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ECOLI:FER

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) fdx
Protein Name(s) 2Fe-2S ferredoxin
External Links
UniProt P0A9R4
EMBL M88654
U05338
U01827
U00096
AP009048
PIR JC1110
RefSeq NP_417020.1
YP_490753.1
PDB 1I7H
PDBsum 1I7H
ProteinModelPortal P0A9R4
SMR P0A9R4
DIP DIP-48512N
IntAct P0A9R4
STRING 511145.b2525
PaxDb P0A9R4
PRIDE P0A9R4
EnsemblBacteria AAC75578
BAA16415
GeneID 12931590
947160
KEGG ecj:Y75_p2478
eco:b2525
PATRIC 32120445
EchoBASE EB1304
EcoGene EG11328
eggNOG COG0633
HOGENOM HOG000244519
InParanoid P0A9R4
KO K04755
OMA SACGGVC
OrthoDB EOG6KMB9X
PhylomeDB P0A9R4
BioCyc EcoCyc:FERREDOXIN-MONOMER
ECOL316407:JW2509-MONOMER
MetaCyc:FERREDOXIN-MONOMER
EvolutionaryTrace P0A9R4
PRO PR:P0A9R4
Proteomes UP000000318
UP000000625
Genevestigator P0A9R4
GO GO:0051537
GO:0009055
GO:0046872
GO:0016226
GO:0055114
Gene3D 3.10.20.30
InterPro IPR001041
IPR001055
IPR018298
IPR012675
IPR011536
Pfam PF00111
PRINTS PR00355
SUPFAM SSF54292
TIGRFAMs TIGR02007
PROSITE PS51085
PS00814

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:1900489

positive regulation of [2Fe-2S] cluster assembly

PMID:23019358[1]

ECO:0000247

UniProtKB:

P

Fig. 2. Resonance Raman spectra of the O2-induced [4Fe-4S]2+ to [2Fe-2S]2+ cluster conversion of FNR with natural abundance (black spectra) and 34S-labeled (red spectra) bridging sulfides. (A) [4Fe-4S]-FNR prepared by anaerobic reconstitution.

complete
CACAO 10703

enables

GO:0051537

2 iron, 2 sulfur cluster binding

PMID:4375562[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0016226

iron-sulfur cluster assembly

PMID:23682711[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A6B7

P

Seeded From UniProt

complete

involved_in

GO:0016226

iron-sulfur cluster assembly

PMID:11432781[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0009055

electron transfer activity

PMID:23682711[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0022900

electron transport chain

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0009055

P

Seeded From UniProt

complete

involved_in

GO:0022900

electron transport chain

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0009055

P

Seeded From UniProt

complete

enables

GO:0009055

electron transfer activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001041
InterPro:IPR001055
InterPro:IPR011536
InterPro:IPR018298
InterPro:IPR036010

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:IPR001041
InterPro:IPR036010

F

Seeded From UniProt

complete

enables

GO:0051537

2 iron, 2 sulfur cluster binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001055
InterPro:IPR011536
InterPro:IPR018298

F

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

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0249

P

Seeded From UniProt

complete

enables

GO:0051537

2 iron, 2 sulfur cluster binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0001

F

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. Zhang, B et al. (2012) Reversible cycling between cysteine persulfide-ligated [2Fe-2S] and cysteine-ligated [4Fe-4S] clusters in the FNR regulatory protein. Proc. Natl. Acad. Sci. U.S.A. 109 15734-9 PubMed GONUTS page
  2. Knoell, HE & Knappe, J (1974) Escherichia coli ferredoxin, an iron-sulfur protein of the adrenodoxin type. Eur. J. Biochem. 50 245-52 PubMed GONUTS page
  3. 3.0 3.1 Kim, JH et al. (2013) [2Fe-2S]-ferredoxin binds directly to cysteine desulfurase and supplies an electron for iron-sulfur cluster assembly but is displaced by the scaffold protein or bacterial frataxin. J. Am. Chem. Soc. 135 8117-20 PubMed GONUTS page
  4. Tokumoto, U & Takahashi, Y (2001) Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins. J. Biochem. 130 63-71 PubMed GONUTS page
  5. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page