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P09373

- PFLB_ECOLI

UniProt

P09373 - PFLB_ECOLI

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Protein
Formate acetyltransferase 1
Gene
pflB, pfl, b0903, JW0886
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

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.

Miscellaneous databases

EvolutionaryTraceiP09373.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 625623PFL
Add
BLAST
Domaini632 – 760129Glycine radical
Add
BLAST

Sequence similaritiesi

Contains 1 PFL domain.

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 150 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

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