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P20921

- FRDB_PROVU

UniProt

P20921 - FRDB_PROVU

Protein

Fumarate reductase iron-sulfur subunit

Gene

frdB

Organism
Proteus vulgaris
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 86 (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 bindingi59 – 591Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi64 – 641Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi67 – 671Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi79 – 791Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi150 – 1501Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi153 – 1531Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi156 – 1561Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi160 – 1601Iron-sulfur 3 (3Fe-4S)By similarity
    Metal bindingi206 – 2061Iron-sulfur 3 (3Fe-4S)By similarity
    Metal bindingi212 – 2121Iron-sulfur 3 (3Fe-4S)By similarity
    Metal bindingi216 – 2161Iron-sulfur 2 (4Fe-4S)By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. 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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate reductase iron-sulfur subunit (EC:1.3.5.1)
    Gene namesi
    Name:frdB
    OrganismiProteus vulgaris
    Taxonomic identifieri585 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 245244Fumarate reductase iron-sulfur subunitPRO_0000158706Add
    BLAST

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP20921.
    SMRiP20921. Positions 4-245.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 98862Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini141 – 170304Fe-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

    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.

    P20921-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADDMKHVKM EVMRYNPETD DAPHFVTYDV PYDEQTSLLD ALGYIKDNLA    50
    PDLSYRWSCR MAICGSCGMM VNRVPKLACK TFMRDYPNGV RIEALGNFPV 100
    ERDLVVDMTH FIESLEAIKP YILGNDRKPS EGPNKQTPAQ MAKYHQFSGC 150
    INCGLCYAAC PQFGLNPEFI GPAAITLAQR YNTDSRDHGA KERMPQLNGE 200
    NGVWSCTFVG YCSEVCPKHV DPAAAIQQGK AASAQDFVIA MLKPR 245
    Length:245
    Mass (Da):27,331
    Last modified:January 23, 2007 - v2
    Checksum:iCEA17E28C8A390C2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06144 Genomic DNA. Translation: CAA29502.1.
    PIRiS00108. RDEBIV.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06144 Genomic DNA. Translation: CAA29502.1 .
    PIRi S00108. RDEBIV.

    3D structure databases

    ProteinModelPortali P20921.
    SMRi P20921. Positions 4-245.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Nucleotide sequence and comparative analysis of the frd operon encoding the fumarate reductase of Proteus vulgaris. Extensive sequence divergence of the membrane anchors and absence of an frd-linked ampC cephalosporinase gene."
      Cole S.T.
      Eur. J. Biochem. 167:481-488(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiFRDB_PROVU
    AccessioniPrimary (citable) accession number: P20921
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3