Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A443

- PFLA_LISIN

UniProt

P0A443 - PFLA_LISIN

Protein

Pyruvate formate-lyase-activating enzyme

Gene

pflA

Organism
Listeria innocua serovar 6a (strain CLIP 11262)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (15 Mar 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.By similarity

    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 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi31 – 311Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
    Metal bindingi35 – 351Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
    Metal bindingi38 – 381Iron-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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate formate-lyase-activating enzyme (EC:1.97.1.4)
    Short name:
    PFL-activating enzyme
    Gene namesi
    Name:pflA
    Synonyms:pflC
    Ordered Locus Names:lin1444
    OrganismiListeria innocua serovar 6a (strain CLIP 11262)
    Taxonomic identifieri272626 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
    ProteomesiUP000002513: Chromosome

    Organism-specific databases

    GenoListiLIN1444.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 248248Pyruvate formate-lyase-activating enzymePRO_0000200530Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi272626.lin1444.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A443.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1180.
    HOGENOMiHOG000011458.
    KOiK04069.
    OMAiWEMETNK.
    OrthoDBiEOG64FKHC.

    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.

    P0A443-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEVLGRVHS VETMGTVDGP GIRFIVFMQG CLLRCQFCHN PDTWKIGTGT    50
    ERSAQDVFDE AIKYKEFWDA SGGGVTVSGG EPLLQVDFLI EFFTLCKAAG 100
    VHTTIDSCGG CFTRDPEFIE KLDRLMEVTD LILLDIKQIN PEKHLKLTTK 150
    SNAPIIDFAH YLRDKEQPIW IRHVLIPTKT DDPEDLTKLH EFIQTLPNVK 200
    QVDVLPYHTM GVYKWKEMGI RYPLEGIEAP EEEVVALANK ILETSSYK 248
    Length:248
    Mass (Da):28,115
    Last modified:March 15, 2005 - v1
    Checksum:i0A6F5BBA95CBEBC9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL596168 Genomic DNA. Translation: CAC96675.1.
    PIRiAC1613.
    RefSeqiNP_470780.1. NC_003212.1.

    Genome annotation databases

    EnsemblBacteriaiCAC96675; CAC96675; CAC96675.
    GeneIDi1130045.
    KEGGilin:lin1444.
    PATRICi20299621. VBILisInn102668_1477.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL596168 Genomic DNA. Translation: CAC96675.1 .
    PIRi AC1613.
    RefSeqi NP_470780.1. NC_003212.1.

    3D structure databases

    ProteinModelPortali P0A443.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272626.lin1444.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC96675 ; CAC96675 ; CAC96675 .
    GeneIDi 1130045.
    KEGGi lin:lin1444.
    PATRICi 20299621. VBILisInn102668_1477.

    Organism-specific databases

    GenoListi LIN1444.

    Phylogenomic databases

    eggNOGi COG1180.
    HOGENOMi HOG000011458.
    KOi K04069.
    OMAi WEMETNK.
    OrthoDBi EOG64FKHC.

    Family and domain databases

    InterProi IPR012838. PFL_activating.
    IPR001989. Radical_activat_CS.
    IPR007197. rSAM.
    [Graphical view ]
    Pfami PF04055. Radical_SAM. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02493. PFLA. 1 hit.
    PROSITEi PS01087. RADICAL_ACTIVATING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CLIP 11262.

    Entry informationi

    Entry nameiPFLA_LISIN
    AccessioniPrimary (citable) accession number: P0A443
    Secondary accession number(s): Q9X767
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 60 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3