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Protein

Long-chain-fatty-acid--CoA ligase

Gene

fadD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi213 – 22412ATPCuratedAdd
BLAST

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • fatty acid binding Source: EcoliWiki
  • long-chain fatty acid-CoA ligase activity Source: EcoCyc
  • oleic acid binding Source: EcoliWiki

GO - Biological processi

  • acyl-CoA metabolic process Source: EcoCyc
  • fatty acid beta-oxidation Source: EcoCyc
  • fatty acid metabolic process Source: EcoliWiki
  • lipid metabolic process Source: EcoliWiki
  • long-chain fatty acid metabolic process Source: GOC
  • phospholipid biosynthetic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Protein family/group databases

TCDBi4.C.1.1.4. the proposed fatty acid transporter (fat) family.

Names & Taxonomyi

Protein namesi
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 namesi
Name:fadD
Synonyms:oldD
Ordered Locus Names:b1805, JW1794
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11530. fadD.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytoplasmic side of plasma membrane Source: EcoCyc
  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi213 – 2131Y → A: Loss of activity. 1 Publication
Mutagenesisi214 – 2141T → A: 10% of wild-type activity. 1 Publication
Mutagenesisi216 – 2161G → A: Decreases activity. 1 Publication
Mutagenesisi217 – 2171T → A: Decreases activity. 1 Publication
Mutagenesisi219 – 2191G → A: Decreases activity. 1 Publication
Mutagenesisi222 – 2221K → A: Decreases activity. 1 Publication
Mutagenesisi361 – 3611E → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 561561Long-chain-fatty-acid--CoA ligasePRO_0000193125Add
BLAST

Proteomic databases

PaxDbiP69451.
PRIDEiP69451.

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

IntActiP69451. 6 interactions.
STRINGi511145.b1805.

Structurei

3D structure databases

ProteinModelPortaliP69451.
SMRiP69451. Positions 60-551.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0318.
HOGENOMiHOG000229983.
InParanoidiP69451.
KOiK01897.
OMAiESFAKFR.
OrthoDBiEOG6MH5BV.
PhylomeDBiP69451.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P69451-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVWLNRYP ADVPTEINPD RYQSLVDMFE QSVARYADQP AFVNMGEVMT
60 70 80 90 100
FRKLEERSRA FAAYLQQGLG LKKGDRVALM MPNLLQYPVA LFGILRAGMI
110 120 130 140 150
VVNVNPLYTP RELEHQLNDS GASAIVIVSN FAHTLEKVVD KTAVQHVILT
160 170 180 190 200
RMGDQLSTAK GTVVNFVVKY IKRLVPKYHL PDAISFRSAL HNGYRMQYVK
210 220 230 240 250
PELVPEDLAF LQYTGGTTGV AKGAMLTHRN MLANLEQVNA TYGPLLHPGK
260 270 280 290 300
ELVVTALPLY HIFALTINCL LFIELGGQNL LITNPRDIPG LVKELAKYPF
310 320 330 340 350
TAITGVNTLF NALLNNKEFQ QLDFSSLHLS AGGGMPVQQV VAERWVKLTG
360 370 380 390 400
QYLLEGYGLT ECAPLVSVNP YDIDYHSGSI GLPVPSTEAK LVDDDDNEVP
410 420 430 440 450
PGQPGELCVK GPQVMLGYWQ RPDATDEIIK NGWLHTGDIA VMDEEGFLRI
460 470 480 490 500
VDRKKDMILV SGFNVYPNEI EDVVMQHPGV QEVAAVGVPS GSSGEAVKIF
510 520 530 540 550
VVKKDPSLTE ESLVTFCRRQ LTGYKVPKLV EFRDELPKSN VGKILRRELR
560
DEARGKVDNK A
Length:561
Mass (Da):62,332
Last modified:March 1, 2005 - v1
Checksum:i249B0AA54B3DBFA5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 5118ARYAD…EVMTF → GALRRSTCVCEYGGGNDL in AAA23752 (PubMed:1460045).CuratedAdd
BLAST
Sequence conflicti468 – 49023NEIED…VGVPS → TRLKMSSCSMVAYRKSRLLA YLP in AAA23752 (PubMed:1460045).CuratedAdd
BLAST
Sequence conflicti496 – 4961A → G in AAA23752 (PubMed:1460045).Curated
Sequence conflicti555 – 5617GKVDNKA → QSGQ in AAA23752 (PubMed:1460045).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70994 Genomic DNA. Translation: CAA50321.1.
L02649 Genomic DNA. Translation: AAA23752.1.
U00096 Genomic DNA. Translation: AAC74875.1.
AP009048 Genomic DNA. Translation: BAA15609.1.
PIRiE64941. S41589.
RefSeqiNP_416319.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC74875; AAC74875; b1805.
BAA15609; BAA15609; BAA15609.
GeneIDi946327.
KEGGieco:b1805.
PATRICi32118927. VBIEscCol129921_1881.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70994 Genomic DNA. Translation: CAA50321.1.
L02649 Genomic DNA. Translation: AAA23752.1.
U00096 Genomic DNA. Translation: AAC74875.1.
AP009048 Genomic DNA. Translation: BAA15609.1.
PIRiE64941. S41589.
RefSeqiNP_416319.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP69451.
SMRiP69451. Positions 60-551.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP69451. 6 interactions.
STRINGi511145.b1805.

Protein family/group databases

TCDBi4.C.1.1.4. the proposed fatty acid transporter (fat) family.

Proteomic databases

PaxDbiP69451.
PRIDEiP69451.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74875; AAC74875; b1805.
BAA15609; BAA15609; BAA15609.
GeneIDi946327.
KEGGieco:b1805.
PATRICi32118927. VBIEscCol129921_1881.

Organism-specific databases

EchoBASEiEB1492.
EcoGeneiEG11530. fadD.

Phylogenomic databases

eggNOGiCOG0318.
HOGENOMiHOG000229983.
InParanoidiP69451.
KOiK01897.
OMAiESFAKFR.
OrthoDBiEOG6MH5BV.
PhylomeDBiP69451.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP69451.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. 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.

Entry informationi

Entry nameiLCFA_ECOLI
AccessioniPrimary (citable) accession number: P69451
Secondary accession number(s): P29212
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: July 22, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Activity is the highest with fatty acid substrates of > 10 carbon atoms.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.