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Protein

2,4-dienoyl-CoA reductase [NADPH]

Gene

fadH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi335Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi338Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi342Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi354Iron-sulfur (4Fe-4S)By similarity1

GO - Molecular functioni

  • 2,4-dienoyl-CoA reductase (NADPH) activity Source: EcoCyc
  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • FAD binding Source: EcoCyc
  • FMN binding Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • NADPH dehydrogenase activity Source: GO_Central

GO - Biological processi

  • fatty acid beta-oxidation, unsaturated, even number, reductase/isomerase pathway Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NADP

Enzyme and pathway databases

BioCyciEcoCyc:DIENOYLCOAREDUCT-MONOMER.
ECOL316407:JW3052-MONOMER.
MetaCyc:DIENOYLCOAREDUCT-MONOMER.
BRENDAi1.3.1.34. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
2,4-dienoyl-CoA reductase [NADPH] (EC:1.3.1.34)
Alternative name(s):
2,4-dienoyl coenzyme A reductase
Gene namesi
Name:fadH
Synonyms:ygjL
Ordered Locus Names:b3081, JW3052
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12723. fadH.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001944822 – 6722,4-dienoyl-CoA reductase [NADPH]Add BLAST671

Proteomic databases

PaxDbiP42593.
PRIDEiP42593.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4261984. 13 interactors.
DIPiDIP-9562N.
IntActiP42593. 10 interactors.
STRINGi511145.b3081.

Structurei

Secondary structure

1672
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 7Combined sources4
Beta strandi16 – 23Combined sources8
Helixi36 – 49Combined sources14
Beta strandi53 – 64Combined sources12
Helixi78 – 80Combined sources3
Helixi81 – 93Combined sources13
Beta strandi98 – 102Combined sources5
Helixi106 – 108Combined sources3
Beta strandi109 – 111Combined sources3
Beta strandi115 – 119Combined sources5
Helixi134 – 153Combined sources20
Beta strandi157 – 163Combined sources7
Helixi168 – 173Combined sources6
Turni175 – 177Combined sources3
Beta strandi185 – 187Combined sources3
Helixi188 – 206Combined sources19
Beta strandi208 – 219Combined sources12
Helixi228 – 241Combined sources14
Beta strandi244 – 250Combined sources7
Beta strandi259 – 261Combined sources3
Turni266 – 269Combined sources4
Helixi270 – 276Combined sources7
Beta strandi284 – 286Combined sources3
Helixi293 – 301Combined sources9
Beta strandi306 – 311Combined sources6
Helixi313 – 316Combined sources4
Helixi320 – 325Combined sources6
Helixi329 – 331Combined sources3
Turni340 – 342Combined sources3
Helixi343 – 347Combined sources5
Turni358 – 361Combined sources4
Turni363 – 365Combined sources3
Beta strandi376 – 380Combined sources5
Helixi384 – 394Combined sources11
Turni395 – 397Combined sources3
Beta strandi399 – 409Combined sources11
Helixi413 – 416Combined sources4
Helixi425 – 439Combined sources15
Beta strandi442 – 446Combined sources5
Beta strandi451 – 454Combined sources4
Beta strandi457 – 462Combined sources6
Beta strandi466 – 468Combined sources3
Turni475 – 477Combined sources3
Beta strandi481 – 483Combined sources3
Helixi484 – 488Combined sources5
Beta strandi496 – 501Combined sources6
Helixi504 – 514Combined sources11
Helixi521 – 523Combined sources3
Helixi525 – 531Combined sources7
Helixi541 – 543Combined sources3
Beta strandi555 – 561Combined sources7
Turni568 – 571Combined sources4
Turni574 – 576Combined sources3
Helixi577 – 586Combined sources10
Beta strandi590 – 592Combined sources3
Beta strandi596 – 601Combined sources6
Beta strandi604 – 609Combined sources6
Beta strandi612 – 616Combined sources5
Beta strandi619 – 623Combined sources5
Beta strandi627 – 629Combined sources3
Helixi634 – 638Combined sources5
Turni639 – 641Combined sources3
Beta strandi644 – 646Combined sources3
Helixi648 – 650Combined sources3
Helixi658 – 671Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PS9X-ray2.20A2-672[»]
ProteinModelPortaliP42593.
SMRiP42593.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42593.

Family & Domainsi

Domaini

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

Phylogenomic databases

eggNOGiENOG4105CCY. Bacteria.
COG0446. LUCA.
COG1902. LUCA.
HOGENOMiHOG000237760.
InParanoidiP42593.
KOiK00219.
OMAiSEVIRQN.
PhylomeDBiP42593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR013785. Aldolase_TIM.
IPR023753. FAD/NAD-binding_dom.
IPR001155. OxRdtase_FMN_N.
[Graphical view]
PfamiPF00724. Oxidored_FMN. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P42593-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYPSLFAPL DLGFTTLKNR VLMGSMHTGL EEYPDGAERL AAFYAERARH
60 70 80 90 100
GVALIVSGGI APDLTGVGME GGAMLNDASQ IPHHRTITEA VHQEGGKIAL
110 120 130 140 150
QILHTGRYSY QPHLVAPSAL QAPINRFVPH ELSHEEILQL IDNFARCAQL
160 170 180 190 200
AREAGYDGVE VMGSEGYLIN EFLTLRTNQR SDQWGGDYRN RMRFAVEVVR
210 220 230 240 250
AVRERVGNDF IIIYRLSMLD LVEDGGTFAE TVELAQAIEA AGATIINTGI
260 270 280 290 300
GWHEARIPTI ATPVPRGAFS WVTRKLKGHV SLPLVTTNRI NDPQVADDIL
310 320 330 340 350
SRGDADMVSM ARPFLADAEL LSKAQSGRAD EINTCIGCNQ ACLDQIFVGK
360 370 380 390 400
VTSCLVNPRA CHETKMPILP AVQKKNLAVV GAGPAGLAFA INAAARGHQV
410 420 430 440 450
TLFDAHSEIG GQFNIAKQIP GKEEFYETLR YYRRMIEVTG VTLKLNHTVT
460 470 480 490 500
ADQLQAFDET ILASGIVPRT PPIDGIDHPK VLSYLDVLRD KAPVGNKVAI
510 520 530 540 550
IGCGGIGFDT AMYLSQPGES TSQNIAGFCN EWGIDSSLQQ AGGLSPQGMQ
560 570 580 590 600
IPRSPRQIVM LQRKASKPGQ GLGKTTGWIH RTTLLSRGVK MIPGVSYQKI
610 620 630 640 650
DDDGLHVVIN GETQVLAVDN VVICAGQEPN RALAQPLIDS GKTVHLIGGC
660 670
DVAMELDARR AIAQGTRLAL EI
Length:672
Mass (Da):72,678
Last modified:January 23, 2007 - v3
Checksum:iB26C7CAAACE760C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93405 Genomic DNA. Translation: AAB82738.1.
U18997 Genomic DNA. Translation: AAA57882.1.
U00096 Genomic DNA. Translation: AAC76116.1.
AP009048 Genomic DNA. Translation: BAE77131.1.
PIRiF65096.
RefSeqiNP_417552.1. NC_000913.3.
WP_000121433.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76116; AAC76116; b3081.
BAE77131; BAE77131; BAE77131.
GeneIDi947594.
KEGGiecj:JW3052.
eco:b3081.
PATRICi32121580. VBIEscCol129921_3176.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93405 Genomic DNA. Translation: AAB82738.1.
U18997 Genomic DNA. Translation: AAA57882.1.
U00096 Genomic DNA. Translation: AAC76116.1.
AP009048 Genomic DNA. Translation: BAE77131.1.
PIRiF65096.
RefSeqiNP_417552.1. NC_000913.3.
WP_000121433.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PS9X-ray2.20A2-672[»]
ProteinModelPortaliP42593.
SMRiP42593.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261984. 13 interactors.
DIPiDIP-9562N.
IntActiP42593. 10 interactors.
STRINGi511145.b3081.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Proteomic databases

PaxDbiP42593.
PRIDEiP42593.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76116; AAC76116; b3081.
BAE77131; BAE77131; BAE77131.
GeneIDi947594.
KEGGiecj:JW3052.
eco:b3081.
PATRICi32121580. VBIEscCol129921_3176.

Organism-specific databases

EchoBASEiEB2582.
EcoGeneiEG12723. fadH.

Phylogenomic databases

eggNOGiENOG4105CCY. Bacteria.
COG0446. LUCA.
COG1902. LUCA.
HOGENOMiHOG000237760.
InParanoidiP42593.
KOiK00219.
OMAiSEVIRQN.
PhylomeDBiP42593.

Enzyme and pathway databases

BioCyciEcoCyc:DIENOYLCOAREDUCT-MONOMER.
ECOL316407:JW3052-MONOMER.
MetaCyc:DIENOYLCOAREDUCT-MONOMER.
BRENDAi1.3.1.34. 2026.

Miscellaneous databases

EvolutionaryTraceiP42593.
PROiP42593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR013785. Aldolase_TIM.
IPR023753. FAD/NAD-binding_dom.
IPR001155. OxRdtase_FMN_N.
[Graphical view]
PfamiPF00724. Oxidored_FMN. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFADH_ECOLI
AccessioniPrimary (citable) accession number: P42593
Secondary accession number(s): Q2M9C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 148 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.