ECOLI:LCFA

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	fadD (synonyms: oldD)
Protein Name(s)	Long-chain-fatty-acid--CoA ligase Long-chain acyl-CoA synthetase Acyl-CoA synthetase
External Links
UniProt	P69451
EMBL	X70994 L02649 U00096 AP009048
PIR	E64941
RefSeq	NP_416319.1 YP_490066.1
ProteinModelPortal	P69451
SMR	P69451
IntAct	P69451
STRING	511145.b1805
TCDB	4.C.1.1.4
PaxDb	P69451
PRIDE	P69451
EnsemblBacteria	AAC74875 BAA15609
GeneID	12930156 946327
KEGG	ecj:Y75_p1780 eco:b1805
PATRIC	32118927
EchoBASE	EB1492
EcoGene	EG11530
eggNOG	COG0318
HOGENOM	HOG000229983
InParanoid	P69451
KO	K01897
OMA	CNPATID
OrthoDB	EOG6MH5BV
PhylomeDB	P69451
BioCyc	EcoCyc:ACYLCOASYN-MONOMER ECOL316407:JW1794-MONOMER MetaCyc:ACYLCOASYN-MONOMER RETL1328306-WGS:GSTH-490-MONOMER
SABIO-RK	P69451
PRO	PR:P69451
Proteomes	UP000000318 UP000000625
Genevestigator	P69451
GO	GO:0005737 GO:0009898 GO:0005829 GO:0005524 GO:0005504 GO:0004467 GO:0070538 GO:0006637 GO:0006635 GO:0006631 GO:0006629 GO:0001676 GO:0008654
InterPro	IPR025110 IPR020845 IPR000873
Pfam	PF00501 PF13193
PROSITE	PS00455

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0006629	lipid metabolic process	PMID:1649829^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9030548^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005504	fatty acid binding	PMID:9030548^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004467	long-chain fatty acid-CoA ligase activity	PMID:9030548^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004467	long-chain fatty acid-CoA ligase activity	PMID:1460045^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0070538	oleic acid binding	PMID:9030548^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0008654	phospholipid biosynthetic process	PMID:1649829^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006631	fatty acid metabolic process	PMID:1649829^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009411	response to UV	PMID:27718375^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006637	acyl-CoA metabolic process	PMID:7016858^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006635	fatty acid beta-oxidation	PMID:7016858^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004467	long-chain fatty acid-CoA ligase activity	PMID:7016858^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0001676	long-chain fatty acid metabolic process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004467	P	Seeded From UniProt	complete
involved_in	GO:0001676	long-chain fatty acid metabolic process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004467	P	Seeded From UniProt	complete
involved_in	GO:0001676	long-chain fatty acid metabolic process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004467	P	Seeded From UniProt	complete
involved_in	GO:0001676	long-chain fatty acid metabolic process	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004467	P	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000873	F	Seeded From UniProt	complete
enables	GO:0003996	acyl-CoA ligase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:6.2.1.3	F	Seeded From UniProt	complete
enables	GO:0004467	long-chain fatty acid-CoA ligase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:6.2.1.3	F	Seeded From UniProt	complete
enables	GO:0102391	decanoate-CoA ligase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:6.2.1.3	F	Seeded From UniProt	complete
part_of	GO:0009898	cytoplasmic side of plasma membrane	PMID:12034706^[6]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:12034706^[6]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
enables	GO:0016874	ligase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0436	F	Seeded From UniProt	complete
involved_in	GO:0006631	fatty acid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0276	P	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C	Seeded From UniProt	complete
involved_in	GO:0006629	lipid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0443	P	Seeded From UniProt	complete
involved_in	GO:0006635	fatty acid beta-oxidation	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00659	P	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Hsu, L et al. (1991) Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity. J. Biol. Chem. 266 13783-8 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Black, PN et al. (1997) Mutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity. J. Biol. Chem. 272 4896-903 PubMed GONUTS page
↑ Black, PN et al. (1992) Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase. J. Biol. Chem. 267 25513-20 PubMed GONUTS page
↑ Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Kameda, K & Nunn, WD (1981) Purification and characterization of acyl coenzyme A synthetase from Escherichia coli. J. Biol. Chem. 256 5702-7 PubMed GONUTS page
↑ ^6.0 ^6.1 Weimar, JD et al. (2002) Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport. J. Biol. Chem. 277 29369-76 PubMed GONUTS page

[PMID:1649829-1] 1.0 ^1.1 ^1.2 Hsu, L et al. (1991) Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity. J. Biol. Chem. 266 13783-8 PubMed GONUTS page

[PMID:9030548-2] 2.0 ^2.1 ^2.2 ^2.3 Black, PN et al. (1997) Mutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity. J. Biol. Chem. 272 4896-903 PubMed GONUTS page

[PMID:1460045-3] Black, PN et al. (1992) Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase. J. Biol. Chem. 267 25513-20 PubMed GONUTS page

[PMID:27718375-4] Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page

[PMID:7016858-5] 5.0 ^5.1 ^5.2 Kameda, K & Nunn, WD (1981) Purification and characterization of acyl coenzyme A synthetase from Escherichia coli. J. Biol. Chem. 256 5702-7 PubMed GONUTS page

[PMID:12034706-6] 6.0 ^6.1 Weimar, JD et al. (2002) Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport. J. Biol. Chem. 277 29369-76 PubMed GONUTS page

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ECOLI:LCFA

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