P38135 (FADK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Short-chain-fatty-acid--CoA ligase
EC=6.2.1.-

Alternative name(s):
Acyl-CoA synthetase

Gene names

Name:	fadK
Synonyms:	ydiD
Ordered Locus Names:	b1701, JW5910

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	548 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	ATP + a short-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.
Subunit structure	Homodimer By similarity.
Subcellular location	Membrane; Peripheral membrane protein. Note: Partially membrane-associated.
Induction	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.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.
Sequence caution	The sequence BAA15470.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence M69116 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid oxidation Inferred from experiment Ref.6. Source: EcoCyc
Cellular_component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW short-chain fatty acid-CoA ligase activity Inferred from experiment Ref.6. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 548	548	Short-chain-fatty-acid--CoA ligase		PRO_0000193132
Regions
	Nucleotide binding	213 – 224	12	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P38135 [UniParc]. Last modified July 15, 1998. Version 3. Checksum: 221C68C6A16DCDF1	FASTA	548	60,773
	10 20 30 40 50 60 MKVTLTFNEQ RRAAYRQQGL WGDASLADYW QQTARAMPDK IAVVDNHGAS YTYSALDHAA 70 80 90 100 110 120 SCLANWMLAK GIESGDRIAF QLPGWCEFTV IYLACLKIGA VSVPLLPSWR EAELVWVLNK 130 140 150 160 170 180 CQAKMFFAPT LFKQTRPVDL ILPLQNQLPQ LQQIVGVDKL APATSSLSLS QIIADNTSLT 190 200 210 220 230 240 TAITTHGDEL AAVLFTSGTE GLPKGVMLTH NNILASERAY CARLNLTWQD VFMMPAPLGH 250 260 270 280 290 300 ATGFLHGVTA PFLIGARSVL LDIFTPDACL ALLEQQRCTC MLGATPFVYD LLNVLEKQPA 310 320 330 340 350 360 DLSALRFFLC GGTTIPKKVA RECQQRGIKL LSVYGSTESS PHAVVNLDDP LSRFMHTDGY 370 380 390 400 410 420 AAAGVEIKVV DDARKTLPPG CEGEEASRGP NVFMGYFDEP ELTARALDEE GWYYSGDLCR 430 440 450 460 470 480 MDEAGYIKIT GRKKDIIVRG GENISSREVE DILLQHPKIH DACVVAMSDE RLGERSCAYV 490 500 510 520 530 540 VLKAPHHSLS LEEVVAFFSR KRVAKYKYPE HIVVIEKLPR TTSGKIQKFL LRKDIMRRLT QDVCEEIE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC74771.2. AP009048 Genomic DNA. Translation: BAA15470.2. Different initiation. M69116 Genomic DNA. No translation available.
PIR	E64928.
RefSeq	NP_416216.4. NC_000913.2. YP_489963.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P38135.
SMR	P38135. Positions 15-538.
ModBase	Search...
Protein-protein interaction databases
STRING	511145.b1701.
Proteomic databases
PRIDE	P38135.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74771; AAC74771; b1701. BAA15470; BAA15470; BAA15470.
GeneID	12931291. 946213.
KEGG	ecj:Y75_p1676. eco:b1701.
PATRIC	32118708. VBIEscCol129921_1772.
Organism-specific databases
EchoBASE	EB2260.
EcoGene	EG12357. fadK.
Phylogenomic databases
eggNOG	COG0318.
HOGENOM	HOG000230000.
KO	K12507.
OMA	SERAYCV.
ProtClustDB	PRK06087.
Enzyme and pathway databases
BioCyc	EcoCyc:EG12357-MONOMER. ECOL316407:JW5910-MONOMER. MetaCyc:EG12357-MONOMER.
Gene expression databases
Genevestigator	P38135.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR025110. DUF4009. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. PF13193. DUF4009. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADK_ECOLI

Accession

Primary (citable) accession number: P38135
Secondary accession number(s): P76202, P76902, P76903

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	July 15, 1998
Last modified:	May 1, 2013
This is version 101 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program