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Reviewed, UniProtKB/Swiss-Prot P83223 (FRDA_SHEON)

Last modified November 25, 2008. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Fumarate reductase flavoprotein subunit
    EC=1.3.99.1
Alternative name(s):
    Flavocytochrome c
      Short name=FL cyt
Gene names
Ordered Locus Names: SO_0970
OrganismShewanella oneidensis [Complete proteome] [HAMAP]
Taxonomic identifier70863 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length596 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown, but evidence indicates that flavocytochrome c participates in electron transfer from formate to fumarate and possibly also to trimethylamine oxide (TMAO). This enzyme is essentially unidirectional By similarity.

Catalytic activity

Succinate + acceptor = fumarate + reduced acceptor.

Cofactor

Binds 1 FAD per subunit.

Subunit structure

Monomer.

Subcellular location

PeriplasmBy similarity.

Induction

By anaerobiosis and fumarate.

Sequence similarities

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

Contains 1 cytochrome c domain.

Ontologies

Keywords

   Biological processElectron transport
Transport
   Cellular componentPeriplasm
   DomainSignal
   LigandFAD
Flavoprotein
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome

Gene Ontology (GO)

   Biological processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

succinate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Probable
Chain26 – 596571Fumarate reductase flavoprotein subunit
PRO_0000010345

Regions

Domain26 – 141116Cytochrome c
Nucleotide binding156 – 16712FAD
Nucleotide binding180 – 1812FAD
Nucleotide binding187 – 1893FAD
Nucleotide binding193 – 1953FAD
Nucleotide binding572 – 5754FAD
Region142 – 596455Flavoprotein-like

Sites

Active site4261Proton donor By similarity
Metal binding341Iron (heme 2 axial ligand)
Metal binding441Iron (heme 1 axial ligand)
Metal binding671Iron (heme 2 axial ligand)
Metal binding851Iron (heme 3 axial ligand)
Metal binding881Iron (heme 4 axial ligand)
Metal binding991Iron (heme 3 axial ligand)
Metal binding1021Iron (heme 1 axial ligand)
Metal binding1131Iron (heme 4 axial ligand)
Binding site401Heme 1 (covalent)
Binding site431Heme 1 (covalent)
Binding site631Heme 2 (covalent)
Binding site661Heme 2 (covalent)
Binding site951Heme 3 (covalent)
Binding site981Heme 3 (covalent)
Binding site1091Heme 4 (covalent)
Binding site1121Heme 4 (covalent)
Binding site3891Substrate
Binding site4011Substrate
Binding site5281Substrate
Binding site5691Substrate

Experimental info

Sequence conflict711K → E Ref.1
Sequence conflict2821A → S Ref.1

Secondary structure

................................................................................................... 596
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P83223-1 [UniParc].

Last modified November 25, 2002. Version 2.
Checksum: 74CB81FE89790463

FASTA59662,448