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Protein

Pyruvate formate-lyase-activating enzyme

Gene

act

Organism
Clostridium pasteurianum
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 activityi

S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi29 – 291Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
Metal bindingi33 – 331Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
Metal bindingi36 – 361Iron-sulfur (4Fe-4S-S-AdoMet)By similarity

GO - Molecular functioni

  1. [formate-C-acetyltransferase]-activating enzyme activity Source: UniProtKB-EC
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12104.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate formate-lyase-activating enzyme (EC:1.97.1.4)
Short name:
PFL-activating enzyme
Alternative name(s):
Formate-C-acetyltransferase-activating enzyme
Gene namesi
Name:act
OrganismiClostridium pasteurianum
Taxonomic identifieri1501 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238Pyruvate formate-lyase-activating enzymePRO_0000200529Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ46267.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR012838. PFL_activating.
IPR001989. Radical_activat_CS.
IPR007197. rSAM.
[Graphical view]
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02493. PFLA. 1 hit.
PROSITEiPS01087. RADICAL_ACTIVATING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q46267-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVMGRIHSIE SMGLVDGPGI RTVVFFQGCG LRCSYCHNPD TWNMAGGKEL
60 70 80 90 100
TAEELLKKLL RFKPYFDRSG GGVTFSGGEV LLQPEFLIDI LKLCKEQGIH
110 120 130 140 150
TAIDTAGYGY GNYEEILKHT DLVLLDIKHV DDDGYKCITG KGKRGFDDFL
160 170 180 190 200
KAVENIGVKV WIRHVIVPTL TDSKENIRKL ANIIKNIRNV EKVELLPYHT
210 220 230
LGINKYEKLN LDYKLRDIEA MDKEKRKKLE KYLKELLE
Length:238
Mass (Da):27,148
Last modified:November 1, 1996 - v1
Checksum:i85E2ACED85C6B7D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X93463 Genomic DNA. Translation: CAA63749.1.
PIRiJC6011.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X93463 Genomic DNA. Translation: CAA63749.1.
PIRiJC6011.

3D structure databases

ProteinModelPortaliQ46267.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12104.

Family and domain databases

InterProiIPR012838. PFL_activating.
IPR001989. Radical_activat_CS.
IPR007197. rSAM.
[Graphical view]
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02493. PFLA. 1 hit.
PROSITEiPS01087. RADICAL_ACTIVATING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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].

Entry informationi

Entry nameiPFLA_CLOPA
AccessioniPrimary (citable) accession number: Q46267
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.