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P0AC47

- FRDB_ECOLI

UniProt

P0AC47 - FRDB_ECOLI

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
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    Binds 1 2Fe-2S cluster.
    Binds 1 3Fe-4S cluster.
    Binds 1 4Fe-4S cluster.

    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. protein binding Source: IntAct
    7. 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

    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

    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 – 139
    Turni16 – 183
    Beta strandi23 – 319
    Helixi37 – 4711
    Beta strandi59 – 635
    Beta strandi67 – 704
    Beta strandi73 – 764
    Helixi77 – 793
    Helixi82 – 843
    Beta strandi89 – 935
    Beta strandi99 – 1013
    Helixi108 – 1169
    Helixi128 – 1303
    Helixi137 – 1415
    Helixi144 – 1474
    Helixi154 – 1585
    Helixi160 – 1645
    Beta strandi166 – 1683
    Helixi171 – 18111
    Helixi190 – 1978
    Turni199 – 2013
    Helixi202 – 2043
    Helixi210 – 2145
    Helixi221 – 24020

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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.
    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

    MAEMKNLKIE VVRYNPEVDT APHSAFYEVP YDATTSLLDA LGYIKDNLAP    50
    DLSYRWSCRM AICGSCGMMV NNVPKLACKT FLRDYTDGMK VEALANFPIE 100
    RDLVVDMTHF IESLEAIKPY IIGNSRTADQ GTNIQTPAQM AKYHQFSGCI 150
    NCGLCYAACP QFGLNPEFIG PAAITLAHRY NEDSRDHGKK ERMAQLNSQN 200
    GVWSCTFVGY CSEVCPKHVD PAAAIQQGKV ESSKDFLIAT LKPR 244
    Length:244
    Mass (Da):27,123
    Last modified:January 23, 2007 - v2
    Checksum:iAC1D7A73244D7AC0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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.
    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

    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: October 1, 2014
    This is version 84 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