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Protein

Short-chain-fatty-acid--CoA ligase

Gene

fadK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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. It has a low activity on medium or long chain fatty acids and is maximally active on C6 and C8 substrates.

Catalytic activityi

ATP + a short-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.

Regions

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

GO - Molecular functioni

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

GO - Biological processi

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:EG12357-MONOMER.
ECOL316407:JW5910-MONOMER.
MetaCyc:EG12357-MONOMER.

Chemistry

SwissLipidsiSLP:000000973.

Names & Taxonomyi

Protein namesi
Recommended name:
Short-chain-fatty-acid--CoA ligase (EC:6.2.1.-)
Alternative name(s):
Acyl-CoA synthetase
Gene namesi
Name:fadK
Synonyms:ydiD
Ordered Locus Names:b1701, JW5910
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12357. fadK.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 548548Short-chain-fatty-acid--CoA ligasePRO_0000193132Add
BLAST

Proteomic databases

PaxDbiP38135.
PRIDEiP38135.

Expressioni

Inductioni

Expression independent of FadR. The levels of expression vary with the terminal electron acceptor (nitrate, fumarate). FadK is not expressed under aerobic growth conditions and it could functionally replace FadD under anaerobic conditions.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi4260285. 308 interactions.
STRINGi511145.b1701.

Structurei

3D structure databases

ProteinModelPortaliP38135.
SMRiP38135. Positions 15-538.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000230000.
InParanoidiP38135.
KOiK12507.
OMAiENFIESH.
OrthoDBiEOG6MH5BV.
PhylomeDBiP38135.

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.

P38135-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVTLTFNEQ RRAAYRQQGL WGDASLADYW QQTARAMPDK IAVVDNHGAS
60 70 80 90 100
YTYSALDHAA SCLANWMLAK GIESGDRIAF QLPGWCEFTV IYLACLKIGA
110 120 130 140 150
VSVPLLPSWR EAELVWVLNK CQAKMFFAPT LFKQTRPVDL ILPLQNQLPQ
160 170 180 190 200
LQQIVGVDKL APATSSLSLS QIIADNTSLT TAITTHGDEL AAVLFTSGTE
210 220 230 240 250
GLPKGVMLTH NNILASERAY CARLNLTWQD VFMMPAPLGH ATGFLHGVTA
260 270 280 290 300
PFLIGARSVL LDIFTPDACL ALLEQQRCTC MLGATPFVYD LLNVLEKQPA
310 320 330 340 350
DLSALRFFLC GGTTIPKKVA RECQQRGIKL LSVYGSTESS PHAVVNLDDP
360 370 380 390 400
LSRFMHTDGY AAAGVEIKVV DDARKTLPPG CEGEEASRGP NVFMGYFDEP
410 420 430 440 450
ELTARALDEE GWYYSGDLCR MDEAGYIKIT GRKKDIIVRG GENISSREVE
460 470 480 490 500
DILLQHPKIH DACVVAMSDE RLGERSCAYV VLKAPHHSLS LEEVVAFFSR
510 520 530 540
KRVAKYKYPE HIVVIEKLPR TTSGKIQKFL LRKDIMRRLT QDVCEEIE
Length:548
Mass (Da):60,773
Last modified:July 15, 1998 - v3
Checksum:i221C68C6A16DCDF1
GO

Sequence cautioni

The sequence BAA15470.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.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.
AP009048 Genomic DNA. Translation: BAA15470.2. Different initiation.
M69116 Genomic DNA. No translation available.
PIRiE64928.
RefSeqiNP_416216.4. NC_000913.3.
WP_001336282.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74771; AAC74771; b1701.
BAA15470; BAA15470; BAA15470.
GeneIDi946213.
KEGGiecj:JW5910.
eco:b1701.
PATRICi32118708. VBIEscCol129921_1772.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74771.2.
AP009048 Genomic DNA. Translation: BAA15470.2. Different initiation.
M69116 Genomic DNA. No translation available.
PIRiE64928.
RefSeqiNP_416216.4. NC_000913.3.
WP_001336282.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP38135.
SMRiP38135. Positions 15-538.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260285. 308 interactions.
STRINGi511145.b1701.

Chemistry

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.
PATRICi32118708. VBIEscCol129921_1772.

Organism-specific databases

EchoBASEiEB2260.
EcoGeneiEG12357. fadK.

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000230000.
InParanoidiP38135.
KOiK12507.
OMAiENFIESH.
OrthoDBiEOG6MH5BV.
PhylomeDBiP38135.

Enzyme and pathway databases

BioCyciEcoCyc:EG12357-MONOMER.
ECOL316407:JW5910-MONOMER.
MetaCyc:EG12357-MONOMER.

Miscellaneous databases

PROiP38135.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "The cloning and sequence of the E. coli pps gene."
    Holzschu D.L., McElver J.A., Liao C.C., Berry A.
    Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 356-548.
    Strain: K12.
  5. "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome."
    Borodovsky M., Rudd K.E., Koonin E.V.
    Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  6. "A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway."
    Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr.
    Mol. Microbiol. 47:793-805(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ANAEROBIC BETA-OXIDATION PATHWAY.
    Strain: K12 / MG1655 / ATCC 47076.
  7. "The Escherichia coli fadK (ydiD) gene encodes an anerobically regulated short chain acyl-CoA synthetase."
    Morgan-Kiss R.M., Cronan J.E.
    J. Biol. Chem. 279:37324-37333(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.

Entry informationi

Entry nameiFADK_ECOLI
AccessioniPrimary (citable) accession number: P38135
Secondary accession number(s): P76202, P76902, P76903
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 15, 1998
Last modified: January 20, 2016
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

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 one 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.