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P0C278 (FRDA_SHEFR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 38. 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
Flavocytochrome c3
Short name=Fcc3
Gene names
Name:fccA
Synonyms:fcc3
OrganismShewanella frigidimarina
Taxonomic identifier56812 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length571 AA.
Sequence statusComplete.
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.

Catalytic activity

Succinate + a quinone = fumarate + a quinol.

Cofactor

Binds 1 FAD per subunit.

Subunit structure

Monomer.

Subcellular location

Periplasm.

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.

Caution

The N-terminal sequence has been extracted from PDB entry 1LJ1.

Mass spectrometry

Molecular mass is 63033±10 Da from positions 1 - 571. Determined by ESI. Ref.7

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 571571Fumarate reductase flavoprotein subunit
PRO_0000010344

Regions

Domain1 – 117117Cytochrome c
Nucleotide binding132 – 14312FAD
Nucleotide binding156 – 1572FAD
Nucleotide binding164 – 1652FAD
Nucleotide binding169 – 1713FAD
Nucleotide binding549 – 5502FAD
Region118 – 571454Flavoprotein-like

Sites

Active site4021Proton donor
Metal binding81Iron (heme 2 axial ligand)
Metal binding181Iron (heme 1 axial ligand)
Metal binding401Iron (heme 2 axial ligand)
Metal binding581Iron (heme 3 axial ligand)
Metal binding611Iron (heme 4 axial ligand)
Metal binding721Iron (heme 3 axial ligand)
Metal binding751Iron (heme 1 axial ligand)
Metal binding861Iron (heme 4 axial ligand)
Binding site141Heme 1 (covalent)
Binding site171Heme 1 (covalent)
Binding site361Heme 2 (covalent)
Binding site391Heme 2 (covalent)
Binding site681Heme 3 (covalent)
Binding site711Heme 3 (covalent)
Binding site821Heme 4 (covalent)
Binding site851Heme 4 (covalent)
Binding site3651Substrate
Binding site3771Substrate
Binding site5041Substrate
Binding site5441Substrate

Experimental info

Mutagenesis611H → A: Reduces catalytic activity 10-fold. Reduces affinity for fumarate. Ref.7
Mutagenesis611H → M: Reduces catalytic activity 5-fold. Reduces affinity for fumarate. Ref.7
Mutagenesis3651H → A: Reduces catalytic activity by over 75%. Ref.3
Mutagenesis3781E → D: Strongly reduced affinity for substrate. Reduces activity 10000-fold. Ref.9
Mutagenesis3811R → M: Strongly reduced catalytic activity. No effect on substrate affinity. Ref.9
Mutagenesis4021R → A: Loss of activity. Ref.3 Ref.4
Mutagenesis4021R → K or Y: Reduces activity 10000-fold. Ref.3 Ref.4
Mutagenesis5041H → A: Reduces catalytic activity by over 64%. Ref.3

Secondary structure

.................................................................................................... 571
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C278 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: D2E4FC43C9A6484C

FASTA57160,621
        10         20         30         40         50         60 
ADNLAEFHVQ NQECDSCHTP DGELSNDSLT YENTQCVSCH GTLEEVAETT KHEHYNAHAS 

        70         80         90        100        110        120 
HFPGEVACTS CHSAHEKSMV YCDSCHSFDF NMPYAKKWQR DEPTIAELAK DKSERQAALA 

       130        140        150        160        170        180 
SAPHDTVDVV VVGSGGAGFS AAISATDSGA KVILIEKEPV IGGNAKLAAG GMNAAWTDQQ 

       190        200        210        220        230        240 
KAKKITDSPE LMFEDTMKGG QNINDPALVK VLSSHSKDSV DWMTAMGADL TDVGMMGGAS 

       250        260        270        280        290        300 
VNRAHRPTGG AGVGAHVVQV LYDNAVKRNI DLRMNTRGIE VLKDDKGTVK GILVKGMYKG 

       310        320        330        340        350        360 
YYWVKADAVI LATGGFAKNN ERVAKLDPSL KGFISTNQPG AVGDGLDVAE NAGGALKDMQ 

       370        380        390        400        410        420 
YIQAHPTLSV KGGVMVTEAV RGNGAILVNR EGKRFVNEIT TRDKASAAIL AQTGKSAYLI 

       430        440        450        460        470        480 
FDDSVRKSLS KIDKYIGLGV APTADSLVKL GKMEGIDGKA LTETVARYNS LVSSGKDTDF 

       490        500        510        520        530        540 
ERPNLPRALN EGNYYAIEVT PGVHHTMGGV MIDTKAEVMN AKKQVIPGLY GAGEVTGGVH 

       550        560        570 
GANRLGGNAI SDIITFGRLA GEEAAKYSKK N 

« Hide

References

[1]"Crystallization and preliminary X-ray analysis of flavocytochrome c(3), the fumarate reductase from Shewanella frigidimarina."
Pealing S.L., Lysek D.A., Taylor P., Alexeev D., Reid G.A., Chapman S.K., Walkinshaw M.D.
J. Struct. Biol. 127:76-78(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-571, CRYSTALLIZATION.
Strain: ACAM591.
[2]"Structural and mechanistic mapping of a unique fumarate reductase."
Taylor P., Pealing S.L., Reid G.A., Chapman S.K., Walkinshaw M.D.
Nat. Struct. Biol. 6:1108-1112(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[3]"Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and crystallographic study."
Doherty M.K., Pealing S.L., Miles C.S., Moysey R., Taylor P., Walkinshaw M.D., Reid G.A., Chapman S.K.
Biochemistry 39:10695-10701(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-365 AND ALA-504 IN COMPLEX WITH FAD; FUMARATE AND HEMES, MUTAGENESIS OF HIS-365; ARG-402 AND HIS-504.
[4]"Kinetic and crystallographic analysis of the key active site acid/base arginine in a soluble fumarate reductase."
Mowat C.G., Moysey R., Miles C.S., Leys D., Doherty M.K., Taylor P., Walkinshaw M.D., Reid G.A., Chapman S.K.
Biochemistry 40:12292-12298(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS ALA-402; LYS-402 AND TYR-402, MUTAGENESIS OF ARG-402, ENZYME KINETICS.
[5]"Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina."
Pankhurst K.L., Mowat C.G., Miles C.S., Leys D., Walkinshaw M.D., Reid G.A., Chapman S.K.
Biochemistry 41:8551-8556(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-505 AND TYR-505, CHARACTERIZATION.
[6]"Engineering water to act as an active site acid catalyst in a soluble fumarate reductase."
Mowat C.G., Pankhurst K.L., Miles C.S., Leys D., Walkinshaw M.D., Reid G.A., Chapman S.K.
Biochemistry 41:11990-11996(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS PHE-363 AND PHE-363/ALA-402, CHARACTERIZATION, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"Histidine 61: an important heme ligand in the soluble fumarate reductase from Shewanella frigidimarina."
Rothery E.L., Mowat C.G., Miles C.S., Walkinshaw M.D., Reid G.A., Chapman S.K.
Biochemistry 42:13160-13169(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANTS ALA-61 AND MET-61 IN COMPLEXES WITH HEME; SUBSTRATE AND FAD, MASS SPECTROMETRY, MUTAGENESIS OF HIS-61.
[8]"Probing domain mobility in a flavocytochrome."
Rothery E.L., Mowat C.G., Miles C.S., Mott S., Walkinshaw M.D., Reid G.A., Chapman S.K.
Biochemistry 43:4983-4989(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MUTANT CYS-251/CYS430.
[9]"A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina."
Pankhurst K.L., Mowat C.G., Rothery E.L., Hudson J.M., Jones A.K., Miles C.S., Walkinshaw M.D., Armstrong F.A., Reid G.A., Chapman S.K.
J. Biol. Chem. 281:20589-20597(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANTS ASP-378 AND MET-381, MUTAGENESIS OF GLU-378 AND ARG-381, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ132010 Genomic DNA. Translation: CAB38558.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E39X-ray1.80A1-571[»]
1JRXX-ray2.00A/B1-571[»]
1JRYX-ray2.00A/B1-571[»]
1JRZX-ray2.00A/B1-571[»]
1KSSX-ray1.80A1-571[»]
1KSUX-ray2.00A/B1-571[»]
1LJ1X-ray2.00A/B1-571[»]
1M64X-ray1.80A/B1-571[»]
1P2EX-ray2.20A1-571[»]
1P2HX-ray2.10A1-571[»]
1Q9IX-ray1.60A1-571[»]
1QJDX-ray1.80A1-571[»]
1Y0PX-ray1.50A1-571[»]
2B7RX-ray1.70A1-571[»]
2B7SX-ray2.12A1-571[»]
ProteinModelPortalP0C278.
SMRP0C278. Positions 1-568.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP0C278.

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.
IPR007087. Znf_C2H2.
[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

EvolutionaryTraceP0C278.

Entry information

Entry nameFRDA_SHEFR
AccessionPrimary (citable) accession number: P0C278
Secondary accession number(s): Q02469, Q9X969
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 38 of the entry and version 1 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