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PEC Original Annotations
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Essentiality
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Class
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non-essential
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References (PMID)
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Deletion
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OCR31
(D)
,
OCR31-7
(D)
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Related gene (W3110 PEC)
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Gene Search
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Search MG1655 PEC by gene name:
lpd
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Related strains
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Strains Search
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Search strains by gene name:
lpd
Search strains by all related name:
lpd b0116 dhl ECK0115 JW0112 lpdA
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General information (Go to Linear View: )
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Gene Name
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lpd
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Alternative name
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b0116,dhl,ECK0115,JW0112,lpdA
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Location, Length
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127,912 - 129,336
(
+
)
;
2.76
min
;
1425
(bp) ,
474
(aa)
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Product
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lipoamide dehydrogenase, E3 component is part of three enzyme complexes
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Operon Name
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pdhR-aceEF-lpd
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Note
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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
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Function
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enzyme; Energy metabolism, carbon: Pyruvate dehydrogenase
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Gene Ontology
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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 )
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PID
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1786307
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EC number
(KEGG Pathway)
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1.8.1.4
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SWISS-PROT
(
Show simple
)
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Entry name(Acc.no)
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DLDH_ECOLI
(
P00391
)
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- Protein name
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Dihydrolipoyl dehydrogenase
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- Synonyms
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EC 1.8.1.4, E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes, Dihydrolipoamide dehydrogenase, Glycine cleavage system L protein
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- Gene name
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OrderedLocusNames=b0116, c0145, z0126, ECs0120, SF0113, S0115;
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- Comments
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FUNCTION:Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes.
CATALYTIC ACTIVITY:Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH.
COFACTOR:Binds 1 FAD per subunit (By similarity).
SUBUNIT:Homodimer.
SUBCELLULAR LOCATION:Cytoplasmic.
MISCELLANEOUS:The active site is a redox-active disulfide bond.
SIMILARITY:Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
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MMBR References
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J Gen Microbiol. 1980;121(2):277-92.
Molecular cloning of the pyruvate dehydrogenase complex genes of Escherichia coli.
Guest JR, Stephens PE.
(
6455499
)
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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
)
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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.
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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
)
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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
)
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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.
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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
)
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| Sequences |
Amino acid
FASTA format
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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
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Nucleotide
FASTA format
View sequence out neighbor 100bp
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-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
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