RegulonDB RegulonDB 10.9: Gene Form
   

lipA gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

lipA ybeF tatE lipAp lipAp

Gene      
Name: lipA    Texpresso search in the literature
Synonym(s): ECK0621, EG11306, b0628, lip
Genome position(nucleotides): 659251 <-- 660216 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
53.42
External database links:  
ASAP:
ABE-0002155
CGSC:
31534
ECHOBASE:
EB1283
ECOLIHUB:
lipA
MIM:
607031
MIM:
614462
OU-MICROARRAY:
b0628
STRING:
511145.b0628
COLOMBOS: lipA


Product      
Name: lipoyl synthase
Synonym(s): Lip, LipA
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 36.072
Isoelectric point: 8.024
Motif(s):
 
Type Positions Sequence
68 -> 79 CEEASCPNLAEC
80 -> 297 FNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFT
91 -> 252 GAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDL
25 -> 73 KNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASC
94 -> 101 CTRRCPFC

 

Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.5 - biosynthesis of building blocks --> 1.5.3 - cofactors, small molecule carriers --> 1.5.3.3 - lipoate
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
molecular_function GO:0102552 - lipoyl synthase activity (acting on glycine-cleavage complex H protein
GO:0102553 - lipoyl synthase activity (acting on pyruvate dehydrogenase E2 protein)
GO:0003824 - catalytic activity
GO:0005515 - protein binding
GO:0016740 - transferase activity
GO:0046872 - metal ion binding
GO:0016783 - sulfurtransferase activity
GO:0051536 - iron-sulfur cluster binding
GO:0051539 - 4 iron, 4 sulfur cluster binding
GO:0016992 - lipoate synthase activity
GO:0042803 - protein homodimerization activity
biological_process GO:0009107 - lipoate biosynthetic process
GO:0009249 - protein lipoylation
Note(s): Note(s): ...[more].
Reference(s): [1] Chang YY., et al., 1991
[2] Choi-Rhee E., et al., 2005
[3] Creaghan IT., et al., 1978
[4] Gonidakis S., et al., 2010
[5] Hayden MA., et al., 1992
[6] Herbert AA., et al., 1968
[7] Inoue K., et al., 2002
[8] Lanz ND., et al., 2014
[9] McCarthy EL., et al., 2017
[10] Sun Y., et al., 2017
[11] Wan JT., et al., 2002
External database links:  
DIP:
DIP-48008N
ECOCYC:
EG11306-MONOMER
ECOLIWIKI:
b0628
INTERPRO:
IPR006638
INTERPRO:
IPR031691
INTERPRO:
IPR013785
INTERPRO:
IPR007197
INTERPRO:
IPR003698
MODBASE:
P60716
PANTHER:
PTHR10949
PFAM:
PF04055
PFAM:
PF16881
PRIDE:
P60716
PRODB:
PRO_000023092
PROSITE:
PS51918
REFSEQ:
NP_415161
SMART:
SM00729
SMR:
P60716
UNIPROT:
P60716


Operon      
Name: lipA         
Operon arrangement:
Transcription unit        Promoter
lipA


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References


Reference(s)    

 [1] Chang YY., Cronan JE., Li SJ., Reed K., Vanden Boom T., Wang AY., 1991, Locations of the lip, poxB, and ilvBN genes on the physical map of Escherichia coli., J Bacteriol 173(17):5258-9

 [2] Choi-Rhee E., Cronan JE., 2005, A nucleosidase required for in vivo function of the S-adenosyl-L-methionine radical enzyme, biotin synthase., Chem Biol 12(5):589-93

 [3] Creaghan IT., Guest JR., 1978, Succinate dehydrogenase-dependent nutritional requirement for succinate in mutants of Escherichia coli K12., J Gen Microbiol 107(1):1-13

 [4] Gonidakis S., Finkel SE., Longo VD., 2010, E. coli hypoxia-inducible factor ArcA mediates lifespan extension in a lipoic acid synthase mutant by suppressing acetyl-CoA synthetase., Biol Chem 391(10):1139-47

 [5] Hayden MA., Huang I., Bussiere DE., Ashley GW., 1992, The biosynthesis of lipoic acid. Cloning of lip, a lipoate biosynthetic locus of Escherichia coli., J Biol Chem 267(14):9512-5

 [6] Herbert AA., Guest JR., 1968, Biochemical and genetic studies with lysine+methionine mutants of Escherichia coli: lipoic acid and alpha-ketoglutarate dehydrogenase-less mutants., J Gen Microbiol 53(3):363-81

 [7] Inoue K., Chen J., Kato I., Inouye M., 2002, Specific growth inhibition by acetate of an Escherichia coli strain expressing Era-dE, a dominant negative Era mutant., J Mol Microbiol Biotechnol 4(4):379-88

 [8] Lanz ND., Pandelia ME., Kakar ES., Lee KH., Krebs C., Booker SJ., 2014, Evidence for a catalytically and kinetically competent enzyme-substrate cross-linked intermediate in catalysis by lipoyl synthase., Biochemistry 53(28):4557-72

 [9] McCarthy EL., Booker SJ., 2017, Destruction and reformation of an iron-sulfur cluster during catalysis by lipoyl synthase., Science 358(6361):373-377

 [10] Sun Y., Zhang W., Ma J., Pang H., Wang H., 2017, Overproduction of α-Lipoic Acid by Gene Manipulated Escherichia coli., PLoS One 12(1):e0169369

 [11] Wan JT., Jarrett JT., 2002, Electron acceptor specificity of ferredoxin (flavodoxin):NADP+ oxidoreductase from Escherichia coli., Arch Biochem Biophys 406(1):116-26


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