Reviewed, UniProtKB/Swiss-Prot P69451 (LCFA_ECOLI)

Names and origin

Protein names

Recommended name:
    Long-chain-fatty-acid--CoA ligase
    EC=6.2.1.3
Alternative name(s):
    Long-chain acyl-CoA synthetase
      Short name=Acyl-CoA synthetase

Gene names

Name:	fadD
Synonyms:	oldD
Ordered Locus Names:	b1805, JW1794

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	561 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids.
Catalytic activity	ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.
Subunit structure	Homodimer Probable.
Subcellular location	Membrane; Peripheral membrane protein By similarity. Note: Partially membrane-associated By similarity.
Miscellaneous	Activity is the highest with fatty acid substrates of > 10 carbon atoms.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain-fatty-acid-CoA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 561	561	Long-chain-fatty-acid--CoA ligase		PRO_0000193125
Regions
	Nucleotide binding	213 – 224	12	ATP Probable
Experimental info
	Mutagenesis	213	1	Y → A: Loss of activity. Ref.6
	Mutagenesis	214	1	T → A: 10% of wild-type activity. Ref.6
	Mutagenesis	216	1	G → A: Decreases activity. Ref.6
	Mutagenesis	217	1	T → A: Decreases activity. Ref.6
	Mutagenesis	219	1	G → A: Decreases activity. Ref.6
	Mutagenesis	222	1	K → A: Decreases activity. Ref.6
	Mutagenesis	361	1	E → A: Loss of activity. Ref.6
	Sequence conflict	34 – 51	18	ARYAD…EVMTF → GALRRSTCVCEYGGGNDL in AAA23752. Ref.2
	Sequence conflict	468 – 490	23	NEIED…VGVPS → TRLKMSSCSMVAYRKSRLLA YLP in AAA23752. Ref.2
	Sequence conflict	496	1	A → G in AAA23752. Ref.2
	Sequence conflict	555 – 561	7	GKVDNKA → QSGQ in AAA23752. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P69451-1 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: 249B0AA54B3DBFA5	FASTA	561	62,332
	10 20 30 40 50 60 MKKVWLNRYP ADVPTEINPD RYQSLVDMFE QSVARYADQP AFVNMGEVMT FRKLEERSRA 70 80 90 100 110 120 FAAYLQQGLG LKKGDRVALM MPNLLQYPVA LFGILRAGMI VVNVNPLYTP RELEHQLNDS 130 140 150 160 170 180 GASAIVIVSN FAHTLEKVVD KTAVQHVILT RMGDQLSTAK GTVVNFVVKY IKRLVPKYHL 190 200 210 220 230 240 PDAISFRSAL HNGYRMQYVK PELVPEDLAF LQYTGGTTGV AKGAMLTHRN MLANLEQVNA 250 260 270 280 290 300 TYGPLLHPGK ELVVTALPLY HIFALTINCL LFIELGGQNL LITNPRDIPG LVKELAKYPF 310 320 330 340 350 360 TAITGVNTLF NALLNNKEFQ QLDFSSLHLS AGGGMPVQQV VAERWVKLTG QYLLEGYGLT 370 380 390 400 410 420 ECAPLVSVNP YDIDYHSGSI GLPVPSTEAK LVDDDDNEVP PGQPGELCVK GPQVMLGYWQ 430 440 450 460 470 480 RPDATDEIIK NGWLHTGDIA VMDEEGFLRI VDRKKDMILV SGFNVYPNEI EDVVMQHPGV 490 500 510 520 530 540 QEVAAVGVPS GSSGEAVKIF VVKKDPSLTE ESLVTFCRRQ LTGYKVPKLV EFRDELPKSN 550 560 VGKILRRELR DEARGKVDNK A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The fadD gene of Escherichia coli K12 is located close to rnd at 39.6 min of the chromosomal map and is a new member of the AMP-binding protein family." Fulda M., Heinz E., Wolter F.P. Mol. Gen. Genet. 242:241-249(1994) [PubMed: 8107670] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase." Black P.N., Dirusso C.C., Metzger A.K., Heimert T.L. J. Biol. Chem. 267:25513-25520(1992) [PubMed: 1460045] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10. Strain: K12.
[3]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"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." Weimar J.D., DiRusso C.C., Delio R., Black P.N. J. Biol. Chem. 277:29369-29376(2002) [PubMed: 12034706] [Abstract] Cited for: IDENTIFICATION OF ATP-BINDING MOTIF, MUTAGENESIS OF TYR-213; THR-214; GLY-216; THR-217; GLY-219; LYS-222 AND GLU-361.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X70994 Genomic DNA. Translation: CAA50321.1. L02649 Genomic DNA. Translation: AAA23752.1. U00096 Genomic DNA. Translation: AAC74875.1. AP009048 Genomic DNA. Translation: BAA15609.1.
PIR	S41589. E64941.
RefSeq	AP_002424.1. NP_416319.1.
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBase	Search...
Protein-protein interaction databases
STRING	P69451.
Protein family/group databases
TCDB	4.C.1.1.4. proposed fatty acid transporter (FAT) family.
Genome annotation databases
GeneID	946327.
GenomeReviews	Gene locus JW1794 in contig AP009048_GR. Gene locus b1805 in contig U00096_GR.
KEGG	ecj:JW1794. eco:b1805.
Organism-specific databases
EchoBASE	EB1492.
EcoGene	EG11530. fadD.
CMR	Search...
Phylogenomic databases
HOGENOM	P69451.
OMA	CRAHLTG.
Enzyme and pathway databases
BioCyc	EcoCyc:ACYLCOASYN-MON. MetaCyc:ACYLCOASYN-MON.
Gene expression databases
Genevestigator	P69451.
Family and domain databases
InterPro	IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LCFA_ECOLI

Accession

Primary (citable) accession number: P69451
Secondary accession number(s): P29212

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	November 3, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)