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ECOLI:PFLA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) pflA (synonyms: act)
Protein Name(s) Pyruvate formate-lyase 1-activating enzyme

Formate-C-acetyltransferase-activating enzyme 1 PFL-activating enzyme 1

External Links
UniProt P0A9N4
EMBL X08035
U00096
AP009048
PIR S01789
RefSeq NP_415422.1
YP_489174.1
PDB 3C8F
3CB8
PDBsum 3C8F
3CB8
ProteinModelPortal P0A9N4
SMR P0A9N4
DIP DIP-35915N
IntAct P0A9N4
STRING 511145.b0902
PaxDb P0A9N4
PRIDE P0A9N4
EnsemblBacteria AAC73988
BAA35637
GeneID 12930359
945517
KEGG ecj:Y75_p0874
eco:b0902
PATRIC 32117017
EchoBASE EB0027
EcoGene EG10028
eggNOG COG1180
HOGENOM HOG000011458
InParanoid P0A9N4
KO K04069
OMA CHNPDCR
OrthoDB EOG64FKHC
PhylomeDB P0A9N4
BioCyc EcoCyc:PFLACTENZ-MONOMER
ECOL316407:JW0885-MONOMER
EvolutionaryTrace P0A9N4
PRO PR:P0A9N4
Proteomes UP000000318
UP000000625
Genevestigator P0A9N4
GO GO:0005737
GO:0051539
GO:0043365
GO:0046872
GO:0016491
GO:0006974
GO:0006006
InterPro IPR006638
IPR012838
IPR001989
IPR007197
Pfam PF04055
SMART SM00729
TIGRFAMs TIGR02493
PROSITE PS01087

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0016491

oxidoreductase activity

ECO:0000314

F

Fig. 2 illustrates that the over-expression of PflA allows for greater use of iron-sulfur clusters in anaerobic environments.

complete

enables

GO:0016491

oxidoreductase activity

PMID:19711960[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

PMID:11967071[2]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

PMID:9478932[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0043365

[formate-C-acetyltransferase]-activating enzyme activity

PMID:6364987[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0018307

enzyme active site formation

PMID:6364987[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[5]

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:IPR007197
InterPro:IPR013785

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001989
InterPro:IPR012839

F

Seeded From UniProt

complete

enables

GO:0043365

[formate-C-acetyltransferase]-activating enzyme activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012838

F

Seeded From UniProt

complete

enables

GO:0051536

iron-sulfur cluster binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR007197

F

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001989

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001989
InterPro:IPR012838
InterPro:IPR012839

P

Seeded From UniProt

complete

enables

GO:0043365

[formate-C-acetyltransferase]-activating enzyme activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.97.1.4

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

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

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0004

F

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:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

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:0051536

iron-sulfur cluster binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0411

F

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 Yang, J et al. (2009) The iron-sulfur cluster of pyruvate formate-lyase activating enzyme in whole cells: cluster interconversion and a valence-localized [4Fe-4S]2+ state. Biochemistry 48 9234-41 PubMed GONUTS page
  2. Khil, PP & Camerini-Otero, RD (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli. Mol. Microbiol. 44 89-105 PubMed GONUTS page
  3. Külzer, R et al. (1998) Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. Molecular properties of the holoenzyme form. J. Biol. Chem. 273 4897-903 PubMed GONUTS page
  4. 4.0 4.1 Conradt, H et al. (1984) Pyruvate formate-lyase (inactive form) and pyruvate formate-lyase activating enzyme of Escherichia coli: isolation and structural properties. Arch. Biochem. Biophys. 228 133-42 PubMed GONUTS page
  5. 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