Q6GCP9 (PFLA_STAAS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate formate-lyase-activating enzyme
Short name=PFL-activating enzyme
EC=1.97.1.4

Gene names

Name:	pflA
Ordered Locus Names:	SAS0202

Organism

Staphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP]

Taxonomic identifier

282459 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	251 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Cytoplasm
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW [formate-C-acetyltransferase]-activating enzyme activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 251	251	Pyruvate formate-lyase-activating enzyme		PRO_0000271715
Sites
	Metal binding	29	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	33	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	36	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6GCP9 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 892A603E273F6C89	FASTA	251	28,499
	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

References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MSSA476.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571857 Genomic DNA. Translation: CAG41970.1.
RefSeq	YP_042324.1. NC_002953.3.
3D structure databases
ProteinModelPortal	Q6GCP9.
SMR	Q6GCP9. Positions 71-207.
ModBase	Search...
Protein-protein interaction databases
STRING	282459.SAS0202.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2864326.
KEGG	sas:SAS0202.
PATRIC	19549750. VBIStaAur96780_0213.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1180.
HOGENOM	HOG000011458.
KO	K04069.
OMA	ILESYGH.
ProtClustDB	CLSK884495.
Family and domain databases
InterPro	IPR012838. PFL_activating. IPR001989. Radical_activat_CS. IPR007197. rSAM. [Graphical view]
Pfam	PF04055. Radical_SAM. 1 hit. [Graphical view]
TIGRFAMs	TIGR02493. PFLA. 1 hit.
PROSITE	PS01087. RADICAL_ACTIVATING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PFLA_STAAS

Accession

Primary (citable) accession number: Q6GCP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program