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O68575

- PFLA_STRMU

UniProt

O68575 - PFLA_STRMU

Protein

Pyruvate formate-lyase-activating enzyme

Gene

act

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    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

    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 bindingi37 – 371Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
    Metal bindingi41 – 411Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
    Metal bindingi44 – 441Iron-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

    Enzyme and pathway databases

    BioCyciSMUT210007:GC7Z-1584-MONOMER.

    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
    Synonyms:pflA, pflC
    Ordered Locus Names:SMU_1692
    OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
    Taxonomic identifieri210007 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000002512: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 263263Pyruvate formate-lyase-activating enzymePRO_0000200533Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi210007.SMU.1692.

    Structurei

    3D structure databases

    ProteinModelPortaliO68575.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1180.
    KOiK04069.
    OMAiWEMETNK.
    OrthoDBiEOG64FKHC.
    PhylomeDBiO68575.

    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.

    O68575-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIEKVDYEKV TGLVNSTESF GSVDGPGIRF VVFMQGCQMR CQYCHNPDTW    50
    AMKNDRATER TAGDVFKEAL RFKDFWGDTG GITVSGGEAT LQMDFLIALF 100
    SLAKEKGIHT TLDTCALTFR NTPKYLEKYE KLMAVTDLVL LDIKEINPDQ 150
    HKIVTGHSNK TILACARYLS DIGKPVWIRH VLVPGLTDRD EDLIKLGEYV 200
    KTLKNVQRFE ILPYHTMGEF KWRELGIPYP LEGVKPPTPD RVRNAKKLMH 250
    TETYEEYKKR INH 263
    Length:263
    Mass (Da):30,150
    Last modified:August 1, 1998 - v1
    Checksum:i575405F3EE248EFC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051356 Genomic DNA. Translation: AAC05773.1.
    AB018417 Genomic DNA. Translation: BAA34998.1.
    AE014133 Genomic DNA. Translation: AAN59329.1.
    RefSeqiNP_722023.1. NC_004350.2.
    WP_002262580.1. NC_004350.2.
    YP_006490815.1. NC_018089.1.

    Genome annotation databases

    EnsemblBacteriaiAAN59329; AAN59329; SMU_1692.
    GeneIDi1028925.
    13299948.
    KEGGismu:SMU_1692.
    smut:SMUGS5_07650.
    PATRICi19665367. VBIStrMut61772_1512.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051356 Genomic DNA. Translation: AAC05773.1 .
    AB018417 Genomic DNA. Translation: BAA34998.1 .
    AE014133 Genomic DNA. Translation: AAN59329.1 .
    RefSeqi NP_722023.1. NC_004350.2.
    WP_002262580.1. NC_004350.2.
    YP_006490815.1. NC_018089.1.

    3D structure databases

    ProteinModelPortali O68575.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 210007.SMU.1692.

    Protocols and materials databases

    DNASUi 1028925.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN59329 ; AAN59329 ; SMU_1692 .
    GeneIDi 1028925.
    13299948.
    KEGGi smu:SMU_1692.
    smut:SMUGS5_07650.
    PATRICi 19665367. VBIStrMut61772_1512.

    Phylogenomic databases

    eggNOGi COG1180.
    KOi K04069.
    OMAi WEMETNK.
    OrthoDBi EOG64FKHC.
    PhylomeDBi O68575.

    Enzyme and pathway databases

    BioCyci SMUT210007:GC7Z-1584-MONOMER.

    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. "Defects in D-alanyl-lipoteichoic acid synthesis in Streptococcus mutans results in acid sensitivity."
      Boyd D.A., Cvitkovitch D.G., Bleiweis A.S., Kiriukhin M.Y., Debabov D.V., Neuhaus F.C., Hamilton I.R.
      J. Bacteriol. 182:6055-6065(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: LT11.
    2. "Characterization of the Streptococcus mutans pyruvate formate-lyase (PFL)-activating enzyme gene by complementary reconstitution of the in vitro PFL-reactivating system."
      Yamamoto Y., Sato Y., Takahashi-Abbe S., Takahashi N., Kizaki H.
      Infect. Immun. 68:4773-4777(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: GS-5.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700610 / UA159.

    Entry informationi

    Entry nameiPFLA_STRMU
    AccessioniPrimary (citable) accession number: O68575
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 112 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3