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P0AC47 (FRDB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fumarate reductase iron-sulfur subunit

EC=1.3.5.1
Gene names
Name:frdB
Ordered Locus Names:b4153, JW4114
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.

Catalytic activity

Succinate + a quinone = fumarate + a quinol.

Cofactor

Binds 1 2Fe-2S cluster.

Binds 1 3Fe-4S cluster.

Binds 1 4Fe-4S cluster.

Subunit structure

Fumarate dehydrogenase forms part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, and two hydrophobic anchor proteins.

Sequence similarities

Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 4Fe-4S ferredoxin-type domain.

Ontologies

Keywords
   Biological processElectron transport
Transport
Tricarboxylic acid cycle
   Ligand2Fe-2S
3Fe-4S
4Fe-4S
Iron
Iron-sulfur
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanaerobic respiration

Inferred from mutant phenotype PubMed 14109218. Source: EcoCyc

bacterial-type flagellum assembly

Inferred from mutant phenotype PubMed 18337747. Source: EcoCyc

bacterial-type flagellum-dependent cell motility

Inferred from mutant phenotype PubMed 18337747. Source: EcoCyc

fermentation

Inferred from mutant phenotype PubMed 14109218. Source: EcoCyc

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.8. Source: EcoCyc

membrane

Inferred from direct assay PubMed 16858726. Source: UniProtKB

   Molecular_function2 iron, 2 sulfur cluster binding

Inferred from direct assay Ref.8. Source: EcoCyc

3 iron, 4 sulfur cluster binding

Inferred from direct assay Ref.8. Source: EcoCyc

4 iron, 4 sulfur cluster binding

Inferred from direct assay Ref.8. Source: EcoCyc

electron carrier activity

Inferred from direct assay PubMed 8499449. Source: EcoCyc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.9PubMed 16858726PubMed 17137328PubMed 24561554. Source: IntAct

succinate dehydrogenase (ubiquinone) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 244243Fumarate reductase iron-sulfur subunit
PRO_0000158698

Regions

Domain16 – 97822Fe-2S ferredoxin-type
Domain140 – 169304Fe-4S ferredoxin-type

Sites

Metal binding581Iron-sulfur 1 (2Fe-2S)
Metal binding631Iron-sulfur 1 (2Fe-2S)
Metal binding661Iron-sulfur 1 (2Fe-2S)
Metal binding781Iron-sulfur 1 (2Fe-2S)
Metal binding1491Iron-sulfur 2 (4Fe-4S)
Metal binding1521Iron-sulfur 2 (4Fe-4S)
Metal binding1551Iron-sulfur 2 (4Fe-4S)
Metal binding1591Iron-sulfur 3 (3Fe-4S)
Metal binding2051Iron-sulfur 3 (3Fe-4S)
Metal binding2111Iron-sulfur 3 (3Fe-4S)
Metal binding2151Iron-sulfur 2 (4Fe-4S)

Experimental info

Mutagenesis581C → S: Affects center 1 (2Fe-2S).
Mutagenesis631C → S: Affects center 1 (2Fe-2S).
Mutagenesis661C → S: Affects center 1 (2Fe-2S).
Mutagenesis781C → S: Affects center 1 (2Fe-2S).

Secondary structure

............................................... 244
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AC47 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AC1D7A73244D7AC0

FASTA24427,123
        10         20         30         40         50         60 
MAEMKNLKIE VVRYNPEVDT APHSAFYEVP YDATTSLLDA LGYIKDNLAP DLSYRWSCRM 

        70         80         90        100        110        120 
AICGSCGMMV NNVPKLACKT FLRDYTDGMK VEALANFPIE RDLVVDMTHF IESLEAIKPY 

       130        140        150        160        170        180 
IIGNSRTADQ GTNIQTPAQM AKYHQFSGCI NCGLCYAACP QFGLNPEFIG PAAITLAHRY 

       190        200        210        220        230        240 
NEDSRDHGKK ERMAQLNSQN GVWSCTFVGY CSEVCPKHVD PAAAIQQGKV ESSKDFLIAT 


LKPR 

« Hide

References

« Hide 'large scale' references
[1]"Location and nucleotide sequence of frdB, the gene coding for the iron-sulphur protein subunit of the fumarate reductase of Escherichia coli."
Cole S.T., Grundstroem T., Jaurin B., Robinson J.J., Weiner J.H.
Eur. J. Biochem. 126:211-216(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Overlap between ampC and frd operons on the Escherichia coli chromosome."
Grundstroem T., Jaurin B.
Proc. Natl. Acad. Sci. U.S.A. 79:1111-1115(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-244.
[6]"Site-directed mutagenesis of conserved cysteine residues in Escherichia coli fumarate reductase: modification of the spectroscopic and electrochemical properties of the [2Fe-2S] cluster."
Werth M.T., Cecchini G., Manodori A., Ackrell B.A.C., Schroeder I., Gunsalus R.P., Johnson M.K.
Proc. Natl. Acad. Sci. U.S.A. 87:8965-8969(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[7]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[8]"Structure of the Escherichia coli fumarate reductase respiratory complex."
Iverson T.M., Luna-Chavez C., Cecchini G., Rees D.C.
Science 284:1961-1966(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
[9]"Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site."
Iverson T.M., Luna-Chavez C., Croal L.R., Cecchini G., Rees D.C.
J. Biol. Chem. 277:16124-16130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01611 Genomic DNA. Translation: AAA23438.1.
U14003 Genomic DNA. Translation: AAA97052.1.
U00096 Genomic DNA. Translation: AAC77113.1.
AP009048 Genomic DNA. Translation: BAE78157.1.
V00277 Genomic DNA. Translation: CAA23534.1.
PIRRDECFS. A00377.
RefSeqNP_418577.1. NC_000913.3.
YP_492298.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KF6X-ray2.70B/N2-244[»]
1KFYX-ray3.60B/N2-244[»]
1L0VX-ray3.30B/N2-244[»]
2B76X-ray3.30B/N2-244[»]
3CIRX-ray3.65B/N2-244[»]
3P4PX-ray2.80B/N2-244[»]
3P4QX-ray3.35B/N2-244[»]
3P4RX-ray3.05B/N2-244[»]
3P4SX-ray3.10B/N2-244[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9682N.
IntActP0AC47. 7 interactions.
STRING511145.b4153.

Proteomic databases

PaxDbP0AC47.
PRIDEP0AC47.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77113; AAC77113; b4153.
BAE78157; BAE78157; BAE78157.
GeneID12933707.
948666.
KEGGecj:Y75_p4042.
eco:b4153.
PATRIC32123879. VBIEscCol129921_4287.

Organism-specific databases

EchoBASEEB0327.
EcoGeneEG10331. frdB.

Phylogenomic databases

eggNOGCOG0479.
HOGENOMHOG000160590.
KOK00245.
OMACHFAASC.
OrthoDBEOG6CK7MG.
PhylomeDBP0AC47.

Enzyme and pathway databases

BioCycEcoCyc:FUM-FE-S.
ECOL316407:JW4114-MONOMER.
MetaCyc:FUM-FE-S.

Gene expression databases

GenevestigatorP0AC47.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamPF13085. Fer2_3. 1 hit.
PF13183. Fer4_8. 1 hit.
[Graphical view]
SUPFAMSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsTIGR00384. dhsB. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AC47.
PROP0AC47.

Entry information

Entry nameFRDB_ECOLI
AccessionPrimary (citable) accession number: P0AC47
Secondary accession number(s): P00364, Q2M6E9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 82 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene