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P0A9N4

- PFLA_ECOLI

UniProt

P0A9N4 - PFLA_ECOLI

Protein

Pyruvate formate-lyase 1-activating enzyme

Gene

pflA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi30 – 301Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
    Metal bindingi34 – 341Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
    Metal bindingi37 – 371Iron-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
    4. oxidoreductase activity Source: EcoliWiki
    5. protein binding Source: IntAct

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: EcoliWiki
    2. glucose metabolic process Source: UniProtKB-KW

    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.

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10028. pflA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 246245Pyruvate formate-lyase 1-activating enzymePRO_0000200522Add
    BLAST

    Proteomic databases

    PaxDbiP0A9N4.
    PRIDEiP0A9N4.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A9N4.

    Interactioni

    Binary interactionsi

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

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    246
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 1410
    Beta strandi18 – 2811
    Helixi40 – 423
    Beta strandi48 – 514
    Helixi53 – 608
    Helixi61 – 633
    Helixi64 – 674
    Beta strandi73 – 797
    Helixi81 – 844
    Helixi85 – 9612
    Turni97 – 993
    Beta strandi102 – 1065
    Helixi115 – 1228
    Beta strandi125 – 1306
    Helixi136 – 1438
    Helixi148 – 16013
    Beta strandi164 – 1707
    Turni172 – 1743
    Helixi178 – 19114
    Beta strandi194 – 2018
    Helixi207 – 2126
    Turni218 – 2214
    Helixi227 – 23812
    Turni239 – 2413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3C8FX-ray2.25A2-246[»]
    3CB8X-ray2.77A2-246[»]
    ProteinModelPortaliP0A9N4.
    SMRiP0A9N4. Positions 2-246.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9N4.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1180.
    HOGENOMiHOG000011458.
    KOiK04069.
    OMAiQNLIGVP.
    OrthoDBiEOG64FKHC.
    PhylomeDBiP0A9N4.

    Family and domain databases

    InterProiIPR006638. Elp3/MiaB/NifB.
    IPR012838. PFL_activating.
    IPR001989. Radical_activat_CS.
    IPR007197. rSAM.
    [Graphical view]
    PfamiPF04055. Radical_SAM. 1 hit.
    [Graphical view]
    SMARTiSM00729. Elp3. 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

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    MSVIGRIHSF ESCGTVDGPG IRFITFFQGC LMRCLYCHNR DTWDTHGGKE    50
    VTVEDLMKEV VTYRHFMNAS GGGVTASGGE AILQAEFVRD WFRACKKEGI 100
    HTCLDTNGFV RRYDPVIDEL LEVTDLVMLD LKQMNDEIHQ NLVGVSNHRT 150
    LEFAKYLANK NVKVWIRYVV VPGWSDDDDS AHRLGEFTRD MGNVEKIELL 200
    PYHELGKHKW VAMGEEYKLD GVKPPKKETM ERVKGILEQY GHKVMF 246
    Length:246
    Mass (Da):28,204
    Last modified:January 23, 2007 - v2
    Checksum:i486E06A9CE97BF37
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_489174.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73988; AAC73988; b0902.
    BAA35637; BAA35637; BAA35637.
    GeneIDi12930359.
    945517.
    KEGGiecj:Y75_p0874.
    eco:b0902.
    PATRICi32117017. VBIEscCol129921_0933.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X08035 Genomic DNA. Translation: CAA30829.1 .
    U00096 Genomic DNA. Translation: AAC73988.1 .
    AP009048 Genomic DNA. Translation: BAA35637.1 .
    PIRi S01789.
    RefSeqi NP_415422.1. NC_000913.3.
    YP_489174.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3C8F X-ray 2.25 A 2-246 [» ]
    3CB8 X-ray 2.77 A 2-246 [» ]
    ProteinModelPortali P0A9N4.
    SMRi P0A9N4. Positions 2-246.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35915N.
    IntActi P0A9N4. 19 interactions.
    STRINGi 511145.b0902.

    Proteomic databases

    PaxDbi P0A9N4.
    PRIDEi P0A9N4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73988 ; AAC73988 ; b0902 .
    BAA35637 ; BAA35637 ; BAA35637 .
    GeneIDi 12930359.
    945517.
    KEGGi ecj:Y75_p0874.
    eco:b0902.
    PATRICi 32117017. VBIEscCol129921_0933.

    Organism-specific databases

    EchoBASEi EB0027.
    EcoGenei EG10028. pflA.

    Phylogenomic databases

    eggNOGi COG1180.
    HOGENOMi HOG000011458.
    KOi K04069.
    OMAi QNLIGVP.
    OrthoDBi EOG64FKHC.
    PhylomeDBi P0A9N4.

    Enzyme and pathway databases

    BioCyci EcoCyc:PFLACTENZ-MONOMER.
    ECOL316407:JW0885-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A9N4.
    PROi P0A9N4.

    Gene expression databases

    Genevestigatori P0A9N4.

    Family and domain databases

    InterProi IPR006638. Elp3/MiaB/NifB.
    IPR012838. PFL_activating.
    IPR001989. Radical_activat_CS.
    IPR007197. rSAM.
    [Graphical view ]
    Pfami PF04055. Radical_SAM. 1 hit.
    [Graphical view ]
    SMARTi SM00729. Elp3. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02493. PFLA. 1 hit.
    PROSITEi PS01087. RADICAL_ACTIVATING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structures of Escherichia coli pyruvate formate-lyase and pyruvate-formate-lyase-activating enzyme deduced from the DNA nucleotide sequences."
      Roedel W., Plaga W., Frank R., Knappe J.
      Eur. J. Biochem. 177:153-158(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: K12.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

    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: October 1, 2014
    This is version 77 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

    External Data

    Dasty 3