MG1655
W3110
Search for
Japanese | English
Gene Report : lpd
PEC Original Annotations
Essentiality
     Class non-essential
     References (PMID)  
     Deletion OCR31 (D)  ,  OCR31-7 (D)  
Related gene (W3110 PEC)
     Gene Search Search MG1655 PEC by gene name:  lpd
Related strains
     Strains Search Search strains by gene name:  lpd   Search strains by all related name:  lpd b0116 dhl ECK0115 JW0112 lpdA

General information  (Go to Linear View:)
 Gene Name lpd  
 Alternative name b0116,dhl,ECK0115,JW0112,lpdA  
 Location, Length 127,912 - 129,336 (  +  ) ;   2.76 min ; 1425 (bp) ,   474 (aa) Go to Linear View
 Product lipoamide dehydrogenase, E3 component is part of three enzyme complexes  
 Operon Name pdhR-aceEF-lpd  
 Note lipoamide dehydrogenase (NADH); component of 2-oxodehydrogenase and pyruvate complexes; L-protein of glycine cleavage complex; GO_component: GO:0005737 - cytoplasm; GO_process: GO:0016052 - carbohydrate catabolic process; GO_process: GO:0009063 - cellular amino acid catabolic process; GO_process: GO:0006096 - glycolysis; GO_process: GO:0006086 - acetyl-CoA biosynthetic process from pyruvate; GO_process: GO:0006099 - tricarboxylic acid cycle; GO_process: GO:0009060 - aerobic respiration; GO_process: GO:0009061 - anaerobic respiration; GO_process: GO:0009436 - glyoxylate catabolic process  
 Function enzyme; Energy metabolism, carbon: Pyruvate dehydrogenase  
 Gene Ontology GO:0004148 ; dihydrolipoyl dehydrogenase activity ( lpdA )
GO:0005515 ; protein binding ( lpdA )
GO:0005624 ; membrane fraction ( lpdA )
GO:0005737 ; cytoplasm ( lpdA )
GO:0005886 ; plasma membrane ( lpdA )
GO:0006096 ; glycolysis ( lpdA )
GO:0006118 ; electron transport ( lpdA )
GO:0016020 ; membrane ( lpdA )
GO:0016491 ; oxidoreductase activity ( lpdA )
GO:0045454 ; cell redox homeostasis ( lpdA )
GO:0050660 ; FAD binding ( lpdA )
 PID 1786307  
 EC number
  (KEGG Pathway)
 
1.8.1.4  
SWISS-PROT  ( Show details )
  botton Entry name(Acc.no) DLDH_ECOLI ( P00391 )
    -  Protein name Dihydrolipoyl dehydrogenase  
    -  Synonyms EC 1.8.1.4, E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes, Dihydrolipoamide dehydrogenase, Glycine cleavage system L protein  
    -  Gene name OrderedLocusNames=b0116, c0145, z0126, ECs0120, SF0113, S0115;  

 Linear View (Whole Mode)
View Location
   117.912  –  142.912 (KBP)

Homology Analysis
BLAST
    Bacteria
         GTOP lpd (  homologous genes of other bacterias  )  
    PDB     (database updated : 2007.02.20 )
         PSI-BLAST Chain A, Dihydrolipoamide Dehydrogenase (E.C.1.8.1.4) Complex With Flavin-Adenine-Dinucleotide (Fad)  
    SWISS-PROT     (database updated : 2007.02.20 )
         BLAST Dihydrolipoyl dehydrogenase (E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes) (Dihydrolipoamide dehydrogenase) (Glycine cleavage system L protein)  
         PSI-BLAST tRNA uridine 5-carboxymethylaminomethyl modification enzyme gidA
    nr     (database updated : 2007.02.20 )
         BLAST dihydrolipoamide dehydrogenase [Shigella flexneri 5 str. 8401]  
Pfam 28.0   (database updated : 2015-05 )
    Pfam
PROSITE
    PROSITE CAMP_PHOSPHO_SITE    PKC_PHOSPHO_SITE    CK2_PHOSPHO_SITE    TYR_PHOSPHO_SITE    MYRISTYL    AMIDATION    PYRIDINE_REDOX_1     

Other Cross-Reference
    COG COG1249C 
    EcoCyc lpd 

MMBR References
J Gen Microbiol. 1980;121(2):277-92.
Molecular cloning of the pyruvate dehydrogenase complex genes of Escherichia coli.
Guest JR, Stephens PE. ( 6455499 )
J Gen Microbiol. 1983;129(3):671-80.
Hybrid plasmids containing the pyruvate dehydrogenase complex genes and gene-DNA relationships in the 2 to 3 minute region of the Escherichia coli chromosome.
Guest JR, Roberts RE, Stephens PE. ( 6308128 )
J Gen Microbiol. 1981;127:65-79.
Organization and expression of the pyruvate dehydrogenase complex genes of Escherichia coli K12.
Guest, J. R., S. T. Cole, and K. Jeyaseelan.
J Gen Microbiol. 1977;99(2):263-76.
Biochemical genetics of the alpha-keto acid dehydrogenase complexes of Escherichia coli K12: isolation and biochemical properties of deletion mutants.
Langley D, Guest JR. ( 327021 )
J Gen Microbiol. 1978;106(1):103-17.
Biochemical genetics of the alpha-keto acid dehydrogenase complexes of Escherichia coli K12: genetic characterization and regulatory properties of deletion mutants.
Langley D, Guest JR. ( 349114 )
Mol Gen Genet. 1985;200(1):145-54.
Transcription analysis of the sucAB, aceEF and lpd genes of Escherichia coli.
Spencer ME, Guest JR. ( 3897791 )
J Bacteriol. 1990;172(10):6142-4.
The lpd gene product functions as the L protein in the Escherichia coli glycine cleavage enzyme system.
Steiert PS, Stauffer LT, Stauffer GV. ( 2211531 )
Eur J Biochem. 1983;135:519-527
Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12.
Stephens, P. E., H. M. Lewis, M. G. Darlison, and J. R. Guest.
FEMS Microbiol Lett. 1998;159(2):325-9.
Environmental control of pyruvate dehydrogenase complex expression in Escherichia coli.
Cassey B, Guest JR, Attwood MM. ( 9503628 )
J Gen Microbiol. 1977;102(1):183-94.
Suppression of the succinate requirement of lipoamide dehydrogenase mutants of Escherichia coli by mutations affecting succinate dehydrogenase activity.
Creaghan IT, Guest JR. ( 335020 )

Sequences
Amino acid
FASTA format
0001 MSTEIKTQVV VLGAGPAGYS AAFRCADLGL ETVIVERYNT LGGVCLNVGC IPSKALLHVA KVIEEAKALA 
0071 EHGIVFGEPK TDIDKIRTWK EKVINQLTGG LAGMAKGRKV KVVNGLGKFT GANTLEVEGE NGKTVINFDN 
0141 AIIAAGSRPI QLPFIPHEDP RIWDSTDALE LKEVPERLLV MGGGIIGLEM GTVYHALGSQ IDVVEMFDQV 
0211 IPAADKDIVK VFTKRISKKF NLMLETKVTA VEAKEDGIYV TMEGKKAPAE PQRYDAVLVA IGRVPNGKNL 
0281 DAGKAGVEVD DRGFIRVDKQ LRTNVPHIFA IGDIVGQPML AHKGVHEGHV AAEVIAGKKH YFDPKVIPSI 
0351 AYTEPEVAWV GLTEKEAKEK GISYETATFP WAASGRAIAS DCADGMTKLI FDKESHRVIG GAIVGTNGGE 
0421 LLGEIGLAIE MGCDAEDIAL TIHAHPTLHE SVGLAAEVFE GSITDLPNPK AKKK

Nucleotide
FASTA format

View sequence out neighbor 100bp
-100                                             TTACATAAGT AAGTGACTGG GGTGAGGGCG 
-070 TGAAGCTAAC GCCGCTGCGG CCTGAAAGAC GACGGGTATG ACCGCCGGAG ATAAATATAT AGAGGTCATG 
0001 atgagtactg aaatcaaaac tcaggtcgtg gtacttgggg caggccccgc aggttactcc gctgccttcc 
0071 gttgcgctga tttaggtctg gaaaccgtaa tcgtagaacg ttacaacacc cttggcggtg tttgcctgaa 
0141 cgtcggctgt atcccttcta aagcactgct gcacgtagca aaagttatcg aagaagccaa agcgctggct 
0211 gaacacggta tcgtcttcgg cgaaccgaaa accgatatcg acaagattcg tacctggaaa gagaaagtga 
0281 tcaatcagct gaccggtggt ctggctggta tggcgaaagg ccgcaaagtc aaagtggtca acggtctggg 
0351 taaattcacc ggggctaaca ccctggaagt tgaaggtgag aacggcaaaa ccgtgatcaa cttcgacaac 
0421 gcgatcattg cagcgggttc tcgcccgatc caactgccgt ttattccgca tgaagatccg cgtatctggg 
0491 actccactga cgcgctggaa ctgaaagaag taccagaacg cctgctggta atgggtggcg gtatcatcgg 
0561 tctggaaatg ggcaccgttt accacgcgct gggttcacag attgacgtgg ttgaaatgtt cgaccaggtt 
0631 atcccggcag ctgacaaaga catcgttaaa gtcttcacca agcgtatcag caagaaattc aacctgatgc 
0701 tggaaaccaa agttaccgcc gttgaagcga aagaagacgg catttatgtg acgatggaag gcaaaaaagc 
0771 acccgctgaa ccgcagcgtt acgacgccgt gctggtagcg attggtcgtg tgccgaacgg taaaaacctc 
0841 gacgcaggca aagcaggcgt ggaagttgac gaccgtggtt tcatccgcgt tgacaaacag ctgcgtacca 
0911 acgtaccgca catctttgct atcggcgata tcgtcggtca accgatgctg gcacacaaag gtgttcacga 
0981 aggtcacgtt gccgctgaag ttatcgccgg taagaaacac tacttcgatc cgaaagttat cccgtccatc 
1051 gcctataccg aaccagaagt tgcatgggtg ggtctgactg agaaagaagc gaaagagaaa ggcatcagct 
1121 atgaaaccgc caccttcccg tgggctgctt ctggtcgtgc tatcgcttcc gactgcgcag acggtatgac 
1191 caagctgatt ttcgacaaag aatctcaccg tgtgatcggt ggtgcgattg tcggtactaa cggcggcgag 
1261 ctgctgggtg aaatcggcct ggcaatcgaa atgggttgtg atgctgaaga catcgcactg accatccacg 
1331 cgcacccgac tctgcacgag tctgtgggcc tggcggcaga agtgttcgaa ggtagcatta ccgacctgcc 
1401 gaacccgaaa gcgaagaaga agtaaTTTTT CGTTTGCCGG AACATCCGGC AATTAAAAAA GCGGCTAACC 
1471 ACGCCGCTTT TTTTACGTCT GCAATTTACC TTTCCAGTCT TCTTGCTCCA CGTTC