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Reviewed, UniProtKB/Swiss-Prot Q2YV52 (PFLA_STAAB)

Last modified June 16, 2009. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pyruvate formate-lyase-activating enzyme
      Short name=PFL-activating enzyme
    EC=1.97.1.4
Gene names
Name: pflA
Ordered Locus Names: SAB0165
OrganismStaphylococcus aureus (strain bovine RF122 / ET3-1) [Complete proteome] [HAMAP]
Taxonomic identifier273036 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Activation of pyruvate formate-lyase 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Pyruvate formate-lyase-activating enzyme
PRO_0000271710

Sites

Metal binding291Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding331Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding361Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YV52-1 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 892A603E273F6C89

FASTA25128,499
        10         20         30         40         50         60 
MLKGHLHSVE SLGTVDGPGL RYILFTQGCL LRCLYCHNPD TWKISEPSRE VTVDEMVNEI 

        70         80         90        100        110        120 
LPYKPYFDAS GGGVTVSGGE PLLQMPFLEK LFAELKENGV HTCLDTSAGC ANDTKAFQRH 

       130        140        150        160        170        180 
FEELQKHTDL ILLDIKHIDN DKHIRLTGKP NTHILNFARK LSDMKQPVWI RHVLVPGYSD 

       190        200        210        220        230        240 
DKDDLIKLGE FINSLDNVEK FEILPYHQLG VHKWKTLGIA YELEDVEAPD DEAVKAAYRY 

       250 
VNFKGKIPVE L 

« Hide

References

[1]"Molecular correlates of host specialization in Staphylococcus aureus."
Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.
PLoS ONE 2:E1120-E1120(2007) [PubMed: 17971880] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AJ938182 Genomic DNA. Translation: CAI79853.1.
RefSeqYP_415675.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3794307.
GenomeReviewsGene locus SAB0165 in contig AJ938182_GR.
KEGGsab:SAB0165.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2YV52.
OMAQ2YV52. RFVVFMQ.

Enzyme and pathway databases

BioCycSAUR273036:SAB0165-MON.

Family and domain databases

InterProIPR012838. PFLA.
IPR001989. Radical_activat_CS.
IPR007197. Radical_SAM.
[Graphical view]
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
TIGRFAMsTIGR02493. PFLA. 1 hit.
PROSITEPS01087. RADICAL_ACTIVATING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFLA_STAAB
AccessionPrimary (citable) accession number: Q2YV52
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: December 20, 2005
Last modified: June 16, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents