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Protein

Formate acetyltransferase 1

Gene

pflB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acetyl-CoA + formate = CoA + pyruvate.

Pathwayi: pyruvate fermentation

This protein is involved in step 1 of the subpathway that synthesizes formate from pyruvate.
Proteins known to be involved in this subpathway in this organism are:
  1. Putative formate acetyltransferase 3 (ybiW), Formate acetyltransferase 1 (pflB), Formate acetyltransferase 2 (pflD)
This subpathway is part of the pathway pyruvate fermentation, which is itself part of Fermentation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes formate from pyruvate, the pathway pyruvate fermentation and in Fermentation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei419S-acetylcysteine intermediate1
Active sitei420Cysteine radical intermediate1

GO - Molecular functioni

  • formate C-acetyltransferase activity Source: EcoCyc

GO - Biological processi

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10701. pflB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001666872 – 760Formate acetyltransferase 1Add BLAST759

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei63N6-acetyllysine; alternate1 Publication1
Modified residuei63N6-succinyllysine; alternate1 Publication1
Modified residuei107N6-succinyllysine1 Publication1
Modified residuei117N6-acetyllysine; alternate1 Publication1
Modified residuei117N6-succinyllysine; alternate1 Publication1
Modified residuei124N6-succinyllysine1 Publication1
Modified residuei195N6-acetyllysine; alternate1 Publication1
Modified residuei195N6-succinyllysine; alternate1 Publication1
Modified residuei454N6-acetyllysine; alternate1 Publication1
Modified residuei454N6-succinyllysine; alternate1 Publication1
Modified residuei467N6-succinyllysine1 Publication1
Modified residuei541N6-acetyllysine1 Publication1
Modified residuei591N6-acetyllysine1 Publication1
Modified residuei654N6-succinyllysine1 Publication1
Modified residuei735Glycine radical1

Keywords - PTMi

Acetylation, Organic radical

Proteomic databases

EPDiP09373.
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.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi4260835. 7 interactors.
DIPiDIP-10467N.
IntActiP09373. 42 interactors.
MINTiMINT-1283506.
STRINGi511145.b0903.

Structurei

Secondary structure

1760
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 11Combined sources6
Turni12 – 14Combined sources3
Helixi19 – 21Combined sources3
Helixi26 – 33Combined sources8
Helixi41 – 43Combined sources3
Helixi49 – 68Combined sources20
Beta strandi72 – 79Combined sources8
Beta strandi82 – 85Combined sources4
Turni92 – 94Combined sources3
Beta strandi101 – 104Combined sources4
Beta strandi107 – 110Combined sources4
Helixi112 – 114Combined sources3
Helixi117 – 125Combined sources9
Helixi132 – 140Combined sources9
Helixi145 – 152Combined sources8
Helixi155 – 162Combined sources8
Beta strandi164 – 167Combined sources4
Beta strandi172 – 174Combined sources3
Helixi183 – 188Combined sources6
Helixi190 – 202Combined sources13
Helixi205 – 210Combined sources6
Turni211 – 213Combined sources3
Helixi214 – 240Combined sources27
Helixi252 – 269Combined sources18
Helixi281 – 293Combined sources13
Helixi299 – 313Combined sources15
Helixi322 – 327Combined sources6
Beta strandi336 – 340Combined sources5
Beta strandi346 – 348Combined sources3
Helixi352 – 363Combined sources12
Beta strandi370 – 376Combined sources7
Helixi382 – 395Combined sources14
Beta strandi399 – 402Combined sources4
Helixi403 – 410Combined sources8
Beta strandi415 – 418Combined sources4
Turni419 – 421Combined sources3
Beta strandi422 – 425Combined sources4
Turni426 – 428Combined sources3
Beta strandi429 – 438Combined sources10
Helixi439 – 447Combined sources9
Turni448 – 450Combined sources3
Turni453 – 455Combined sources3
Beta strandi468 – 470Combined sources3
Helixi473 – 505Combined sources33
Helixi509 – 512Combined sources4
Beta strandi520 – 528Combined sources9
Helixi530 – 542Combined sources13
Beta strandi543 – 549Combined sources7
Beta strandi555 – 562Combined sources8
Beta strandi567 – 570Combined sources4
Helixi572 – 590Combined sources19
Helixi595 – 597Combined sources3
Beta strandi599 – 604Combined sources6
Helixi609 – 615Combined sources7
Turni638 – 640Combined sources3
Helixi645 – 653Combined sources9
Helixi657 – 659Combined sources3
Beta strandi667 – 670Combined sources4
Helixi672 – 675Combined sources4
Helixi679 – 694Combined sources16
Beta strandi705 – 710Combined sources6
Helixi713 – 721Combined sources9
Helixi723 – 725Combined sources3
Beta strandi730 – 732Combined sources3
Beta strandi734 – 739Combined sources6
Helixi740 – 742Combined sources3
Helixi745 – 752Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09373.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 625PFLPROSITE-ProRule annotationAdd BLAST623
Domaini632 – 760Glycine radicalPROSITE-ProRule annotationAdd BLAST129

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C6N. Bacteria.
COG1882. LUCA.
HOGENOMiHOG000011346.
InParanoidiP09373.
KOiK00656.
OMAiKATSALW.
PhylomeDBiP09373.

Family and domain databases

CDDicd01678. PFL1. 1 hit.
InterProiIPR005949. Form_AcTrfase.
IPR019777. Form_AcTrfase_GR_CS.
IPR001150. Gly_radical.
IPR004184. PFL_dom.
[Graphical view]
PfamiPF01228. Gly_radical. 1 hit.
PF02901. PFL-like. 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

        10         20         30         40         50
MSELNEKLAT AWEGFTKGDW QNEVNVRDFI QKNYTPYEGD ESFLAGATEA
60 70 80 90 100
TTTLWDKVME GVKLENRTHA PVDFDTAVAS TITSHDAGYI NKQLEKIVGL
110 120 130 140 150
QTEAPLKRAL IPFGGIKMIE GSCKAYNREL DPMIKKIFTE YRKTHNQGVF
160 170 180 190 200
DVYTPDILRC RKSGVLTGLP DAYGRGRIIG DYRRVALYGI DYLMKDKLAQ
210 220 230 240 250
FTSLQADLEN GVNLEQTIRL REEIAEQHRA LGQMKEMAAK YGYDISGPAT
260 270 280 290 300
NAQEAIQWTY FGYLAAVKSQ NGAAMSFGRT STFLDVYIER DLKAGKITEQ
310 320 330 340 350
EAQEMVDHLV MKLRMVRFLR TPEYDELFSG DPIWATESIG GMGLDGRTLV
360 370 380 390 400
TKNSFRFLNT LYTMGPSPEP NMTILWSEKL PLNFKKFAAK VSIDTSSLQY
410 420 430 440 450
ENDDLMRPDF NNDDYAIACC VSPMIVGKQM QFFGARANLA KTMLYAINGG
460 470 480 490 500
VDEKLKMQVG PKSEPIKGDV LNYDEVMERM DHFMDWLAKQ YITALNIIHY
510 520 530 540 550
MHDKYSYEAS LMALHDRDVI RTMACGIAGL SVAADSLSAI KYAKVKPIRD
560 570 580 590 600
EDGLAIDFEI EGEYPQFGNN DPRVDDLAVD LVERFMKKIQ KLHTYRDAIP
610 620 630 640 650
TQSVLTITSN VVYGKKTGNT PDGRRAGAPF GPGANPMHGR DQKGAVASLT
660 670 680 690 700
SVAKLPFAYA KDGISYTFSI VPNALGKDDE VRKTNLAGLM DGYFHHEASI
710 720 730 740 750
EGGQHLNVNV MNREMLLDAM ENPEKYPQLT IRVSGYAVRF NSLTKEQQQD
760
VITRTFTQSM
Length:760
Mass (Da):85,357
Last modified:January 23, 2007 - v2
Checksum:i19323C63081625D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_001292822.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73989; AAC73989; b0903.
BAA35638; BAA35638; BAA35638.
GeneIDi945514.
KEGGiecj:JW0886.
eco:b0903.
PATRICi32117019. VBIEscCol129921_0934.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_001292822.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260835. 7 interactors.
DIPiDIP-10467N.
IntActiP09373. 42 interactors.
MINTiMINT-1283506.
STRINGi511145.b0903.

2D gel databases

SWISS-2DPAGEP09373.

Proteomic databases

EPDiP09373.
PaxDbiP09373.
PRIDEiP09373.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73989; AAC73989; b0903.
BAA35638; BAA35638; BAA35638.
GeneIDi945514.
KEGGiecj:JW0886.
eco:b0903.
PATRICi32117019. VBIEscCol129921_0934.

Organism-specific databases

EchoBASEiEB0695.
EcoGeneiEG10701. pflB.

Phylogenomic databases

eggNOGiENOG4105C6N. Bacteria.
COG1882. LUCA.
HOGENOMiHOG000011346.
InParanoidiP09373.
KOiK00656.
OMAiKATSALW.
PhylomeDBiP09373.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP09373.
PROiP09373.

Family and domain databases

CDDicd01678. PFL1. 1 hit.
InterProiIPR005949. Form_AcTrfase.
IPR019777. Form_AcTrfase_GR_CS.
IPR001150. Gly_radical.
IPR004184. PFL_dom.
[Graphical view]
PfamiPF01228. Gly_radical. 1 hit.
PF02901. PFL-like. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 166 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.