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P09373 (PFLB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Formate acetyltransferase 1

EC=2.3.1.54
Alternative name(s):
Pyruvate formate-lyase 1
Gene names
Name:pflB
Synonyms:pfl
Ordered Locus Names:b0903, JW0886
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length760 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acetyl-CoA + formate = CoA + pyruvate.

Pathway

Fermentation; pyruvate fermentation; formate from pyruvate: step 1/1.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Induction

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.

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.

Sequence similarities

Contains 1 glycine radical domain.

Contains 1 PFL domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

tpiAP0A8585EBI-546682,EBI-368978

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 760759Formate acetyltransferase 1
PRO_0000166687

Regions

Domain3 – 625623PFL
Domain632 – 760129Glycine radical

Sites

Active site4191S-acetylcysteine intermediate
Active site4201Cysteine radical intermediate

Amino acid modifications

Modified residue631N6-acetyllysine; alternate Ref.9
Modified residue631N6-succinyllysine; alternate Ref.10
Modified residue1071N6-succinyllysine Ref.10
Modified residue1171N6-acetyllysine; alternate Ref.9
Modified residue1171N6-succinyllysine; alternate Ref.10
Modified residue1241N6-acetyllysine; alternate
Modified residue1241N6-succinyllysine; alternate Ref.10
Modified residue1951N6-acetyllysine; alternate Ref.9
Modified residue1951N6-succinyllysine; alternate Ref.10
Modified residue4541N6-acetyllysine; alternate Ref.9
Modified residue4541N6-succinyllysine; alternate Ref.10
Modified residue4671N6-succinyllysine Ref.10
Modified residue5411N6-acetyllysine Ref.9
Modified residue5911N6-acetyllysine Ref.9
Modified residue6541N6-succinyllysine Ref.10
Modified residue7351Glycine radical

Secondary structure

........................................................................................................................... 760
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09373 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 19323C63081625D6

FASTA76085,357
        10         20         30         40         50         60 
MSELNEKLAT AWEGFTKGDW QNEVNVRDFI QKNYTPYEGD ESFLAGATEA TTTLWDKVME 

        70         80         90        100        110        120 
GVKLENRTHA PVDFDTAVAS TITSHDAGYI NKQLEKIVGL QTEAPLKRAL IPFGGIKMIE 

       130        140        150        160        170        180 
GSCKAYNREL DPMIKKIFTE YRKTHNQGVF DVYTPDILRC RKSGVLTGLP DAYGRGRIIG 

       190        200        210        220        230        240 
DYRRVALYGI DYLMKDKLAQ FTSLQADLEN GVNLEQTIRL REEIAEQHRA LGQMKEMAAK 

       250        260        270        280        290        300 
YGYDISGPAT NAQEAIQWTY FGYLAAVKSQ NGAAMSFGRT STFLDVYIER DLKAGKITEQ 

       310        320        330        340        350        360 
EAQEMVDHLV MKLRMVRFLR TPEYDELFSG DPIWATESIG GMGLDGRTLV TKNSFRFLNT 

       370        380        390        400        410        420 
LYTMGPSPEP NMTILWSEKL PLNFKKFAAK VSIDTSSLQY ENDDLMRPDF NNDDYAIACC 

       430        440        450        460        470        480 
VSPMIVGKQM QFFGARANLA KTMLYAINGG VDEKLKMQVG PKSEPIKGDV LNYDEVMERM 

       490        500        510        520        530        540 
DHFMDWLAKQ YITALNIIHY MHDKYSYEAS LMALHDRDVI RTMACGIAGL SVAADSLSAI 

       550        560        570        580        590        600 
KYAKVKPIRD EDGLAIDFEI EGEYPQFGNN DPRVDDLAVD LVERFMKKIQ KLHTYRDAIP 

       610        620        630        640        650        660 
TQSVLTITSN VVYGKKTGNT PDGRRAGAPF GPGANPMHGR DQKGAVASLT SVAKLPFAYA 

       670        680        690        700        710        720 
KDGISYTFSI VPNALGKDDE VRKTNLAGLM DGYFHHEASI EGGQHLNVNV MNREMLLDAM 

       730        740        750        760 
ENPEKYPQLT IRVSGYAVRF NSLTKEQQQD VITRTFTQSM 

« Hide

References

« Hide 'large scale' references
[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]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X08035 Genomic DNA. Translation: CAA30828.1.
U00096 Genomic DNA. Translation: AAC73989.1.
AP009048 Genomic DNA. Translation: BAA35638.1.
M26413 Genomic DNA. Translation: AAA20391.1.
PIRS01788.
RefSeqNP_415423.1. NC_000913.3.
YP_489175.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP09373.
SMRP09373. Positions 2-760.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10467N.
IntActP09373. 42 interactions.
MINTMINT-1283506.
STRING511145.b0903.

2D gel databases

SWISS-2DPAGEP09373.

Proteomic databases

PaxDbP09373.
PRIDEP09373.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73989; AAC73989; b0903.
BAA35638; BAA35638; BAA35638.
GeneID12931841.
945514.
KEGGecj:Y75_p0875.
eco:b0903.
PATRIC32117019. VBIEscCol129921_0934.

Organism-specific databases

EchoBASEEB0695.
EcoGeneEG10701. pflB.

Phylogenomic databases

eggNOGCOG1882.
HOGENOMHOG000011346.
KOK00656.
OMAYERIQMA.
OrthoDBEOG6Q8J0J.
PhylomeDBP09373.

Enzyme and pathway databases

BioCycEcoCyc:PYRUVFORMLY-MONOMER.
ECOL316407:JW0886-MONOMER.
MetaCyc:PYRUVFORMLY-MONOMER.
BRENDA2.3.1.54. 2026.
UniPathwayUPA00920; UER00891.

Gene expression databases

GenevestigatorP09373.

Family and domain databases

InterProIPR005949. Form_AcTrfase.
IPR019777. Form_AcTrfase_GR_CS.
IPR001150. Gly_radical.
IPR004184. PFL_dom.
[Graphical view]
PfamPF01228. Gly_radical. 1 hit.
PF02901. PFL. 1 hit.
[Graphical view]
PIRSFPIRSF000379. For_Ac_trans_1. 1 hit.
TIGRFAMsTIGR01255. pyr_form_ly_1. 1 hit.
PROSITEPS00850. GLY_RADICAL_1. 1 hit.
PS51149. GLY_RADICAL_2. 1 hit.
PS51554. PFL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09373.
PROP09373.

Entry information

Entry namePFLB_ECOLI
AccessionPrimary (citable) accession number: P09373
Secondary accession number(s): P76826, Q47478
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Keywords

Controlled vocabulary of keywords

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene