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Reviewed, UniProtKB/Swiss-Prot Q07WU7 (FRDA_SHEFN)

Last modified November 25, 2008. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
    Flavocytochrome c3
      Short name=Fcc3
Gene names
Name: fccA
Synonyms: fcc3
Ordered Locus Names: Sfri_3690
OrganismShewanella frigidimarina (strain NCIMB 400) [Complete proteome] [HAMAP]
Taxonomic identifier318167 [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 By similarity.

Subunit structure

Monomer By similarity.

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 termComplete proteome
Direct protein sequencing

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
Chain26 – 596571Fumarate reductase flavoprotein subunit
PRO_0000269231

Regions

Domain26 – 142117Cytochrome c
Nucleotide binding154 – 16815FAD Potential
Nucleotide binding157 – 16812FAD By similarity
Nucleotide binding181 – 1822FAD By similarity
Nucleotide binding189 – 1902FAD By similarity
Nucleotide binding194 – 1963FAD By similarity
Nucleotide binding574 – 5752FAD By similarity
Region143 – 596454Flavoprotein-like

Sites

Active site4271Proton donor By similarity
Metal binding331Iron (heme 2 axial ligand)
Metal binding431Iron (heme 1 axial ligand)
Metal binding651Iron (heme 2 axial ligand)
Metal binding831Iron (heme 3 axial ligand)
Metal binding861Iron (heme 4 axial ligand)
Metal binding971Iron (heme 3 axial ligand)
Metal binding1001Iron (heme 1 axial ligand)
Metal binding1111Iron (heme 4 axial ligand)
Binding site391Heme 1 (covalent)
Binding site421Heme 1 (covalent)
Binding site611Heme 2 (covalent)
Binding site641Heme 2 (covalent)
Binding site931Heme 3 (covalent)
Binding site961Heme 3 (covalent)
Binding site1071Heme 4 (covalent)
Binding site1101Heme 4 (covalent)
Binding site3901Substrate By similarity
Binding site4021Substrate By similarity
Binding site5291Substrate By similarity
Binding site5691Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q07WU7-1 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: 914B69FD502BAC5B

FASTA59663,027
        10         20         30         40         50         60 
MKKMNLAVCI ATLMGTAGLM GTAVAADNLA EFHVQNQECD SCHTPDGELS NDSLTYENTQ 

        70         80         90        100        110        120 
CVSCHGTLAE VAETTKHEHY NAHASHFPGE VACTSCHSAH EKSMVYCDSC HSFDFNMPYA 

       130        140        150        160        170        180 
KKWLRDEPTI AELAKDKSER QAALASAPHD TVDVVVVGSG GAGFSAAISA TDSGAKVILI 

       190        200        210        220        230        240 
EKEPVIGGNA KLAAGGMNAA WTDQQKAKKI TDSPELMFED TMKGGQNIND PALVKVLSSH 

       250        260        270        280        290        300 
SKDSVDWMTA MGADLTDVGM MGGASVNRAH RPTGGAGVGA HVVQVLYDNA VKRNIDLRMN 

       310        320        330        340        350        360 
TRGIEVLKDD KGTVKGILVK GMYKGYYWVK ADAVILATGG FAKNNERVAK LDPSLKGFIS 

       370        380        390        400        410        420 
TNQPGAVGDG LDVAENAGGA LKDMQYIQAH PTLSVKGGVM VTEAVRGNGA ILVNREGKRF 

       430        440        450        460        470        480 
VNEITTRDKA SAAILAQTGK SAYLIFDDSV RKSLSKIDKY IGLGVAPTAD SLVKLGKMEG 

       490        500        510        520        530        540 
IDGKALTETV ARYNSLVSSG KDTDFERPNL PRALNEGNYY AIEVTPGVHH TMGGVMIDTK 

       550        560        570        580        590 
AEVMNAKKQV IPGLYGAGEV TGGVHGANRL GGNAISDIIT FGRLAGEEAA KYSKKN 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens: a tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-bound enzymes from other bacteria."
Pealing S.L., Black A.C., Manson F.D.C., Ward F.B., Chapman S.K., Reid G.A.
Biochemistry 31:12132-12140(1992) [PubMed: 1333793] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-38.
[2]"Complete sequence of Shewanella frigidimarina NCIMB 400."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H., Newman D., Tiedje J.M. expand/collapse author list , Zhou J., Romine M.F., Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

L04283 Genomic DNA. Translation: AAA70385.1.
CP000447 Genomic DNA. Translation: ABI73517.1. Different initiation.
RefSeqYP_752356.1.

3D structure databases

SMRQ07WU7. Positions 26-593.
ModBaseSearch...

Genome annotation databases

GeneID4280583.
GenomeReviewsGene locus Sfri_3690 in contig CP000447_GR.
KEGGsfr:Sfri_3690.
NMPDRfig|318167.10.peg.3515.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ07WU7.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
IPR012286. Fcc3_N_cyt.
IPR010960. Flavocytochrome_c.
IPR011031. Multihaem_cyt.
[Graphical view]
Gene3DG3DSA:1.10.1130.10. Fcc3_N_cyt. 1 hit.
PfamPF00890. FAD_binding_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR01813. flavo_cyto_c. 1 hit.
PROSITEPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRDA_SHEFN
AccessionPrimary (citable) accession number: Q07WU7
Secondary accession number(s): Q02469, Q9X969
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: November 25, 2008
This is version 18 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents