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P69452 (LCFA_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Ordered Locus Names:c2209
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length561 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

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 By similarity.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Sequence caution

The sequence AAN80668.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMembrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentmembrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

long-chain fatty acid-CoA ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 561561Long-chain-fatty-acid--CoA ligase
PRO_0000193126

Regions

Nucleotide binding213 – 22412ATP Probable

Sequences

Sequence LengthMass (Da)Tools
P69452 [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

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN80668.1. Different initiation.
PIRS41589. E64941.
RefSeqNP_754103.1. NC_004431.1.

3D structure databases

ProteinModelPortalP69452.
SMRP69452. Positions 60-551.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c2209.

Proteomic databases

PRIDEP69452.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN80668; AAN80668; c2209.
GeneID1036653.
KEGGecc:c2209.
PATRIC18282309. VBIEscCol75197_2071.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000229983.
KOK01897.
OMANIIEGYG.
OrthoDBEOG6MH5BV.
ProtClustDBPRK08974.

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...

Entry information

Entry nameLCFA_ECOL6
AccessionPrimary (citable) accession number: P69452
Secondary accession number(s): P29212
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: April 16, 2014
This is version 60 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