Reviewed, UniProtKB/Swiss-Prot P0A442 (PFLA_LISMO)

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
Synonyms:	pflC
Ordered Locus Names:	lmo1407

Organism

Listeria monocytogenes [Complete proteome] [HAMAP]

Taxonomic identifier

1639 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxygen and reactive oxygen species metabolic process Inferred from electronic annotation. Source: InterPro
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 iron 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 – 248	248	Pyruvate formate-lyase-activating enzyme		PRO_0000200532
Sites
	Metal binding	31	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	35	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	38	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A442-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 0A6F5BBA95CBEBC9	FASTA	248	28,115
	10 20 30 40 50 60 MTEVLGRVHS VETMGTVDGP GIRFIVFMQG CLLRCQFCHN PDTWKIGTGT ERSAQDVFDE 70 80 90 100 110 120 AIKYKEFWDA SGGGVTVSGG EPLLQVDFLI EFFTLCKAAG VHTTIDSCGG CFTRDPEFIE 130 140 150 160 170 180 KLDRLMEVTD LILLDIKQIN PEKHLKLTTK SNAPIIDFAH YLRDKEQPIW IRHVLIPTKT 190 200 210 220 230 240 DDPEDLTKLH EFIQTLPNVK QVDVLPYHTM GVYKWKEMGI RYPLEGIEAP EEEVVALANK ILETSSYK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a new locus in Listeria monocytogenes involved in cellobiose-dependent repression of hly expression." Huillet E.E.H., Larpin S., Pardon P., Berche P. FEMS Microbiol. Lett. 174:265-272(1999) [PubMed: 10339818] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ009627 Genomic DNA. Translation: CAB43713.1. AL591979 Genomic DNA. Translation: CAC99485.1.
PIR	AG1250. T46708.
RefSeq	NP_464932.1. YP_002758115.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	7704049. 986485.
GenomeReviews	Gene locus lmo1407 in contig AL591824_GR.
KEGG	lmo:lmo1407.
Organism-specific databases
ListiList	LMO01407.
CMR	Search...
Phylogenomic databases
HOGENOM	P0A442.
OMA	P0A442. REENIST.
Enzyme and pathway databases
BioCyc	LMON169963:LMO1407-MON.
BRENDA	1.97.1.4. 96770.
Family and domain databases
InterPro	IPR012838. PFLA. IPR001989. Radical_activat_CS. IPR007197. Radical_SAM. [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_LISMO

Accession

Primary (citable) accession number: P0A442
Secondary accession number(s): Q9X767

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	June 16, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)