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P42593 (FADH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2,4-dienoyl-CoA reductase [NADPH]

EC=1.3.1.34
Alternative name(s):
2,4-dienoyl coenzyme A reductase
Gene names
Name:fadH
Synonyms:ygjL
Ordered Locus Names:b3081, JW3052
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length672 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-2- enoyl-CoA.

Catalytic activity

Trans-2,3-didehydroacyl-CoA + NADP+ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH.

Cofactor

FAD.

Subunit structure

Monomer.

Domain

The N-terminus may contain the FAD-binding domain whereas the NADPH-binding domain may be located in the C-terminus.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 6726712,4-dienoyl-CoA reductase [NADPH]
PRO_0000194482

Sites

Metal binding3351Iron-sulfur (4Fe-4S) By similarity
Metal binding3381Iron-sulfur (4Fe-4S) By similarity
Metal binding3421Iron-sulfur (4Fe-4S) By similarity
Metal binding3541Iron-sulfur (4Fe-4S) By similarity

Secondary structure

.......................................................................................................................... 672
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42593 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B26C7CAAACE760C3

FASTA67272,678
        10         20         30         40         50         60 
MSYPSLFAPL DLGFTTLKNR VLMGSMHTGL EEYPDGAERL AAFYAERARH GVALIVSGGI 

        70         80         90        100        110        120 
APDLTGVGME GGAMLNDASQ IPHHRTITEA VHQEGGKIAL QILHTGRYSY QPHLVAPSAL 

       130        140        150        160        170        180 
QAPINRFVPH ELSHEEILQL IDNFARCAQL AREAGYDGVE VMGSEGYLIN EFLTLRTNQR 

       190        200        210        220        230        240 
SDQWGGDYRN RMRFAVEVVR AVRERVGNDF IIIYRLSMLD LVEDGGTFAE TVELAQAIEA 

       250        260        270        280        290        300 
AGATIINTGI GWHEARIPTI ATPVPRGAFS WVTRKLKGHV SLPLVTTNRI NDPQVADDIL 

       310        320        330        340        350        360 
SRGDADMVSM ARPFLADAEL LSKAQSGRAD EINTCIGCNQ ACLDQIFVGK VTSCLVNPRA 

       370        380        390        400        410        420 
CHETKMPILP AVQKKNLAVV GAGPAGLAFA INAAARGHQV TLFDAHSEIG GQFNIAKQIP 

       430        440        450        460        470        480 
GKEEFYETLR YYRRMIEVTG VTLKLNHTVT ADQLQAFDET ILASGIVPRT PPIDGIDHPK 

       490        500        510        520        530        540 
VLSYLDVLRD KAPVGNKVAI IGCGGIGFDT AMYLSQPGES TSQNIAGFCN EWGIDSSLQQ 

       550        560        570        580        590        600 
AGGLSPQGMQ IPRSPRQIVM LQRKASKPGQ GLGKTTGWIH RTTLLSRGVK MIPGVSYQKI 

       610        620        630        640        650        660 
DDDGLHVVIN GETQVLAVDN VVICAGQEPN RALAQPLIDS GKTVHLIGGC DVAMELDARR 

       670 
AIAQGTRLAL EI 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of the fadH gene and characterization of the gene product 2,4-dienoyl coenzyme A reductase from Escherichia coli."
He X.-Y., Yang S.-Y., Schulz H.
Eur. J. Biochem. 248:516-520(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31.
Strain: K12.
[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 277:1453-1462(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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U93405 Genomic DNA. Translation: AAB82738.1.
U18997 Genomic DNA. Translation: AAA57882.1.
U00096 Genomic DNA. Translation: AAC76116.1.
AP009048 Genomic DNA. Translation: BAE77131.1.
PIRF65096.
RefSeqNP_417552.1. NC_000913.3.
YP_491272.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PS9X-ray2.20A2-671[»]
ProteinModelPortalP42593.
SMRP42593. Positions 2-672.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9562N.
IntActP42593. 10 interactions.
STRING511145.b3081.

Proteomic databases

PRIDEP42593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76116; AAC76116; b3081.
BAE77131; BAE77131; BAE77131.
GeneID12932990.
947594.
KEGGecj:Y75_p3006.
eco:b3081.
PATRIC32121580. VBIEscCol129921_3176.

Organism-specific databases

EchoBASEEB2582.
EcoGeneEG12723. fadH.

Phylogenomic databases

eggNOGCOG1902.
HOGENOMHOG000237760.
KOK00219.
OMANRFTPHE.
OrthoDBEOG6VF2ZQ.
PhylomeDBP42593.
ProtClustDBCLSK867750.

Enzyme and pathway databases

BioCycEcoCyc:DIENOYLCOAREDUCT-MONOMER.
ECOL316407:JW3052-MONOMER.
MetaCyc:DIENOYLCOAREDUCT-MONOMER.

Gene expression databases

GenevestigatorP42593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR001155. OxRdtase_FMN_N.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
[Graphical view]
PfamPF00724. Oxidored_FMN. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
ProtoNetSearch...

Other

EvolutionaryTraceP42593.
PROP42593.

Entry information

Entry nameFADH_ECOLI
AccessionPrimary (citable) accession number: P42593
Secondary accession number(s): Q2M9C5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene