Formate acetyltransferase 1 - Escherichia coli (strain K12)

Preferred order of sections

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	760 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
PTM	Acetylation Organic radical
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	anaerobic respiration Inferred from expression pattern PubMed 6758723. Source: EcoCyc glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay PubMed 16858726. Source: UniProtKB membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	formate C-acetyltransferase activity Inferred from direct assay PubMed 4615902. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
mgtA	P0ABB8	1	EBI-546682,EBI-556753

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed Ref.7

Chain

2 – 760

759

Formate acetyltransferase 1

PRO_0000166687

Regions

Domain

3 – 625

623

PFL

Domain

632 – 760

129

Glycine radical

Sites

Active site

419

1

S-acetylcysteine intermediate

Active site

420

1

Cysteine radical intermediate

Amino acid modifications

Modified residue

63

1

N6-acetyllysine; alternate Ref.9

Modified residue

63

1

N6-succinyllysine; alternate Ref.10

Modified residue

107

1

N6-succinyllysine Ref.10

Modified residue

117

1

N6-acetyllysine; alternate Ref.9

Modified residue

117

1

N6-succinyllysine; alternate Ref.10

Modified residue

124

1

N6-acetyllysine; alternate

Modified residue

124

1

N6-succinyllysine; alternate Ref.10

Modified residue

195

1

N6-acetyllysine; alternate Ref.9

Modified residue

195

1

N6-succinyllysine; alternate Ref.10

Modified residue

454

1

N6-acetyllysine; alternate Ref.9

Modified residue

454

1

N6-succinyllysine; alternate Ref.10

Modified residue

467

1

N6-succinyllysine Ref.10

Modified residue

541

1

N6-acetyllysine Ref.9

Modified residue

591

1

N6-acetyllysine Ref.9

Modified residue

654

1

N6-succinyllysine Ref.10

Modified residue

735

1

Glycine radical

Secondary structure

1

.

760

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P09373 [UniParc].

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

FASTA

760

85,357

        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' referencesShow '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. 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 277:1453-1474(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, 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.

PIR

S01788.

RefSeq

NP_415423.1. NC_000913.2.
YP_489175.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CM5	X-ray	2.30	A/B	2-760	[»]
1H16	X-ray	1.53	A	2-759	[»]
1H17	X-ray	1.75	A	2-759	[»]
1H18	X-ray	2.30	A/B	2-759	[»]
1MZO	X-ray	2.70	A/B	2-759	[»]
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	[»]

ProteinModelPortal

P09373.

SMR

P09373. Positions 2-760.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10467N.

IntAct

P09373. 41 interactions.

MINT

MINT-1283506.

STRING

511145.b0903.

2D gel databases

SWISS-2DPAGE

P09373.

Proteomic databases

PaxDb

P09373.

PRIDE

P09373.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73989; AAC73989; b0903.
BAA35638; BAA35638; BAA35638.

GeneID

12931841.
945514.

KEGG

ecj:Y75_p0875.
eco:b0903.

PATRIC

32117019. VBIEscCol129921_0934.

Organism-specific databases

EchoBASE

EB0695.

EcoGene

EG10701. pflB.

Phylogenomic databases

eggNOG

COG1882.

HOGENOM

HOG000011346.

KO

K00656.

OMA

FLRTPDY.

ProtClustDB

CLSK869953.

Enzyme and pathway databases

BioCyc

EcoCyc:PYRUVFORMLY-MONOMER.
ECOL316407:JW0886-MONOMER.
MetaCyc:PYRUVFORMLY-MONOMER.

BRENDA

2.3.1.54. 2026.

UniPathway

UPA00920; UER00891.

Gene expression databases

Genevestigator

P09373.

Family and domain databases

InterPro

IPR005949. Form_AcTrfase.
IPR019777. Form_AcTrfase_GR_CS.
IPR001150. Gly_radical.
IPR004184. PFL_dom.
[Graphical view]

Pfam

PF01228. Gly_radical. 1 hit.
PF02901. PFL. 1 hit.
[Graphical view]

PIRSF

PIRSF000379. For_Ac_trans_1. 1 hit.

TIGRFAMs

TIGR01255. pyr_form_ly_1. 1 hit.

PROSITE

PS00850. GLY_RADICAL_1. 1 hit.
PS51149. GLY_RADICAL_2. 1 hit.
PS51554. PFL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P09373.

Entry information

Entry name

PFLB_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Keywords

Controlled vocabulary of keywords

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents