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P09373

- PFLB_ECOLI

UniProt

P09373 - PFLB_ECOLI

Protein

Formate acetyltransferase 1

Gene

pflB

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 151 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Acetyl-CoA + formate = CoA + pyruvate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei419 – 4191S-acetylcysteine intermediate
    Active sitei420 – 4201Cysteine radical intermediate

    GO - Molecular functioni

    1. formate C-acetyltransferase activity Source: EcoCyc
    2. protein binding Source: IntAct

    GO - Biological processi

    1. anaerobic respiration Source: EcoCyc
    2. glucose metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism

    Enzyme and pathway databases

    BioCyciEcoCyc:PYRUVFORMLY-MONOMER.
    ECOL316407:JW0886-MONOMER.
    MetaCyc:PYRUVFORMLY-MONOMER.
    BRENDAi2.3.1.54. 2026.
    UniPathwayiUPA00920; UER00891.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formate acetyltransferase 1 (EC:2.3.1.54)
    Alternative name(s):
    Pyruvate formate-lyase 1
    Gene namesi
    Name:pflB
    Synonyms:pfl
    Ordered Locus Names:b0903, JW0886
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10701. pflB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 760759Formate acetyltransferase 1PRO_0000166687Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei63 – 631N6-acetyllysine; alternate1 Publication
    Modified residuei63 – 631N6-succinyllysine; alternate1 Publication
    Modified residuei107 – 1071N6-succinyllysine1 Publication
    Modified residuei117 – 1171N6-acetyllysine; alternate1 Publication
    Modified residuei117 – 1171N6-succinyllysine; alternate1 Publication
    Modified residuei124 – 1241N6-acetyllysine; alternate
    Modified residuei124 – 1241N6-succinyllysine; alternate1 Publication
    Modified residuei195 – 1951N6-acetyllysine; alternate1 Publication
    Modified residuei195 – 1951N6-succinyllysine; alternate1 Publication
    Modified residuei454 – 4541N6-acetyllysine; alternate1 Publication
    Modified residuei454 – 4541N6-succinyllysine; alternate1 Publication
    Modified residuei467 – 4671N6-succinyllysine1 Publication
    Modified residuei541 – 5411N6-acetyllysine1 Publication
    Modified residuei591 – 5911N6-acetyllysine1 Publication
    Modified residuei654 – 6541N6-succinyllysine1 Publication
    Modified residuei735 – 7351Glycine radical

    Keywords - PTMi

    Acetylation, Organic radical

    Proteomic databases

    PaxDbiP09373.
    PRIDEiP09373.

    2D gel databases

    SWISS-2DPAGEP09373.

    Expressioni

    Inductioni

    By pfl-activating enzyme under anaerobic conditions by generation of an organic free radical. Exposure of activated pfl to oxygen resulted in cleavage at the glycine residue harboring its organic radical with loss of the 25 C-terminal AA.

    Gene expression databases

    GenevestigatoriP09373.

    Interactioni

    Subunit structurei

    Homodimer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    tpiAP0A8585EBI-546682,EBI-368978

    Protein-protein interaction databases

    DIPiDIP-10467N.
    IntActiP09373. 42 interactions.
    MINTiMINT-1283506.
    STRINGi511145.b0903.

    Structurei

    Secondary structure

    1
    760
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 116
    Turni12 – 143
    Helixi19 – 213
    Helixi26 – 338
    Helixi41 – 433
    Helixi49 – 6820
    Beta strandi72 – 798
    Beta strandi82 – 854
    Turni92 – 943
    Beta strandi101 – 1044
    Beta strandi107 – 1104
    Helixi112 – 1143
    Helixi117 – 1259
    Helixi132 – 1409
    Helixi145 – 1528
    Helixi155 – 1628
    Beta strandi164 – 1674
    Beta strandi172 – 1743
    Helixi183 – 1886
    Helixi190 – 20213
    Helixi205 – 2106
    Turni211 – 2133
    Helixi214 – 24027
    Helixi252 – 26918
    Helixi281 – 29313
    Helixi299 – 31315
    Helixi322 – 3276
    Beta strandi336 – 3405
    Beta strandi346 – 3483
    Helixi352 – 36312
    Beta strandi370 – 3767
    Helixi382 – 39514
    Beta strandi399 – 4024
    Helixi403 – 4108
    Beta strandi415 – 4184
    Turni419 – 4213
    Beta strandi422 – 4254
    Turni426 – 4283
    Beta strandi429 – 43810
    Helixi439 – 4479
    Turni448 – 4503
    Turni453 – 4553
    Beta strandi468 – 4703
    Helixi473 – 50533
    Helixi509 – 5124
    Beta strandi520 – 5289
    Helixi530 – 54213
    Beta strandi543 – 5497
    Beta strandi555 – 5628
    Beta strandi567 – 5704
    Helixi572 – 59019
    Helixi595 – 5973
    Beta strandi599 – 6046
    Helixi609 – 6157
    Turni638 – 6403
    Helixi645 – 6539
    Helixi657 – 6593
    Beta strandi667 – 6704
    Helixi672 – 6754
    Helixi679 – 69416
    Beta strandi705 – 7106
    Helixi713 – 7219
    Helixi723 – 7253
    Beta strandi730 – 7323
    Beta strandi734 – 7396
    Helixi740 – 7423
    Helixi745 – 7528

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CM5X-ray2.30A/B2-760[»]
    1H16X-ray1.53A2-760[»]
    1H17X-ray1.75A2-760[»]
    1H18X-ray2.30A/B2-760[»]
    1MZOX-ray2.70A/B2-760[»]
    1QHMX-ray2.80A/B2-625[»]
    2PFLX-ray2.90A/B2-760[»]
    3PFLX-ray2.60A/B2-760[»]
    ProteinModelPortaliP09373.
    SMRiP09373. Positions 2-760.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09373.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 625623PFLPROSITE-ProRule annotationAdd
    BLAST
    Domaini632 – 760129Glycine radicalPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 glycine radical domain.PROSITE-ProRule annotation
    Contains 1 PFL domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1882.
    HOGENOMiHOG000011346.
    KOiK00656.
    OMAiYERIQMA.
    OrthoDBiEOG6Q8J0J.
    PhylomeDBiP09373.

    Family and domain databases

    InterProiIPR005949. Form_AcTrfase.
    IPR019777. Form_AcTrfase_GR_CS.
    IPR001150. Gly_radical.
    IPR004184. PFL_dom.
    [Graphical view]
    PfamiPF01228. Gly_radical. 1 hit.
    PF02901. PFL. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000379. For_Ac_trans_1. 1 hit.
    TIGRFAMsiTIGR01255. pyr_form_ly_1. 1 hit.
    PROSITEiPS00850. GLY_RADICAL_1. 1 hit.
    PS51149. GLY_RADICAL_2. 1 hit.
    PS51554. PFL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P09373-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSELNEKLAT AWEGFTKGDW QNEVNVRDFI QKNYTPYEGD ESFLAGATEA    50
    TTTLWDKVME GVKLENRTHA PVDFDTAVAS TITSHDAGYI NKQLEKIVGL 100
    QTEAPLKRAL IPFGGIKMIE GSCKAYNREL DPMIKKIFTE YRKTHNQGVF 150
    DVYTPDILRC RKSGVLTGLP DAYGRGRIIG DYRRVALYGI DYLMKDKLAQ 200
    FTSLQADLEN GVNLEQTIRL REEIAEQHRA LGQMKEMAAK YGYDISGPAT 250
    NAQEAIQWTY FGYLAAVKSQ NGAAMSFGRT STFLDVYIER DLKAGKITEQ 300
    EAQEMVDHLV MKLRMVRFLR TPEYDELFSG DPIWATESIG GMGLDGRTLV 350
    TKNSFRFLNT LYTMGPSPEP NMTILWSEKL PLNFKKFAAK VSIDTSSLQY 400
    ENDDLMRPDF NNDDYAIACC VSPMIVGKQM QFFGARANLA KTMLYAINGG 450
    VDEKLKMQVG PKSEPIKGDV LNYDEVMERM DHFMDWLAKQ YITALNIIHY 500
    MHDKYSYEAS LMALHDRDVI RTMACGIAGL SVAADSLSAI KYAKVKPIRD 550
    EDGLAIDFEI EGEYPQFGNN DPRVDDLAVD LVERFMKKIQ KLHTYRDAIP 600
    TQSVLTITSN VVYGKKTGNT PDGRRAGAPF GPGANPMHGR DQKGAVASLT 650
    SVAKLPFAYA KDGISYTFSI VPNALGKDDE VRKTNLAGLM DGYFHHEASI 700
    EGGQHLNVNV MNREMLLDAM ENPEKYPQLT IRVSGYAVRF NSLTKEQQQD 750
    VITRTFTQSM 760
    Length:760
    Mass (Da):85,357
    Last modified:January 23, 2007 - v2
    Checksum:i19323C63081625D6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X08035 Genomic DNA. Translation: CAA30828.1.
    U00096 Genomic DNA. Translation: AAC73989.1.
    AP009048 Genomic DNA. Translation: BAA35638.1.
    M26413 Genomic DNA. Translation: AAA20391.1.
    PIRiS01788.
    RefSeqiNP_415423.1. NC_000913.3.
    YP_489175.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73989; AAC73989; b0903.
    BAA35638; BAA35638; BAA35638.
    GeneIDi12931841.
    945514.
    KEGGiecj:Y75_p0875.
    eco:b0903.
    PATRICi32117019. VBIEscCol129921_0934.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X08035 Genomic DNA. Translation: CAA30828.1 .
    U00096 Genomic DNA. Translation: AAC73989.1 .
    AP009048 Genomic DNA. Translation: BAA35638.1 .
    M26413 Genomic DNA. Translation: AAA20391.1 .
    PIRi S01788.
    RefSeqi NP_415423.1. NC_000913.3.
    YP_489175.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CM5 X-ray 2.30 A/B 2-760 [» ]
    1H16 X-ray 1.53 A 2-760 [» ]
    1H17 X-ray 1.75 A 2-760 [» ]
    1H18 X-ray 2.30 A/B 2-760 [» ]
    1MZO X-ray 2.70 A/B 2-760 [» ]
    1QHM X-ray 2.80 A/B 2-625 [» ]
    2PFL X-ray 2.90 A/B 2-760 [» ]
    3PFL X-ray 2.60 A/B 2-760 [» ]
    ProteinModelPortali P09373.
    SMRi P09373. Positions 2-760.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10467N.
    IntActi P09373. 42 interactions.
    MINTi MINT-1283506.
    STRINGi 511145.b0903.

    2D gel databases

    SWISS-2DPAGE P09373.

    Proteomic databases

    PaxDbi P09373.
    PRIDEi P09373.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73989 ; AAC73989 ; b0903 .
    BAA35638 ; BAA35638 ; BAA35638 .
    GeneIDi 12931841.
    945514.
    KEGGi ecj:Y75_p0875.
    eco:b0903.
    PATRICi 32117019. VBIEscCol129921_0934.

    Organism-specific databases

    EchoBASEi EB0695.
    EcoGenei EG10701. pflB.

    Phylogenomic databases

    eggNOGi COG1882.
    HOGENOMi HOG000011346.
    KOi K00656.
    OMAi YERIQMA.
    OrthoDBi EOG6Q8J0J.
    PhylomeDBi P09373.

    Enzyme and pathway databases

    UniPathwayi UPA00920 ; UER00891 .
    BioCyci EcoCyc:PYRUVFORMLY-MONOMER.
    ECOL316407:JW0886-MONOMER.
    MetaCyc:PYRUVFORMLY-MONOMER.
    BRENDAi 2.3.1.54. 2026.

    Miscellaneous databases

    EvolutionaryTracei P09373.
    PROi P09373.

    Gene expression databases

    Genevestigatori P09373.

    Family and domain databases

    InterProi IPR005949. Form_AcTrfase.
    IPR019777. Form_AcTrfase_GR_CS.
    IPR001150. Gly_radical.
    IPR004184. PFL_dom.
    [Graphical view ]
    Pfami PF01228. Gly_radical. 1 hit.
    PF02901. PFL. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000379. For_Ac_trans_1. 1 hit.
    TIGRFAMsi TIGR01255. pyr_form_ly_1. 1 hit.
    PROSITEi PS00850. GLY_RADICAL_1. 1 hit.
    PS51149. GLY_RADICAL_2. 1 hit.
    PS51554. PFL. 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.
    5. "Novel transcriptional control of the pyruvate formate-lyase gene: upstream regulatory sequences and multiple promoters regulate anaerobic expression."
      Sawers G., Boeck A.
      J. Bacteriol. 171:2485-2498(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
    6. "The free radical in pyruvate formate-lyase is located on glycine-734."
      Wagner A.F.V., Frey M., Neugebauer F.A., Schaefer W., Knappe J.
      Proc. Natl. Acad. Sci. U.S.A. 89:996-1000(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: ORGANIC RADICAL.
    7. "Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis."
      Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M., Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.
      Electrophoresis 19:837-844(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-6.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    9. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-117; LYS-195; LYS-454; LYS-541 AND LYS-591, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    10. "Identification of lysine succinylation as a new post-translational modification."
      Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
      Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION AT LYS-63; LYS-107; LYS-117; LYS-124; LYS-195; LYS-454; LYS-467 AND LYS-654.
      Strain: K12.
    11. "Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase."
      Becker A., Fritz-Wolf K., Kabsch W., Knappe J., Schultz S., Wagner A.F.V.
      Nat. Struct. Biol. 6:969-975(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

    Entry informationi

    Entry nameiPFLB_ECOLI
    AccessioniPrimary (citable) accession number: P09373
    Secondary accession number(s): P76826, Q47478
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 151 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Several mechanisms have been proposed based on complexes formed with substrate analogs. After activation by the glycine radical, the cysteine radical, Cys-420, can abstract hydrogen atoms from the other active site cysteine, Cys-419, and from coenzyme A, and it can also transfer hydrogen atoms to product radicals. The other active site cysteine can attack the central carbonyl of pyruvate and covalently bind the product acetyl group.

    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. Keywords
      Controlled vocabulary of keywords
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3