Reviewed, UniProtKB/Swiss-Prot Q46267 (PFLA_CLOPA)

Names and origin

Protein names

Recommended name:
    Pyruvate formate-lyase-activating enzyme
      Short name=PFL-activating enzyme
    EC=1.97.1.4
Alternative name(s):
    Formate-C-acetyltransferase-activating enzyme

Gene names

Name:

act

Organism

Clostridium pasteurianum

Taxonomic identifier

1501 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	238 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.
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.
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
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 – 238	238	Pyruvate formate-lyase-activating enzyme		PRO_0000200529
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)
	Q46267-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 85E2ACED85C6B7D1	FASTA	238	27,148
	10 20 30 40 50 60 MVMGRIHSIE SMGLVDGPGI RTVVFFQGCG LRCSYCHNPD TWNMAGGKEL TAEELLKKLL 70 80 90 100 110 120 RFKPYFDRSG GGVTFSGGEV LLQPEFLIDI LKLCKEQGIH TAIDTAGYGY GNYEEILKHT 130 140 150 160 170 180 DLVLLDIKHV DDDGYKCITG KGKRGFDDFL KAVENIGVKV WIRHVIVPTL TDSKENIRKL 190 200 210 220 230 ANIIKNIRNV EKVELLPYHT LGINKYEKLN LDYKLRDIEA MDKEKRKKLE KYLKELLE

References

[1]	"Molecular characterization of the genes encoding pyruvate formate-lyase and its activating enzyme of Clostridium pasteurianum." Weidner G., Sawers G. J. Bacteriol. 178:2440-2444(1996) [PubMed: 8636053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	X93463 Genomic DNA. Translation: CAA63749.1.
PIR	JC6011.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MON-12104.
BRENDA	1.97.1.4. 871.
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_CLOPA

Accession

Primary (citable) accession number: Q46267

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 52 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)