Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P83223 (FRDA_SHEON) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fumarate reductase flavoprotein subunit

EC=1.3.5.4
Alternative name(s):
Flavocytochrome c
Short name=FL cyt
Gene names
Ordered Locus Names:SO_0970
OrganismShewanella oneidensis (strain MR-1) [Reference proteome] [HAMAP]
Taxonomic identifier211586 [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 + a quinone = fumarate + a quinol.

Cofactor

Binds 1 FAD per subunit.

Subunit structure

Monomer.

Subcellular location

Periplasm By similarity.

Induction

By anaerobiosis and fumarate. Ref.1

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
Reference proteome
Gene Ontology (GO)
   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal 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 [UniParc].

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

FASTA59662,448
        10         20         30         40         50         60 
MFTRKIQKTA LAMLISGAMA GTAYAAPEVL ADFHGEMGGC DSCHVSDKGG VTNDNLTHEN 

        70         80         90        100        110        120 
GQCVSCHGDL KELAAAAPKD KVSPHKSHLI GEIACTSCHK GHEKSVAYCD ACHSFGFDMP 

       130        140        150        160        170        180 
FGGKWERKFV PVDADKAAQD KAIAAGVKET TDVVIIGSGG AGLAAAVSAR DAGAKVILLE 

       190        200        210        220        230        240 
KEPIPGGNTK LAAGGMNAAE TKPQAKLGIE DKKQIMIDDT MKGGRNINDP ELVKVLANNS 

       250        260        270        280        290        300 
SDSIDWLTSM GADMTDVGRM GGASVNRSHR PTGGAGVGAH VAQVLWDNAV KRGTDIRLNS 

       310        320        330        340        350        360 
RVVRILEDAS GKVTGVLVKG EYTGYYVIKA DAVVIAAGGF AKNNERVSKY DPKLKGFKAT 

       370        380        390        400        410        420 
NHPGATGDGL DVALQAGAAT RDLEYIQAHP TYSPAGGVMI TEAVRGNGAI VVNREGNRFM 

       430        440        450        460        470        480 
NEITTRDKAS AAILQQKGES AYLVFDDSIR KSLKAIEGYV HLNIVKEGKT IEELAKQIDV 

       490        500        510        520        530        540 
PAAELAKTVT AYNGFVKSGK DAQFERPDLP RELVVAPFYA LEIAPAVHHT MGGLVIDTKA 

       550        560        570        580        590 
EVKSEKTGKP ITGLYAAGEV TGGVHGANRL GGNAISDIVT YGRIAGASAA KFAKDN 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a small tetraheme cytochrome c and a flavocytochrome c as two of the principal soluble cytochromes c in Shewanella oneidensis strain MR1."
Tsapin A.I., Vandenberghe I., Nealson K.H., Scott J.H., Meyer T.E., Cusanovich M.A., Harada E., Kaizu T., Akutsu H., Leys D., Van Beeumen J.J.
Appl. Environ. Microbiol. 67:3236-3244(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
Strain: MR-1.
[2]"Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis."
Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C., DeBoy R.T. expand/collapse author list , Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.
Nat. Biotechnol. 20:1118-1123(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MR-1.
[3]"Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1."
Leys D., Tsapin A.S., Nealson K.H., Meyer T.E., Cusanovich M.A., Van Beeumen J.J.
Nat. Struct. Biol. 6:1113-1117(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FAD; HEMES AND SUBSTRATE.
Strain: MR-1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014299 Genomic DNA. Translation: AAN54044.1.
RefSeqNP_716599.1. NC_004347.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D4CX-ray2.90A/B/C/D25-596[»]
1D4DX-ray2.50A25-596[»]
1D4EX-ray2.80A25-596[»]
ProteinModelPortalP83223.
SMRP83223. Positions 26-595.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING211586.SO_0970.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN54044; AAN54044; SO_0970.
GeneID1168814.
KEGGson:SO_0970.
PATRIC23521593. VBISheOne101494_0930.

Phylogenomic databases

eggNOGCOG1053.
HOGENOMHOG000227327.
KOK00244.
OMACDSCHSF.
OrthoDBEOG6XHC2W.
PhylomeDBP83223.

Family and domain databases

Gene3D1.10.1130.10. 1 hit.
3.90.700.10. 1 hit.
InterProIPR003953. FAD_bind_dom.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR010960. Flavocytochrome_c.
IPR011031. Multihaem_cyt.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR012286. Tetrahaem_cytochrome.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF56425. SSF56425. 1 hit.
TIGRFAMsTIGR01813. flavo_cyto_c. 1 hit.
PROSITEPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP83223.

Entry information

Entry nameFRDA_SHEON
AccessionPrimary (citable) accession number: P83223
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: November 25, 2002
Last modified: July 9, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references