Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Medium-chain fatty-acid--CoA ligase

Gene

fadK

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

Functioni

Catalyzes the esterification, concomitant with transport, of exogenous fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Is maximally active on C6:0, C8:0 and C12:0 fatty acids, while has a low activity on C14-C18 chain length fatty acids (PubMed:15213221, PubMed:19477415). Is involved in the anaerobic beta-oxidative degradation of fatty acids, which allows anaerobic growth of E.coli on fatty acids as a sole carbon and energy source in the presence of nitrate or fumarate as a terminal electron acceptor (PubMed:12535077). Can functionally replace FadD under anaerobic conditions (PubMed:12535077).3 Publications

Miscellaneous

Probably starts on Met-1; overexpressed protein starting at Met-19 has lower activity, forms aggregates during reaction and is unstable in storage at -80 degrees Celsius (PubMed:15213221).1 Publication
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 + hexanoate + CoA = AMP + diphosphate + hexanoyl-CoA.1 Publication
ATP + octanoate + CoA = AMP + diphosphate + octanoyl-CoA.2 Publications
ATP + dodecanoate + CoA = AMP + diphosphate + dodecanoyl-CoA.1 Publication

Cofactori

Mg2+1 Publication

pH dependencei

Optimum pH is 7.7-8.2.1 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 bindingi231 – 242ATPBy similarityAdd BLAST12

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • medium-chain fatty acid-CoA ligase activity Source: EcoCyc

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:EG12357-MONOMER
MetaCyc:EG12357-MONOMER
UniPathwayi
UPA00659

Chemistry databases

SwissLipidsiSLP:000000973

Names & Taxonomyi

Protein namesi
Recommended name:
Medium-chain fatty-acid--CoA ligase2 Publications (EC:6.2.1.-2 Publications)
Alternative name(s):
Acyl-CoA synthetase1 Publication
Short name:
ACS1 Publication
Fatty acyl-CoA synthetase FadKCurated
Gene namesi
Name:fadK1 Publication
Synonyms:ydiD
Ordered Locus Names:b1701, JW5910
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12357 fadK

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene grow normally on aerobic oleate plates, but grow relatively poorly on oleate plus nitrate plates under anaerobic conditions. 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001931321 – 566Medium-chain fatty-acid--CoA ligaseAdd BLAST566

Proteomic databases

PaxDbiP38135
PRIDEiP38135

Expressioni

Inductioni

Expression independent of FadR (PubMed:12535077). FadK is not expressed under aerobic growth conditions, the levels of anaerobic expression vary with the terminal electron acceptor, with more expression during growth on fumarate than on nitrate (at protein level) (PubMed:15213221).2 Publications

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi4260285, 308 interactors
STRINGi316385.ECDH10B_1837

Structurei

3D structure databases

ProteinModelPortaliP38135
SMRiP38135
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CEY Bacteria
COG0318 LUCA
HOGENOMiHOG000230000
InParanoidiP38135
KOiK12507

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.

P38135-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHPTGPHLGP DVLFRESNMK VTLTFNEQRR AAYRQQGLWG DASLADYWQQ
60 70 80 90 100
TARAMPDKIA VVDNHGASYT YSALDHAASC LANWMLAKGI ESGDRIAFQL
110 120 130 140 150
PGWCEFTVIY LACLKIGAVS VPLLPSWREA ELVWVLNKCQ AKMFFAPTLF
160 170 180 190 200
KQTRPVDLIL PLQNQLPQLQ QIVGVDKLAP ATSSLSLSQI IADNTSLTTA
210 220 230 240 250
ITTHGDELAA VLFTSGTEGL PKGVMLTHNN ILASERAYCA RLNLTWQDVF
260 270 280 290 300
MMPAPLGHAT GFLHGVTAPF LIGARSVLLD IFTPDACLAL LEQQRCTCML
310 320 330 340 350
GATPFVYDLL NVLEKQPADL SALRFFLCGG TTIPKKVARE CQQRGIKLLS
360 370 380 390 400
VYGSTESSPH AVVNLDDPLS RFMHTDGYAA AGVEIKVVDD ARKTLPPGCE
410 420 430 440 450
GEEASRGPNV FMGYFDEPEL TARALDEEGW YYSGDLCRMD EAGYIKITGR
460 470 480 490 500
KKDIIVRGGE NISSREVEDI LLQHPKIHDA CVVAMSDERL GERSCAYVVL
510 520 530 540 550
KAPHHSLSLE EVVAFFSRKR VAKYKYPEHI VVIEKLPRTT SGKIQKFLLR
560
KDIMRRLTQD VCEEIE
Length:566
Mass (Da):62,759
Last modified:September 7, 2016 - v4
Checksum:i057236D5F7F2FCE7
GO

Sequence cautioni

The sequence AAC74771 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence M69116 differs from that shown. Reason: Frameshift at several positions.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC74771.2 Different initiation.
AP009048 Genomic DNA Translation: BAA15470.2
M69116 Genomic DNA No translation available.
PIRiE64928
RefSeqiNP_416216.4, NC_000913.3

Genome annotation databases

EnsemblBacteriaiAAC74771; AAC74771; b1701
BAA15470; BAA15470; BAA15470
GeneIDi946213
KEGGiecj:JW5910
eco:b1701
PATRICifig|511145.12.peg.1772

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC74771.2 Different initiation.
AP009048 Genomic DNA Translation: BAA15470.2
M69116 Genomic DNA No translation available.
PIRiE64928
RefSeqiNP_416216.4, NC_000913.3

3D structure databases

ProteinModelPortaliP38135
SMRiP38135
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260285, 308 interactors
STRINGi316385.ECDH10B_1837

Chemistry databases

SwissLipidsiSLP:000000973

Proteomic databases

PaxDbiP38135
PRIDEiP38135

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74771; AAC74771; b1701
BAA15470; BAA15470; BAA15470
GeneIDi946213
KEGGiecj:JW5910
eco:b1701
PATRICifig|511145.12.peg.1772

Organism-specific databases

EchoBASEiEB2260
EcoGeneiEG12357 fadK

Phylogenomic databases

eggNOGiENOG4105CEY Bacteria
COG0318 LUCA
HOGENOMiHOG000230000
InParanoidiP38135
KOiK12507

Enzyme and pathway databases

UniPathwayi
UPA00659

BioCyciEcoCyc:EG12357-MONOMER
MetaCyc:EG12357-MONOMER

Miscellaneous databases

PROiPR:P38135

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
ProtoNetiSearch...

Entry informationi

Entry nameiFADK_ECOLI
AccessioniPrimary (citable) accession number: P38135
Secondary accession number(s): P76202, P76902, P76903
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: September 7, 2016
Last modified: November 22, 2017
This is version 128 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again