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)

Q5HJF3

- PFLA_STAAC

UniProt

Q5HJF3 - PFLA_STAAC

Protein

Pyruvate formate-lyase-activating enzyme

Gene

pflA

Organism
Staphylococcus aureus (strain COL)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (15 Feb 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 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

    GO - Biological processi

    1. 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

    BioCyciSAUR93062:GCEP-200-MONOMER.

    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
    Ordered Locus Names:SACOL0205
    OrganismiStaphylococcus aureus (strain COL)
    Taxonomic identifieri93062 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000530: Chromosome

    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 – 251251Pyruvate formate-lyase-activating enzymePRO_0000271711Add
    BLAST

    Proteomic databases

    PRIDEiQ5HJF3.

    Interactioni

    Protein-protein interaction databases

    STRINGi93062.SACOL0205.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5HJF3.
    SMRiQ5HJF3. Positions 71-207.
    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.

    Q5HJF3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLKGHLHSVE SLGTVDGPGL RYILFTQGCL LRCLYCHNPD TWKISEPSRE    50
    VTVDEMVNEI LPYKPYFDAS GGGVTVSGGE PLLQMPFLEK LFAELKENGV 100
    HTCLDTSAGC ANDTKAFQRH FEELQKHTDL ILLDIKHIDN DKHIRLTGKP 150
    NTHILNFARK LSDMKQPVWI RHVLVPGYSD DKDDLIKLGE FINSLDNVEK 200
    FEILPYHQLG VHKWKTLGIA YELEDVEAPD DEAVKAAYRY VNFKGKIPVE 250
    L 251
    Length:251
    Mass (Da):28,499
    Last modified:February 15, 2005 - v1
    Checksum:i892A603E273F6C89
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000046 Genomic DNA. Translation: AAW37501.1.
    RefSeqiYP_185104.1. NC_002951.2.

    Genome annotation databases

    EnsemblBacteriaiAAW37501; AAW37501; SACOL0205.
    GeneIDi3236775.
    KEGGisac:SACOL0205.
    PATRICi19526676. VBIStaAur112458_0204.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000046 Genomic DNA. Translation: AAW37501.1 .
    RefSeqi YP_185104.1. NC_002951.2.

    3D structure databases

    ProteinModelPortali Q5HJF3.
    SMRi Q5HJF3. Positions 71-207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 93062.SACOL0205.

    Proteomic databases

    PRIDEi Q5HJF3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAW37501 ; AAW37501 ; SACOL0205 .
    GeneIDi 3236775.
    KEGGi sac:SACOL0205.
    PATRICi 19526676. VBIStaAur112458_0204.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SAUR93062:GCEP-200-MONOMER.

    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. "Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
      Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H.
      , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
      J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: COL.

    Entry informationi

    Entry nameiPFLA_STAAC
    AccessioniPrimary (citable) accession number: Q5HJF3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 67 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