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P42593

- FADH_ECOLI

UniProt

P42593 - FADH_ECOLI

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Protein

2,4-dienoyl-CoA reductase [NADPH]

Gene

fadH

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi335 – 3351Iron-sulfur (4Fe-4S)By similarity
Metal bindingi338 – 3381Iron-sulfur (4Fe-4S)By similarity
Metal bindingi342 – 3421Iron-sulfur (4Fe-4S)By similarity
Metal bindingi354 – 3541Iron-sulfur (4Fe-4S)By similarity

GO - Molecular functioni

  1. 2,4-dienoyl-CoA reductase (NADPH) activity Source: EcoCyc
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. FMN binding Source: InterPro
  4. metal ion binding Source: UniProtKB-KW
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.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG12723. fadH.

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 6726712,4-dienoyl-CoA reductase [NADPH]PRO_0000194482Add
BLAST

Proteomic databases

PRIDEiP42593.

Expressioni

Gene expression databases

GenevestigatoriP42593.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

DIPiDIP-9562N.
IntActiP42593. 10 interactions.
STRINGi511145.b3081.

Structurei

Secondary structure

1
672
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 74Combined sources
Beta strandi16 – 238Combined sources
Helixi36 – 4914Combined sources
Beta strandi53 – 6412Combined sources
Helixi78 – 803Combined sources
Helixi81 – 9313Combined sources
Beta strandi98 – 1025Combined sources
Helixi106 – 1083Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi115 – 1195Combined sources
Helixi134 – 15320Combined sources
Beta strandi157 – 1637Combined sources
Helixi168 – 1736Combined sources
Turni175 – 1773Combined sources
Beta strandi185 – 1873Combined sources
Helixi188 – 20619Combined sources
Beta strandi208 – 21912Combined sources
Helixi228 – 24114Combined sources
Beta strandi244 – 2507Combined sources
Beta strandi259 – 2613Combined sources
Turni266 – 2694Combined sources
Helixi270 – 2767Combined sources
Beta strandi284 – 2863Combined sources
Helixi293 – 3019Combined sources
Beta strandi306 – 3116Combined sources
Helixi313 – 3164Combined sources
Helixi320 – 3256Combined sources
Helixi329 – 3313Combined sources
Turni340 – 3423Combined sources
Helixi343 – 3475Combined sources
Turni358 – 3614Combined sources
Turni363 – 3653Combined sources
Beta strandi376 – 3805Combined sources
Helixi384 – 39411Combined sources
Turni395 – 3973Combined sources
Beta strandi399 – 40911Combined sources
Helixi413 – 4164Combined sources
Helixi425 – 43915Combined sources
Beta strandi442 – 4465Combined sources
Beta strandi451 – 4544Combined sources
Beta strandi457 – 4626Combined sources
Beta strandi466 – 4683Combined sources
Turni475 – 4773Combined sources
Beta strandi481 – 4833Combined sources
Helixi484 – 4885Combined sources
Beta strandi496 – 5016Combined sources
Helixi504 – 51411Combined sources
Helixi521 – 5233Combined sources
Helixi525 – 5317Combined sources
Helixi541 – 5433Combined sources
Beta strandi555 – 5617Combined sources
Turni568 – 5714Combined sources
Turni574 – 5763Combined sources
Helixi577 – 58610Combined sources
Beta strandi590 – 5923Combined sources
Beta strandi596 – 6016Combined sources
Beta strandi604 – 6096Combined sources
Beta strandi612 – 6165Combined sources
Beta strandi619 – 6235Combined sources
Beta strandi627 – 6293Combined sources
Helixi634 – 6385Combined sources
Turni639 – 6413Combined sources
Beta strandi644 – 6463Combined sources
Helixi648 – 6503Combined sources
Helixi658 – 67114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PS9X-ray2.20A2-672[»]
ProteinModelPortaliP42593.
SMRiP42593. Positions 2-672.
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

eggNOGiCOG1902.
HOGENOMiHOG000237760.
InParanoidiP42593.
KOiK00219.
OMAiIAEFCNE.
OrthoDBiEOG6VF2ZQ.
PhylomeDBiP42593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR001155. OxRdtase_FMN_N.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
[Graphical view]
PfamiPF00724. Oxidored_FMN. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.

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.
YP_491272.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76116; AAC76116; b3081.
BAE77131; BAE77131; BAE77131.
GeneIDi12932990.
947594.
KEGGiecj:Y75_p3006.
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 .
PIRi F65096.
RefSeqi NP_417552.1. NC_000913.3.
YP_491272.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PS9 X-ray 2.20 A 2-672 [» ]
ProteinModelPortali P42593.
SMRi P42593. Positions 2-672.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9562N.
IntActi P42593. 10 interactions.
STRINGi 511145.b3081.

Chemistry

DrugBanki DB03147. Flavin adenine dinucleotide.

Proteomic databases

PRIDEi P42593.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76116 ; AAC76116 ; b3081 .
BAE77131 ; BAE77131 ; BAE77131 .
GeneIDi 12932990.
947594.
KEGGi ecj:Y75_p3006.
eco:b3081.
PATRICi 32121580. VBIEscCol129921_3176.

Organism-specific databases

EchoBASEi EB2582.
EcoGenei EG12723. fadH.

Phylogenomic databases

eggNOGi COG1902.
HOGENOMi HOG000237760.
InParanoidi P42593.
KOi K00219.
OMAi IAEFCNE.
OrthoDBi EOG6VF2ZQ.
PhylomeDBi P42593.

Enzyme and pathway databases

BioCyci EcoCyc:DIENOYLCOAREDUCT-MONOMER.
ECOL316407:JW3052-MONOMER.
MetaCyc:DIENOYLCOAREDUCT-MONOMER.

Miscellaneous databases

EvolutionaryTracei P42593.
PROi P42593.

Gene expression databases

Genevestigatori P42593.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR001155. OxRdtase_FMN_N.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
[Graphical view ]
Pfami PF00724. Oxidored_FMN. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

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 26, 2014
This is version 134 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

External Data

Dasty 3