Dihydrolipoamide dehydrogenase (LpdG) from Pseudomonas aeruginosa | Pseudomonas aeruginosa (strain UCBPP-PA14) | 1.35 | X-RAY DIFFRACTION | 100.0 |
1LPF | OXIDOREDUCTASE | 10/26/92 | THREE-DIMENSIONAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM PSEUDOMONAS FLUORESCENS AT 2.8 ANGSTROMS RESOLUTION. ANALYSIS OF REDOX AND THERMOSTABILITY PROPERTIES | Pseudomonas fluorescens | 2.8 | X-RAY DIFFRACTION | 99.8 |
Identified by Diamond using e-value cutoff of 0.0001 and returning alignments that span 100% of the query sequence and that have more than 95% identity.
Drug Name | Source Accession | Source DB | Version | Target Accession | Target Description | Percent Identity | Alignment Length | E-Value |
Flavin adenine dinucleotide | DB03147 | DrugBank | 5.1.4 | P14218 | Dihydrolipoyl dehydrogenase | 99.8 | 478 | 1.6e-265 |
Source 1 | |
Database | PseudoCAP |
Category | dihydrolipoamide dehydrogenase |
Evidence |
ECO:0000314
direct assay evidence used in manual assertion
|
Host Organism | Homo sapiens |
Notes | |
Infection model | Serum bactericidal assay |
Reference | 23071278 |
Results |
Common
Found in both pathogen and nonpathogenic strains
Hits to this gene were found in 650 genera
|
Pseudomonas Ortholog Database | View orthologs at Pseudomonas Ortholog Database |
Pseudomonas Ortholog Group |
POG003776 (538 members) |
Putative Inparalogs | None Found |
STRING database | Search for predicted protein-protein interactions using:
Search term: PA1587
Search term: lpd
Search term: dihydrolipoamide dehydrogenase Lpd
|
Ensembl
110, assembly
GRCh38.p14
|
dihydrolipoamide dehydrogenase [Source:HGNC Symbol;Acc:HGNC:2898]
E-value:
1.1e-120
Percent Identity:
49.8
|
Ensembl
110, assembly
GRCh38.p14
|
dihydrolipoamide dehydrogenase [Source:HGNC Symbol;Acc:HGNC:2898]
E-value:
1.1e-120
Percent Identity:
49.8
|
Sequence analysis of the lpdV gene for lipoamide dehydrogenase of branched-chain-oxoacid dehydrogenase of Pseudomonas putida.
Burns G, Brown T, Hatter K, Sokatch JR
Eur J Biochem 1989 Jan 15;179(1):61-9
PubMed ID: 2917566
|
Cloning and sequence analysis of the LPD-glc structural gene of Pseudomonas putida.
Palmer JA, Hatter K, Sokatch JR
J Bacteriol 1991 May;173(10):3109-16
PubMed ID: 1902462
|
Analysis of the periplasmic proteome of Pseudomonas aeruginosa, a metabolically versatile opportunistic pathogen.
Imperi F, Ciccosanti F, Perdomo AB, Tiburzi F, Mancone C, Alonzi T, Ascenzi P, Piacentini M, Visca P, Fimia GM
Proteomics 2009 Apr;9(7):1901-15
PubMed ID: 19333994
|
Proteomic analysis of outer membrane vesicles derived from Pseudomonas aeruginosa.
Choi DS, Kim DK, Choi SJ, Lee J, Choi JP, Rho S, Park SH, Kim YK, Hwang D, Gho YS
Proteomics 2011 Aug;11(16):3424-9
PubMed ID: 21751344
|
Dihydrolipoamide dehydrogenase of Pseudomonas aeruginosa is a surface-exposed immune evasion protein that binds three members of the factor H family and plasminogen.
Hallström T, Mörgelin M, Barthel D, Raguse M, Kunert A, Hoffmann R, Skerka C, Zipfel PF
J Immunol 2012 Nov 15;189(10):4939-50
PubMed ID: 23071278
|