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P69451 (LCFA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length561 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 561561Long-chain-fatty-acid--CoA ligase
PRO_0000193125

Regions

Nucleotide binding213 – 22412ATP Probable

Experimental info

Mutagenesis2131Y → A: Loss of activity. Ref.6
Mutagenesis2141T → A: 10% of wild-type activity. Ref.6
Mutagenesis2161G → A: Decreases activity. Ref.6
Mutagenesis2171T → A: Decreases activity. Ref.6
Mutagenesis2191G → A: Decreases activity. Ref.6
Mutagenesis2221K → A: Decreases activity. Ref.6
Mutagenesis3611E → A: Loss of activity. Ref.6
Sequence conflict34 – 5118ARYAD…EVMTF → GALRRSTCVCEYGGGNDL in AAA23752. Ref.2
Sequence conflict468 – 49023NEIED…VGVPS → TRLKMSSCSMVAYRKSRLLA YLP in AAA23752. Ref.2
Sequence conflict4961A → G in AAA23752. Ref.2
Sequence conflict555 – 5617GKVDNKA → QSGQ in AAA23752. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P69451 [UniParc].

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

FASTA56162,332
        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' 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. expand/collapse author list , 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] [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 277:1453-1462(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.
+Additional computationally mapped references.

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.
PIRS41589. E64941.
RefSeqNP_416319.1. NC_000913.3.
YP_490066.1. NC_007779.1.

3D structure databases

ProteinModelPortalP69451.
SMRP69451. Positions 60-551.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP69451. 6 interactions.
STRING511145.b1805.

Protein family/group databases

TCDB4.C.1.1.4. the proposed fatty acid transporter (fat) family.

Proteomic databases

PaxDbP69451.
PRIDEP69451.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74875; AAC74875; b1805.
BAA15609; BAA15609; BAA15609.
GeneID12930156.
946327.
KEGGecj:Y75_p1780.
eco:b1805.
PATRIC32118927. VBIEscCol129921_1881.

Organism-specific databases

EchoBASEEB1492.
EcoGeneEG11530. fadD.

Phylogenomic databases

eggNOGCOG0318.
HOGENOMHOG000229983.
KOK01897.
OMAVATRWHE.
OrthoDBEOG6MH5BV.
PhylomeDBP69451.

Enzyme and pathway databases

BioCycEcoCyc:ACYLCOASYN-MONOMER.
ECOL316407:JW1794-MONOMER.
MetaCyc:ACYLCOASYN-MONOMER.
RETL1328306-WGS:GSTH-490-MONOMER.
SABIO-RKP69451.

Gene expression databases

GenevestigatorP69451.

Family and domain databases

InterProIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP69451.

Entry information

Entry nameLCFA_ECOLI
AccessionPrimary (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: July 9, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

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