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Q46267 (PFLA_CLOPA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismClostridium pasteurianum
Taxonomic identifier1501 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length238 AA.
Sequence statusComplete.
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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 238238Pyruvate formate-lyase-activating enzyme
PRO_0000200529

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
Q46267 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 85E2ACED85C6B7D1

FASTA23827,148
        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 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X93463 Genomic DNA. Translation: CAA63749.1.
PIRJC6011.

3D structure databases

ProteinModelPortalQ46267.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12104.

Family and domain databases

InterProIPR012838. PFL_activating.
IPR001989. Radical_activat_CS.
IPR007197. rSAM.
[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_CLOPA
AccessionPrimary (citable) accession number: Q46267
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 67 of the entry and version 1 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