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Protein

Pyruvate formate-lyase 1-activating enzyme

Gene

pflA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Activation of pyruvate formate-lyase 1 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] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi30Iron-sulfur (4Fe-4S-S-AdoMet)1 Publication1
Metal bindingi34Iron-sulfur (4Fe-4S-S-AdoMet)1 Publication1
Metal bindingi37Iron-sulfur (4Fe-4S-S-AdoMet)1 Publication1
Binding sitei79S-adenosyl-L-methionine; via carbonyl oxygen1 Publication1
Binding sitei203S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen1 Publication1

GO - Molecular functioni

  • [formate-C-acetyltransferase]-activating enzyme activity Source: EcoCyc
  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • oxidoreductase activity Source: EcoliWiki

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • enzyme active site formation Source: EcoCyc
  • glucose metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciEcoCyc:PFLACTENZ-MONOMER.
ECOL316407:JW0885-MONOMER.
BRENDAi1.97.1.4. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate formate-lyase 1-activating enzyme (EC:1.97.1.4)
Alternative name(s):
Formate-C-acetyltransferase-activating enzyme 1
PFL-activating enzyme 1
Gene namesi
Name:pflA
Synonyms:act
Ordered Locus Names:b0902, JW0885
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10028. pflA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00002005222 – 246Pyruvate formate-lyase 1-activating enzymeAdd BLAST245

Proteomic databases

EPDiP0A9N4.
PaxDbiP0A9N4.
PRIDEiP0A9N4.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ydcYP644554EBI-1114060,EBI-9129853

Protein-protein interaction databases

DIPiDIP-35915N.
IntActiP0A9N4. 19 interactors.
STRINGi511145.b0902.

Structurei

Secondary structure

1246
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 14Combined sources10
Beta strandi18 – 28Combined sources11
Helixi40 – 42Combined sources3
Beta strandi48 – 51Combined sources4
Helixi53 – 60Combined sources8
Helixi61 – 63Combined sources3
Helixi64 – 67Combined sources4
Beta strandi73 – 79Combined sources7
Helixi81 – 84Combined sources4
Helixi85 – 96Combined sources12
Turni97 – 99Combined sources3
Beta strandi102 – 106Combined sources5
Helixi115 – 122Combined sources8
Beta strandi125 – 130Combined sources6
Helixi136 – 143Combined sources8
Helixi148 – 160Combined sources13
Beta strandi164 – 170Combined sources7
Turni172 – 174Combined sources3
Helixi178 – 191Combined sources14
Beta strandi194 – 201Combined sources8
Helixi207 – 212Combined sources6
Turni218 – 221Combined sources4
Helixi227 – 238Combined sources12
Turni239 – 241Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C8FX-ray2.25A2-246[»]
3CB8X-ray2.77A2-246[»]
ProteinModelPortaliP0A9N4.
SMRiP0A9N4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9N4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni36 – 38S-adenosyl-L-methionine binding1 Publication3
Regioni130 – 132S-adenosyl-L-methionine binding1 Publication3

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105F1A. Bacteria.
COG1180. LUCA.
HOGENOMiHOG000011458.
InParanoidiP0A9N4.
KOiK04069.
OMAiYCHNPDC.
PhylomeDBiP0A9N4.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A9N4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVIGRIHSF ESCGTVDGPG IRFITFFQGC LMRCLYCHNR DTWDTHGGKE
60 70 80 90 100
VTVEDLMKEV VTYRHFMNAS GGGVTASGGE AILQAEFVRD WFRACKKEGI
110 120 130 140 150
HTCLDTNGFV RRYDPVIDEL LEVTDLVMLD LKQMNDEIHQ NLVGVSNHRT
160 170 180 190 200
LEFAKYLANK NVKVWIRYVV VPGWSDDDDS AHRLGEFTRD MGNVEKIELL
210 220 230 240
PYHELGKHKW VAMGEEYKLD GVKPPKKETM ERVKGILEQY GHKVMF
Length:246
Mass (Da):28,204
Last modified:January 23, 2007 - v2
Checksum:i486E06A9CE97BF37
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X08035 Genomic DNA. Translation: CAA30829.1.
U00096 Genomic DNA. Translation: AAC73988.1.
AP009048 Genomic DNA. Translation: BAA35637.1.
PIRiS01789.
RefSeqiNP_415422.1. NC_000913.3.
WP_000111043.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73988; AAC73988; b0902.
BAA35637; BAA35637; BAA35637.
GeneIDi945517.
KEGGiecj:JW0885.
eco:b0902.
PATRICi32117017. VBIEscCol129921_0933.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X08035 Genomic DNA. Translation: CAA30829.1.
U00096 Genomic DNA. Translation: AAC73988.1.
AP009048 Genomic DNA. Translation: BAA35637.1.
PIRiS01789.
RefSeqiNP_415422.1. NC_000913.3.
WP_000111043.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C8FX-ray2.25A2-246[»]
3CB8X-ray2.77A2-246[»]
ProteinModelPortaliP0A9N4.
SMRiP0A9N4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35915N.
IntActiP0A9N4. 19 interactors.
STRINGi511145.b0902.

Proteomic databases

EPDiP0A9N4.
PaxDbiP0A9N4.
PRIDEiP0A9N4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73988; AAC73988; b0902.
BAA35637; BAA35637; BAA35637.
GeneIDi945517.
KEGGiecj:JW0885.
eco:b0902.
PATRICi32117017. VBIEscCol129921_0933.

Organism-specific databases

EchoBASEiEB0027.
EcoGeneiEG10028. pflA.

Phylogenomic databases

eggNOGiENOG4105F1A. Bacteria.
COG1180. LUCA.
HOGENOMiHOG000011458.
InParanoidiP0A9N4.
KOiK04069.
OMAiYCHNPDC.
PhylomeDBiP0A9N4.

Enzyme and pathway databases

BioCyciEcoCyc:PFLACTENZ-MONOMER.
ECOL316407:JW0885-MONOMER.
BRENDAi1.97.1.4. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A9N4.
PROiP0A9N4.

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...

Entry informationi

Entry nameiPFLA_ECOLI
AccessioniPrimary (citable) accession number: P0A9N4
Secondary accession number(s): P09374
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.