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ECOLI:PFLB

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) pflB (synonyms: pfl)
Protein Name(s) Formate acetyltransferase 1

Pyruvate formate-lyase 1

External Links
UniProt P09373
EMBL X08035
U00096
AP009048
M26413
PIR S01788
RefSeq NP_415423.1
YP_489175.1
PDB 1CM5
1H16
1H17
1H18
1MZO
1QHM
2PFL
3PFL
PDBsum 1CM5
1H16
1H17
1H18
1MZO
1QHM
2PFL
3PFL
ProteinModelPortal P09373
SMR P09373
DIP DIP-10467N
IntAct P09373
MINT MINT-1283506
STRING 511145.b0903
SWISS-2DPAGE P09373
PaxDb P09373
PRIDE P09373
EnsemblBacteria AAC73989
BAA35638
GeneID 12931841
945514
KEGG ecj:Y75_p0875
eco:b0903
PATRIC 32117019
EchoBASE EB0695
EcoGene EG10701
eggNOG COG1882
HOGENOM HOG000011346
InParanoid P09373
KO K00656
OMA YDKIMSG
OrthoDB EOG6Q8J0J
PhylomeDB P09373
BioCyc EcoCyc:PYRUVFORMLY-MONOMER
ECOL316407:JW0886-MONOMER
MetaCyc:PYRUVFORMLY-MONOMER
BRENDA 2.3.1.54
UniPathway UPA00920
EvolutionaryTrace P09373
PRO PR:P09373
Proteomes UP000000318
UP000000625
Genevestigator P09373
GO GO:0005737
GO:0016020
GO:0008861
GO:0009061
GO:0006006
InterPro IPR005949
IPR019777
IPR001150
IPR004184
Pfam PF01228
PF02901
PIRSF PIRSF000379
TIGRFAMs TIGR01255
PROSITE PS00850
PS51149
PS51554

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0016020

membrane

PMID:16858726[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008861

formate C-acetyltransferase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10701
EcoGene:EG11784
EcoGene:EG12758
PANTHER:PTN000766230

F

Seeded From UniProt

complete

involved_in

GO:0006567

threonine catabolic process

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12758
PANTHER:PTN000766230

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10701
EcoGene:EG11784
PANTHER:PTN000766230

C

Seeded From UniProt

complete

enables

GO:0008861

formate C-acetyltransferase activity

PMID:4615902[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:17309111[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001150
InterPro:IPR004184

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005949

C

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005949

P

Seeded From UniProt

complete

enables

GO:0008861

formate C-acetyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005949

F

Seeded From UniProt

complete

enables

GO:0008861

formate C-acetyltransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.3.1.54

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0119

P

Seeded From UniProt

complete

enables

GO:0016746

transferase activity, transferring acyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0012

F

Seeded From UniProt

complete

involved_in

GO:0006006

glucose metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0313

P

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  2. 2.0 2.1 2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. Knappe, J et al. (1974) Pyruvate formate-lyase of Escherichia coli: the acetyl-enzyme intermediate. Eur. J. Biochem. 50 253-63 PubMed GONUTS page
  4. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  5. Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page
  6. Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page