Q9Z4P0 · IFCA_SHEFN

Function

function

Flavocytochrome that catalyzes the reduction of fumarate to succinate in vitro (PubMed:10455032).
Is essentially unidirectional, catalyzing only fumarate reduction (PubMed:10455032).
In vitro, can use the artificial electron donor methyl viologen (PubMed:10455032).
May be involved in an alternative route for electron transport to Fe3+ (PubMed:10455032).

Cofactor

Protein has several cofactor binding sites:
FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.
heme c (UniProtKB | Rhea| CHEBI:61717 )

Note: Binds 4 heme c groups covalently per monomer.

Features

Showing features for binding site, active site.

158850100150200250300350400450500550
TypeIDPosition(s)Description
Binding site31Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue
Binding site37heme c 1 (UniProtKB | ChEBI); covalent
Binding site40heme c 1 (UniProtKB | ChEBI); covalent
Binding site41Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue
Binding site58heme c 2 (UniProtKB | ChEBI); covalent
Binding site61heme c 2 (UniProtKB | ChEBI); covalent
Binding site62Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue
Binding site78Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue
Binding site81Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue
Binding site87heme c 3 (UniProtKB | ChEBI); covalent
Binding site90heme c 3 (UniProtKB | ChEBI); covalent
Binding site91Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue
Binding site93heme c 1 (UniProtKB | ChEBI)
Binding site94Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue
Binding site101heme c 4 (UniProtKB | ChEBI); covalent
Binding site104heme c 4 (UniProtKB | ChEBI); covalent
Binding site105Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue
Binding site154FAD (UniProtKB | ChEBI)
Binding site173FAD (UniProtKB | ChEBI)
Binding site181FAD (UniProtKB | ChEBI)
Binding site182FAD (UniProtKB | ChEBI)
Binding site187FAD (UniProtKB | ChEBI)
Binding site187fumarate (UniProtKB | ChEBI)
Binding site187succinate (UniProtKB | ChEBI)
Binding site188FAD (UniProtKB | ChEBI)
Binding site218heme c 2 (UniProtKB | ChEBI)
Binding site295FAD (UniProtKB | ChEBI)
Binding site361FAD (UniProtKB | ChEBI)
Binding site382succinate (UniProtKB | ChEBI)
Binding site394fumarate (UniProtKB | ChEBI)
Binding site394succinate (UniProtKB | ChEBI)
Binding site395fumarate (UniProtKB | ChEBI)
Binding site395succinate (UniProtKB | ChEBI)
Active site419Proton donor
Binding site521fumarate (UniProtKB | ChEBI)
Binding site521succinate (UniProtKB | ChEBI)
Binding site551FAD (UniProtKB | ChEBI)
Binding site561fumarate (UniProtKB | ChEBI)
Binding site561succinate (UniProtKB | ChEBI)
Binding site564FAD (UniProtKB | ChEBI)
Binding site564fumarate (UniProtKB | ChEBI)
Binding site564succinate (UniProtKB | ChEBI)
Binding site566FAD (UniProtKB | ChEBI)
Binding site567FAD (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentperiplasmic space
Molecular FunctionFMN binding
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity
Biological Processsteroid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable fumarate reductase Ifc3
  • EC number
  • Alternative names
    • Fe(3+)-induced flavocytochrome C3
    • Iron-induced flavocytochrome C3
      (Ifc3
      )

Gene names

    • Name
      ifcA
    • Ordered locus names
      Sfri_2586

Organism names

Accessions

  • Primary accession
    Q9Z4P0
  • Secondary accessions
    • Q07ZY8

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Chemistry

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-22
ChainPRO_000001034623-588Probable fumarate reductase Ifc3

Expression

Induction

By anaerobic growth on Fe3+ ions (PubMed:10455032).
Not expressed in cells cultured either anaerobically with other soluble respiratory substrates or microaerobically (PubMed:10455032).

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region135-588Flavoprotein-like

Sequence similarities

In the C-terminal section; belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    588
  • Mass (Da)
    62,946
  • Last updated
    1999-05-01 v1
  • Checksum
    99C4AE25814693D2
MKLKYLVSAMALVVLSSGTAMAKTPDMGSFHADMGSCQSCHAKPIKVTDSETHENAQCKSCHGEYAELANDKLQFDPHNSHLGDINCTSCHKGHEEPKFYCNECHSFDIKPMPFSDAKKKKSWDDGWDQDKIQKAIAAGPSETTQVLVVGAGSAGFNASLAAKKAGANVILVDKAPFSGGNSMISAGGMNAVGTKQQTAHGVEDKVEWFIEDAMKGGRQQNDIKLVTILAEQSADGVQWLESLGANLDDLKRSGGARVDRTHRPHGGKSSGPEIIDTLRKAAKEQGIDTRLNSRVVKLVVNDDHSVVGAVVHGKHTGYYMIGAKSVVLATGGYGMNKEMIAYYRPTMKDMTSSNNITATGDGVLMAKEIGASMTDIDWVQAHPTVGKDSRILISETVRGVGAVMVNKDGNRFISELTTRDKASDAILKQPGQFAWIIFDNQLYKKAKMVRGYDHLEMLYKGDTVEQLAKSTGMKVADLAKTVSDYNGYVASGKDTAFGRADMPLNMTQSPYYAVKVAPGIHHTMGGVAINTTASVLDLQSKPIDGLFAAGEVTGGVHGYNRLGGNAIADTVVFGRIAGDNAAKHALDK

Mass Spectrometry

Molecular mass is 63,985 Da. Determined by MALDI.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ236923
EMBL· GenBank· DDBJ
CAB37062.1
EMBL· GenBank· DDBJ
Genomic DNA
CP000447
EMBL· GenBank· DDBJ
ABI72427.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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