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P0AC47

- FRDB_ECOLI

UniProt

P0AC47 - FRDB_ECOLI

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Protein

Fumarate reductase iron-sulfur subunit

Gene

frdB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi58 – 581Iron-sulfur 1 (2Fe-2S)
Metal bindingi63 – 631Iron-sulfur 1 (2Fe-2S)
Metal bindingi66 – 661Iron-sulfur 1 (2Fe-2S)
Metal bindingi78 – 781Iron-sulfur 1 (2Fe-2S)
Metal bindingi149 – 1491Iron-sulfur 2 (4Fe-4S)
Metal bindingi152 – 1521Iron-sulfur 2 (4Fe-4S)
Metal bindingi155 – 1551Iron-sulfur 2 (4Fe-4S)
Metal bindingi159 – 1591Iron-sulfur 3 (3Fe-4S)
Metal bindingi205 – 2051Iron-sulfur 3 (3Fe-4S)
Metal bindingi211 – 2111Iron-sulfur 3 (3Fe-4S)
Metal bindingi215 – 2151Iron-sulfur 2 (4Fe-4S)

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: EcoCyc
  2. 3 iron, 4 sulfur cluster binding Source: EcoCyc
  3. 4 iron, 4 sulfur cluster binding Source: EcoCyc
  4. electron carrier activity Source: EcoCyc
  5. metal ion binding Source: UniProtKB-KW
  6. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC

GO - Biological processi

  1. anaerobic respiration Source: EcoCyc
  2. bacterial-type flagellum assembly Source: EcoCyc
  3. bacterial-type flagellum-dependent cell motility Source: EcoCyc
  4. fermentation Source: EcoCyc
  5. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

2Fe-2S, 3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate reductase iron-sulfur subunit (EC:1.3.5.1)
Gene namesi
Name:frdB
Ordered Locus Names:b4153, JW4114
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10331. frdB.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoCyc
  2. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581C → S: Affects center 1 (2Fe-2S). 1 Publication
Mutagenesisi63 – 631C → S: Affects center 1 (2Fe-2S). 1 Publication
Mutagenesisi66 – 661C → S: Affects center 1 (2Fe-2S). 1 Publication
Mutagenesisi78 – 781C → S: Affects center 1 (2Fe-2S). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 244243Fumarate reductase iron-sulfur subunitPRO_0000158698Add
BLAST

Proteomic databases

PaxDbiP0AC47.
PRIDEiP0AC47.

Expressioni

Gene expression databases

GenevestigatoriP0AC47.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
frdAP003634EBI-906724,EBI-550480
mutTP083374EBI-906724,EBI-1121389
ompWP0A9152EBI-906724,EBI-1132929

Protein-protein interaction databases

DIPiDIP-9682N.
IntActiP0AC47. 7 interactions.
STRINGi511145.b4153.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Turni16 – 183Combined sources
Beta strandi23 – 319Combined sources
Helixi37 – 4711Combined sources
Beta strandi59 – 635Combined sources
Beta strandi67 – 704Combined sources
Beta strandi73 – 764Combined sources
Helixi77 – 793Combined sources
Helixi82 – 843Combined sources
Beta strandi89 – 935Combined sources
Beta strandi99 – 1013Combined sources
Helixi108 – 1169Combined sources
Helixi128 – 1303Combined sources
Helixi137 – 1415Combined sources
Helixi144 – 1474Combined sources
Helixi154 – 1585Combined sources
Helixi160 – 1645Combined sources
Beta strandi166 – 1683Combined sources
Helixi171 – 18111Combined sources
Helixi190 – 1978Combined sources
Turni199 – 2013Combined sources
Helixi202 – 2043Combined sources
Helixi210 – 2145Combined sources
Helixi221 – 24020Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0AC47.
SMRiP0AC47. Positions 2-244.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AC47.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 97822Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini140 – 169304Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0479.
HOGENOMiHOG000160590.
InParanoidiP0AC47.
KOiK00245.
OMAiCHFAASC.
OrthoDBiEOG6CK7MG.
PhylomeDBiP0AC47.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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]
PfamiPF13085. Fer2_3. 1 hit.
PF13183. Fer4_8. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AC47-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEMKNLKIE VVRYNPEVDT APHSAFYEVP YDATTSLLDA LGYIKDNLAP
60 70 80 90 100
DLSYRWSCRM AICGSCGMMV NNVPKLACKT FLRDYTDGMK VEALANFPIE
110 120 130 140 150
RDLVVDMTHF IESLEAIKPY IIGNSRTADQ GTNIQTPAQM AKYHQFSGCI
160 170 180 190 200
NCGLCYAACP QFGLNPEFIG PAAITLAHRY NEDSRDHGKK ERMAQLNSQN
210 220 230 240
GVWSCTFVGY CSEVCPKHVD PAAAIQQGKV ESSKDFLIAT LKPR
Length:244
Mass (Da):27,123
Last modified:January 23, 2007 - v2
Checksum:iAC1D7A73244D7AC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA00377. RDECFS.
RefSeqiNP_418577.1. NC_000913.3.
YP_492298.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77113; AAC77113; b4153.
BAE78157; BAE78157; BAE78157.
GeneIDi12933707.
948666.
KEGGiecj:Y75_p4042.
eco:b4153.
PATRICi32123879. VBIEscCol129921_4287.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi A00377. RDECFS.
RefSeqi NP_418577.1. NC_000913.3.
YP_492298.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KF6 X-ray 2.70 B/N 2-244 [» ]
1KFY X-ray 3.60 B/N 2-244 [» ]
1L0V X-ray 3.30 B/N 2-244 [» ]
2B76 X-ray 3.30 B/N 2-244 [» ]
3CIR X-ray 3.65 B/N 2-244 [» ]
3P4P X-ray 2.80 B/N 2-244 [» ]
3P4Q X-ray 3.35 B/N 2-244 [» ]
3P4R X-ray 3.05 B/N 2-244 [» ]
3P4S X-ray 3.10 B/N 2-244 [» ]
ProteinModelPortali P0AC47.
SMRi P0AC47. Positions 2-244.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9682N.
IntActi P0AC47. 7 interactions.
STRINGi 511145.b4153.

Proteomic databases

PaxDbi P0AC47.
PRIDEi P0AC47.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77113 ; AAC77113 ; b4153 .
BAE78157 ; BAE78157 ; BAE78157 .
GeneIDi 12933707.
948666.
KEGGi ecj:Y75_p4042.
eco:b4153.
PATRICi 32123879. VBIEscCol129921_4287.

Organism-specific databases

EchoBASEi EB0327.
EcoGenei EG10331. frdB.

Phylogenomic databases

eggNOGi COG0479.
HOGENOMi HOG000160590.
InParanoidi P0AC47.
KOi K00245.
OMAi CHFAASC.
OrthoDBi EOG6CK7MG.
PhylomeDBi P0AC47.

Enzyme and pathway databases

BioCyci EcoCyc:FUM-FE-S.
ECOL316407:JW4114-MONOMER.
MetaCyc:FUM-FE-S.

Miscellaneous databases

EvolutionaryTracei P0AC47.
PROi P0AC47.

Gene expression databases

Genevestigatori P0AC47.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR001041. 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 ]
Pfami PF13085. Fer2_3. 1 hit.
PF13183. Fer4_8. 1 hit.
[Graphical view ]
SUPFAMi SSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsi TIGR00384. dhsB. 1 hit.
PROSITEi PS00197. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiFRDB_ECOLI
AccessioniPrimary (citable) accession number: P0AC47
Secondary accession number(s): P00364, Q2M6E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3