Long-chain-fatty-acid--CoA ligase - Escherichia coli (strain K12)

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P69451 (LCFA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	561 AA.
Sequence status	Complete.
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 fatty 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 Reference proteome
Gene Ontology (GO)
Biological_process	acyl-CoA metabolic process Inferred from direct assay PubMed 7016858. Source: EcoCyc fatty acid beta-oxidation Inferred from direct assay PubMed 7016858. Source: EcoCyc phospholipid biosynthetic process Inferred from mutant phenotype PubMed 1649829. Source: EcoliWiki
Cellular_component	cytosol Traceable author statement Ref.6. Source: EcoCyc internal side of plasma membrane Traceable author statement Ref.6. Source: EcoCyc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain fatty acid-CoA ligase activity Inferred from direct assay PubMed 7016858. Source: EcoCyc oleic acid binding Inferred from mutant phenotype PubMed 9030548. Source: EcoliWiki
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

ATP Probable

Experimental info

Mutagenesis

213

Y → A: Loss of activity. Ref.6

Mutagenesis

214

T → A: 10% of wild-type activity. Ref.6

Mutagenesis

216

G → A: Decreases activity. Ref.6

Mutagenesis

217

T → A: Decreases activity. Ref.6

Mutagenesis

219

G → A: Decreases activity. Ref.6

Mutagenesis

222

K → A: Decreases activity. Ref.6

Mutagenesis

361

E → A: Loss of activity. Ref.6

Sequence conflict

34 – 51

ARYAD…EVMTF → GALRRSTCVCEYGGGNDL in AAA23752. Ref.2

Sequence conflict

468 – 490

NEIED…VGVPS → TRLKMSSCSMVAYRKSRLLA YLP in AAA23752. Ref.2

Sequence conflict

496

A → G in AAA23752. Ref.2

Sequence conflict

555 – 561

GKVDNKA → QSGQ in AAA23752. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P69451 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 249B0AA54B3DBFA5
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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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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. Horiuchi T. DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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
EMBL GenBank DDBJ	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	NP_416319.1. NC_000913.2. YP_490066.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P69451.
SMR	P69451. Positions 19-551.
ModBase	Search...
Protein-protein interaction databases
IntAct	P69451. 6 interactions.
STRING	511145.b1805.
Protein family/group databases
TCDB	4.C.1.1.4. proposed fatty acid transporter (FAT) family.
Proteomic databases
PaxDb	P69451.
PRIDE	P69451.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74875; AAC74875; b1805. BAA15609; BAA15609; BAA15609.
GeneID	12930156. 946327.
KEGG	ecj:Y75_p1780. eco:b1805.
PATRIC	32118927. VBIEscCol129921_1881.
Organism-specific databases
EchoBASE	EB1492.
EcoGene	EG11530. fadD.
Phylogenomic databases
eggNOG	COG0318.
HOGENOM	HOG000229983.
KO	K01897.
OMA	MPVQQAV.
ProtClustDB	PRK08974.
Enzyme and pathway databases
BioCyc	EcoCyc:ACYLCOASYN-MONOMER. ECOL316407:JW1794-MONOMER. MetaCyc:ACYLCOASYN-MONOMER.
SABIO-RK	P69451.
Gene expression databases
Genevestigator	P69451.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR025110. DUF4009. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. PF13193. DUF4009. 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:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents