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UniProtKB/Swiss-Prot entry P14218

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DLDH_PSEFL
Primary accession number P14218
Secondary accession numbers None
Integrated into Swiss-Prot on January 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 84)
Name and origin of the protein
Protein name Dihydrolipoyl dehydrogenase
Synonyms EC 1.8.1.4
Dihydrolipoamide dehydrogenase
E3 component of 2-oxoglutarate dehydrogenase complex
Gene name
Name: lpd
From
Pseudomonas fluorescens [TaxID: 294] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-23.
PubMed=2515251 [NCBI, ExPASy, EBI, Israel, Japan]
Benen J.A.E., van Berkel W.J.H., van Dongen W.M.A.M., Mueller F., de Kok A.;
"Molecular cloning and sequence determination of the lpd gene encoding lipoamide dehydrogenase from Pseudomonas fluorescens.";
J. Gen. Microbiol. 135:1787-1797(1989).
[2]
 X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD, SUBUNIT, AND DISULFIDE BOND.
DOI=10.1006/jmbi.1993.1236; PubMed=8487301 [NCBI, ExPASy, EBI, Israel, Japan]
Mattevi A., Obmolova G., Kalk K.H., van Berkel W.J.H., Hol W.G.J.;
"Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas fluorescens at 2.8-A resolution. Analysis of redox and thermostability properties.";
J. Mol. Biol. 230:1200-1215(1993).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M28356; AAA99234.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1LPF; X-ray; 2.80 A; A/B=1-478.[ExPASy / RCSB / EBI]
PDBsum 1LPF; -.
ModBase P14218.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0004148; Molecular function: dihydrolipoyl dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000815; Hg_reductase.
IPR006258; Lipoamide_DHase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR003042; Rng_hydrolase.
Graphical view of domain structure.
Gene3D G3DSA:3.30.390.30; Pyr_redox_dim; 1.
PANTHER PTHR22912:SF20; Lipoamide_DH; 1.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.
PR00420; RNGMNOXGNASE.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01350; lipoamide_DH; 1.
PROSITE PS00076; PYRIDINE_REDOX_1; 1.
ProtoNet P14218.
Other
LinkHub P14218; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   478  477     Dihydrolipoyl dehydrogenase. PRO_0000068037
NP_BIND   34    49  16     FAD. 
NP_BIND   188   192  5     NAD (By similarity). 
NP_BIND   276   279  4     NAD (By similarity). 
ACT_SITE   451   451        Proton acceptor (By similarity). 
BINDING   58    58        FAD. 
BINDING   122   122        FAD; via amide nitrogen and carbonyl oxygen. 
BINDING   211   211        NAD (By similarity). 
BINDING   245   245        NAD; via amide nitrogen (By similarity). 
BINDING   319   319        FAD. 
BINDING   327   327        FAD; via amide nitrogen. 
DISULFID   49    54        Redox-active. 
STRAND   4    10  7      
HELIX   14    25  12      
STRAND   30    34  5      
STRAND   39    43  5      
HELIX   47    52  6      
HELIX   54    72  19      
HELIX   75    77  3      
STRAND   79    86  8      
HELIX   88   113  26      
STRAND   115   124  10      
HELIX   126   128  3      
STRAND   129   134  6      
STRAND   139   149  11      
STRAND   153   155  3      
TURN   165   167  3      
HELIX   171   174  4      
STRAND   182   187  6      
HELIX   191   202  12      
STRAND   206   210  5      
STRAND   212   217  6      
HELIX   222   235  14      
STRAND   238   240  3      
STRAND   244   247  4      
STRAND   254   260  7      
STRAND   265   271  7      
STRAND   273   275  3      
STRAND   279   281  3      
TURN   284   286  3      
STRAND   308   311  4      
STRAND   314   316  3      
HELIX   318   320  3      
STRAND   321   323  3      
HELIX   327   341  15      
HELIX   350   352  3      
STRAND   355   357  3      
STRAND   359   367  9      
HELIX   370   375  6      
STRAND   380   386  7      
HELIX   387   389  3      
HELIX   391   396  6      
STRAND   402   411  10      
STRAND   413   421  9      
HELIX   424   436  13      
HELIX   441   445  5      
HELIX   455   465  11      
Sequence information
Length: 478 AA [This is the length of the unprocessed precursor] Molecular weight: 50151 Da [This is the MW of the unprocessed precursor] CRC64: B23EB31268C69EC7 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSQKFDVVVI GAGPGGYVAA IRAAQLGLKT ACIEKYIGKE GKVALGGTCL NVGCIPSKAL 

        70         80         90        100        110        120 
LDSSYKYHEA KEAFKVHGIE AKGVTIDVPA MVARKANIVK NLTGGIATLF KANGVTSFEG 

       130        140        150        160        170        180 
HGKLLANKQV EVTGLDGKTQ VLEAENVIIA SGSRPVEIPP APLSDDIIVD STGALEFQAV 

       190        200        210        220        230        240 
PKKLGVIGAG VIGLELGSVW ARLGAEVTVL EALDKFLPAA DEQIAKEALK VLTKQGLNIR 

       250        260        270        280        290        300 
LGARVTASEV KKKQVTVTFT DANGEQKETF DKLIVAVGRR PVTTDLLAAD SGVTLDERGF 

       310        320        330        340        350        360 
IYVDDHCKTS VPGVFAIGDV VRGAMLAHKA SEEGVMVAER IAGHKAQMNY DLIPSVIYTH 

       370        380        390        400        410        420 
PEIAWVGKTE QTLKAEGVEV NVGTFPFAAS GRAMAANDTT GLVKVIADAK TDRVLGVHVI 

       430        440        450        460        470 
GPSAAELVQQ GAIGMEFGTS AEDLGMMVFS HPTLSEALHE AALAVNGHAI HIANRKKR
P14218 in FASTA format

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