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Protein

Long-chain-fatty-acid--CoA ligase

Gene

fadD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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. Activity is the highest with fatty acid substrates of > 10 carbon atoms (PubMed:15213221). Is involved in the aerobic beta-oxidative degradation of fatty acids, which allows aerobic growth of E.coli on fatty acids as a sole carbon and energy source (PubMed:12535077).2 Publications

Miscellaneous

The enzymatic mechanism is a two-step reaction that proceeds via the intermediate formation of an acyl-adenylate (acyl-AMP) intermediate.1 Publication

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.1 Publication

Cofactori

Mg2+1 Publication

pH dependencei

Optimum pH is 7.5-7.8.1 Publication

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.1 Publication1 Publication
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi213 – 224ATPCuratedAdd BLAST12

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • decanoate-CoA ligase activity Source: UniProtKB-EC
  • 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
  • phospholipid biosynthetic process Source: EcoliWiki
  • response to UV Source: EcoCyc

Keywordsi

Molecular functionLigase
Biological processFatty acid metabolism, Lipid metabolism
LigandATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ACYLCOASYN-MONOMER
MetaCyc:ACYLCOASYN-MONOMER
SABIO-RKiP69451
UniPathwayiUPA00659

Protein family/group databases

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

Chemistry databases

SwissLipidsiSLP:000001723

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain-fatty-acid--CoA ligase (EC:6.2.1.31 Publication)
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are completely blocked in aerobic growth on fatty acids. The double fadD fadK deletion mutant fails to grow on fatty acids under either aerobic or anaerobic conditions, although fadD mutants grow on fatty acids under anaerobic conditions.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi213Y → A: Loss of activity. 1 Publication1
Mutagenesisi214T → A: 10% of wild-type activity. 1 Publication1
Mutagenesisi216G → A: Decreases activity. 1 Publication1
Mutagenesisi217T → A: Decreases activity. 1 Publication1
Mutagenesisi219G → A: Decreases activity. 1 Publication1
Mutagenesisi222K → A: Decreases activity. 1 Publication1
Mutagenesisi361E → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001931251 – 561Long-chain-fatty-acid--CoA ligaseAdd BLAST561

Post-translational modificationi

Post-translationally cleaved by OmpT (PubMed:15213221).1 Publication

Proteomic databases

EPDiP69451
PaxDbiP69451
PRIDEiP69451

Expressioni

Inductioni

Well expressed during log and stationary phase aerobic growth but only poorly expressed during anaerobic growth (at protein level); aerobic expression is suppressed by glucose or C8 fatty acids (PubMed:15213221).1 Publication

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi4259150, 224 interactors
IntActiP69451, 6 interactors
STRINGi316385.ECDH10B_1943

Structurei

3D structure databases

ProteinModelPortaliP69451
SMRiP69451
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CEY Bacteria
COG0318 LUCA
HOGENOMiHOG000229983
InParanoidiP69451
KOiK01897
OMAiKTQVKHV
PhylomeDBiP69451

Family and domain databases

InterProiView protein in InterPro
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti34 – 51ARYAD…EVMTF → GALRRSTCVCEYGGGNDL in AAA23752 (PubMed:1460045).CuratedAdd BLAST18
Sequence conflicti468 – 490NEIED…VGVPS → TRLKMSSCSMVAYRKSRLLA YLP in AAA23752 (PubMed:1460045).CuratedAdd BLAST23
Sequence conflicti496A → G in AAA23752 (PubMed:1460045).Curated1
Sequence conflicti555 – 561GKVDNKA → QSGQ in AAA23752 (PubMed:1460045).Curated7

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
WP_000758422.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74875; AAC74875; b1805
BAA15609; BAA15609; BAA15609
GeneIDi946327
KEGGiecj:JW1794
eco:b1805
PATRICifig|511145.12.peg.1881

Similar proteinsi

Entry informationi

Entry nameiLCFA_ECOLI
AccessioniPrimary (citable) accession number: P69451
Secondary accession number(s): P29212
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: April 25, 2018
This is version 107 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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