Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0A9N5 (PFLA_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
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
Ordered Locus Names:c1038
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 By similarity.

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 By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the organic radical-activating enzymes family.

Sequence caution

The sequence AAN79510.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 246245Pyruvate formate-lyase 1-activating enzyme
PRO_0000200524

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

Sequences

Sequence LengthMass (Da)Tools
P0A9N5 [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

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN79510.1. Different initiation.
RefSeqNP_752967.2. NC_004431.1.

3D structure databases

ProteinModelPortalP0A9N5.
SMRP0A9N5. Positions 2-246.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c1038.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN79510; AAN79510; c1038.
GeneID1038676.
KEGGecc:c1038.
PATRIC18280119. VBIEscCol75197_0988.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000011458.
KOK04069.
OMADDASAHK.
OrthoDBEOG64FKHC.

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...

Entry information

Entry namePFLA_ECOL6
AccessionPrimary (citable) accession number: P0A9N5
Secondary accession number(s): P09374
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 62 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