RegulonDB RegulonDB 11.1: Gene Form
   

fadD gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

fadD rnd yeaY sroD FadR CRP FadR ArcA ppGpp anti-anti-terminator anti-terminator terminator fadDp fadDp rndp rndp

Gene      
Name: fadD    Texpresso search in the literature
Synonym(s): ECK1803, EG11530, b1805, oldD
Genome position(nucleotides): 1888061 <-- 1889746
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
51.19
External database links:  
ASAP:
ABE-0006005
CGSC:
792
ECHOBASE:
EB1492
ECOLIHUB:
fadD
OU-MICROARRAY:
b1805
STRING:
511145.b1805
COLOMBOS: fadD


Shine dalgarno      
Sequence: acgcattttaGAGGTGaagaATT


Product      
Name: long-chain-fatty-acid—CoA ligase
Synonym(s): FadD, OldD, fatty acyl-CoA synthetase
Sequence: Get amino acid sequence Fasta Format
Cellular location: inner membrane,cytosol
Molecular weight: 62.332
Isoelectric point: 6.664
Motif(s):
 
Type Positions Sequence Comment
29 -> 460 FEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKGTVVNFVVKYIKRLVPKYHLPDAISFRSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELVVTALPLYHIFALTINCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILV
34 -> 51 ARYADQPAFVNMGEVMTF UniProt: In Ref. 2; AAA23752..
213 -> 224 YTGGTTGVAKGA UniProt: ATP.
214 -> 214 T UniProt: 10% of wild-type activity..
216 -> 216 G UniProt: Decreases activity..

 

Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.1 - carbon utilization --> 1.1.2 - fatty acids
  1 - metabolism --> 1.6 - biosynthesis of macromolecules (cellular constituents) --> 1.6.1 - phospholipid
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
GO:0016020 - membrane
GO:0005886 - plasma membrane
GO:0009898 - cytoplasmic side of plasma membrane
molecular_function GO:0016874 - ligase activity
GO:0000166 - nucleotide binding
GO:0005524 - ATP binding
GO:0004467 - long-chain fatty acid-CoA ligase activity
GO:0005504 - fatty acid binding
GO:0042803 - protein homodimerization activity
GO:0070538 - oleic acid binding
GO:0102391 - decanoate-CoA ligase activity
biological_process GO:0006629 - lipid metabolic process
GO:0006631 - fatty acid metabolic process
GO:0008654 - phospholipid biosynthetic process
GO:0009411 - response to UV
GO:0006635 - fatty acid beta-oxidation
GO:0006637 - acyl-CoA metabolic process
GO:0015908 - fatty acid transport
GO:0001676 - long-chain fatty acid metabolic process
Note(s): Note(s): ...[more].
Reference(s): [1] Klein K., et al., 1971
[2] Overath P., et al., 1969
[3] Sargentini NJ., et al., 2016
External database links:  
ALPHAFOLD:
P69451
ECOCYC:
ACYLCOASYN-MONOMER
ECOLIWIKI:
b1805
INTERPRO:
IPR025110
INTERPRO:
IPR042099
INTERPRO:
IPR020845
INTERPRO:
IPR000873
MODBASE:
P69451
PFAM:
PF13193
PFAM:
PF00501
PRIDE:
P69451
PRODB:
PRO_000022568
PROSITE:
PS00455
REFSEQ:
NP_416319
SMR:
P69451
UNIPROT:
P69451


Operon      
Name: fadD-sroD         
Operon arrangement:
Transcription unit        Promoter
fadD-sroD


Transcriptional Regulation      
Display Regulation             
Activated by: CRP
Repressed by: FadR, ArcA


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] Klein K., Steinberg R., Fiethen B., Overath P., 1971, Fatty acid degradation in Escherichia coli. An inducible system for the uptake of fatty acids and further characterization of old mutants., Eur J Biochem 19(3):442-50

 [2] Overath P., Pauli G., Schairer HU., 1969, Fatty acid degradation in Escherichia coli. An inducible acyl-CoA synthetase, the mapping of old-mutations, and the isolation of regulatory mutants., Eur J Biochem 7(4):559-74

 [3] Sargentini NJ., Gularte NP., Hudman DA., 2016, Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database., Mutat Res 793-794:1-14


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