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Q9Z4P0 (FRD2_SHEFN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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=1.3.99.1
Alternative name(s):
Fe(3+)-induced flavocytochrome C3
Short name=Ifc3
Iron(III)-induced flavocytochrome C3
Gene names
Name:ifcA
Ordered Locus Names:Sfri_2586
OrganismShewanella frigidimarina (strain NCIMB 400) [Complete proteome] [HAMAP]
Taxonomic identifier318167 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length588 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes unidirectional fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown.

Catalytic activity

Succinate + acceptor = fumarate + reduced acceptor.

Cofactor

Binds 1 FAD per subunit.

Subunit structure

Homodimer Probable.

Subcellular location

Periplasm.

Induction

By anaerobic growth on Fe3+ ions.

Sequence similarities

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

Contains 1 cytochrome c domain.

Mass spectrometry

Molecular mass is 63985±0.1 Da from positions 23 - 588. Determined by MALDI. Ref.1

Ontologies

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

   Molecular functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

succinate dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.1
Chain23 – 588566Fumarate reductase flavoprotein subunit
PRO_0000010346

Regions

Domain24 – 134111Cytochrome c
Nucleotide binding146 – 16015FAD Potential
Region135 – 588454Flavoprotein-like

Sites

Active site3821 By similarity
Active site3981 By similarity
Metal binding311Iron (heme 2 axial ligand)
Metal binding411Iron (heme 1 axial ligand)
Metal binding621Iron (heme 2 axial ligand)
Metal binding781Iron (heme 3 axial ligand)
Metal binding811Iron (heme 4 axial ligand)
Metal binding911Iron (heme 3 axial ligand)
Metal binding941Iron (heme 1 axial ligand)
Metal binding1051Iron (heme 4 axial ligand)
Binding site371Heme 1 (covalent)
Binding site401Heme 1 (covalent)
Binding site581Heme 2 (covalent)
Binding site611Heme 2 (covalent)
Binding site871Heme 3 (covalent)
Binding site901Heme 3 (covalent)
Binding site1011Heme 4 (covalent)
Binding site1041Heme 4 (covalent)

Secondary structure

1 ............................................................................................ 588
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Z4P0 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 99C4AE25814693D2

FASTA58862,946
        10         20         30         40         50         60 
MKLKYLVSAM ALVVLSSGTA MAKTPDMGSF HADMGSCQSC HAKPIKVTDS ETHENAQCKS 

        70         80         90        100        110        120 
CHGEYAELAN DKLQFDPHNS HLGDINCTSC HKGHEEPKFY CNECHSFDIK PMPFSDAKKK 

       130        140        150        160        170        180 
KSWDDGWDQD KIQKAIAAGP SETTQVLVVG AGSAGFNASL AAKKAGANVI LVDKAPFSGG 

       190        200        210        220        230        240 
NSMISAGGMN AVGTKQQTAH GVEDKVEWFI EDAMKGGRQQ NDIKLVTILA EQSADGVQWL 

       250        260        270        280        290        300 
ESLGANLDDL KRSGGARVDR THRPHGGKSS GPEIIDTLRK AAKEQGIDTR LNSRVVKLVV 

       310        320        330        340        350        360 
NDDHSVVGAV VHGKHTGYYM IGAKSVVLAT GGYGMNKEMI AYYRPTMKDM TSSNNITATG 

       370        380        390        400        410        420 
DGVLMAKEIG ASMTDIDWVQ AHPTVGKDSR ILISETVRGV GAVMVNKDGN RFISELTTRD 

       430        440        450        460        470        480 
KASDAILKQP GQFAWIIFDN QLYKKAKMVR GYDHLEMLYK GDTVEQLAKS TGMKVADLAK 

       490        500        510        520        530        540 
TVSDYNGYVA SGKDTAFGRA DMPLNMTQSP YYAVKVAPGI HHTMGGVAIN TTASVLDLQS 

       550        560        570        580 
KPIDGLFAAG EVTGGVHGYN RLGGNAIADT VVFGRIAGDN AAKHALDK

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a flavocytochrome that is induced during the anaerobic respiration of Fe3+ by Shewanella frigidimarina NCIMB400."
Dobbin P.S., Butt J.N., Powell A.K., Reid G.A., Richardson D.J.
Biochem. J. 342:439-448(1999) [PubMed: 10455032] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-32; 190-199 AND 215-229, CHARACTERIZATION, MASS SPECTROMETRY.
[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].
Strain: NCIMB 400.
[3]"Open conformation of a flavocytochrome c3 fumarate reductase."
Bamford V., Dobbin P.S., Richardson D.J., Hemmings A.M.
Nat. Struct. Biol. 6:1104-1107(1999) [PubMed: 10581549] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ236923 Genomic DNA. Translation: CAB37062.1.
CP000447 Genomic DNA. Translation: ABI72427.1.
RefSeqYP_751265.1. NC_008345.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QO8X-ray2.15A/D23-588[»]
ProteinModelPortalQ9Z4P0.
SMRQ9Z4P0. Positions 24-587.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9Z4P0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4279493.
GenomeReviewsGene locus Sfri_2586 in contig CP000447_GR.
KEGGsfr:Sfri_2586.
NMPDRfig|318167.10.peg.2480.
PATRIC23499229. VBISheFri14343_2684.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1053.
HOGENOMHBG678063.
OMACADCHGK.
PhylomeDBQ9Z4P0.
ProtClustDBCLSK906032.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR010960. Flavocytochrome_c.
IPR011031. Multihaem_cyt.
[Graphical view]
KOK00244.
PfamPF00890. FAD_binding_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
TIGRFAMsTIGR01813. Flavo_cyto_c. 1 hit.
PROSITEPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRD2_SHEFN
AccessionPrimary (citable) accession number: Q9Z4P0
Secondary accession number(s): Q07ZY8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1999
Last modified: January 25, 2012
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents