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P0A9N4 (PFLA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate formate-lyase 1-activating enzyme

EC=1.97.1.4
Alternative name(s):
Formate-C-acetyltransferase-activating enzyme 1
PFL-activating enzyme 1
Gene names
Name:pflA
Synonyms:act
Ordered Locus Names:b0902, JW0885
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activation of pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.

Catalytic activity

S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.

Cofactor

Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the organic radical-activating enzymes family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ydcYP644554EBI-1114060,EBI-9129853

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 246245Pyruvate formate-lyase 1-activating enzyme
PRO_0000200522

Sites

Metal binding301Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding341Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding371Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Secondary structure

............................................ 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A9N4 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 486E06A9CE97BF37

FASTA24628,204
        10         20         30         40         50         60 
MSVIGRIHSF ESCGTVDGPG IRFITFFQGC LMRCLYCHNR DTWDTHGGKE VTVEDLMKEV 

        70         80         90        100        110        120 
VTYRHFMNAS GGGVTASGGE AILQAEFVRD WFRACKKEGI HTCLDTNGFV RRYDPVIDEL 

       130        140        150        160        170        180 
LEVTDLVMLD LKQMNDEIHQ NLVGVSNHRT LEFAKYLANK NVKVWIRYVV VPGWSDDDDS 

       190        200        210        220        230        240 
AHRLGEFTRD MGNVEKIELL PYHELGKHKW VAMGEEYKLD GVKPPKKETM ERVKGILEQY 


GHKVMF 

« Hide

References

« Hide 'large scale' references
[1]"Primary structures of Escherichia coli pyruvate formate-lyase and pyruvate-formate-lyase-activating enzyme deduced from the DNA nucleotide sequences."
Roedel W., Plaga W., Frank R., Knappe J.
Eur. J. Biochem. 177:153-158(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: K12.
[2]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"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.
[4]"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
X08035 Genomic DNA. Translation: CAA30829.1.
U00096 Genomic DNA. Translation: AAC73988.1.
AP009048 Genomic DNA. Translation: BAA35637.1.
PIRS01789.
RefSeqNP_415422.1. NC_000913.3.
YP_489174.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3C8FX-ray2.25A2-246[»]
3CB8X-ray2.77A2-246[»]
ProteinModelPortalP0A9N4.
SMRP0A9N4. Positions 2-246.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35915N.
IntActP0A9N4. 19 interactions.
STRING511145.b0902.

Proteomic databases

PaxDbP0A9N4.
PRIDEP0A9N4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73988; AAC73988; b0902.
BAA35637; BAA35637; BAA35637.
GeneID12930359.
945517.
KEGGecj:Y75_p0874.
eco:b0902.
PATRIC32117017. VBIEscCol129921_0933.

Organism-specific databases

EchoBASEEB0027.
EcoGeneEG10028. pflA.

Phylogenomic databases

eggNOGCOG1180.
HOGENOMHOG000011458.
KOK04069.
OMAQNLIGVP.
OrthoDBEOG64FKHC.
PhylomeDBP0A9N4.
ProtClustDBPRK11145.

Enzyme and pathway databases

BioCycEcoCyc:PFLACTENZ-MONOMER.
ECOL316407:JW0885-MONOMER.

Gene expression databases

GenevestigatorP0A9N4.

Family and domain databases

InterProIPR006638. Elp3/MiaB/NifB.
IPR012838. PFL_activating.
IPR001989. Radical_activat_CS.
IPR007197. rSAM.
[Graphical view]
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR02493. PFLA. 1 hit.
PROSITEPS01087. RADICAL_ACTIVATING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A9N4.
PROP0A9N4.

Entry information

Entry namePFLA_ECOLI
AccessionPrimary (citable) accession number: P0A9N4
Secondary accession number(s): P09374
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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