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P83223

- FRDA_SHEON

UniProt

P83223 - FRDA_SHEON

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Protein
Fumarate reductase flavoprotein subunit
Gene
SO_0970
Organism
Shewanella oneidensis (strain MR-1)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 By similarity.

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Iron (heme 2 axial ligand)
Binding sitei40 – 401Heme 1 (covalent)
Binding sitei43 – 431Heme 1 (covalent)
Metal bindingi44 – 441Iron (heme 1 axial ligand)
Binding sitei63 – 631Heme 2 (covalent)
Binding sitei66 – 661Heme 2 (covalent)
Metal bindingi67 – 671Iron (heme 2 axial ligand)
Metal bindingi85 – 851Iron (heme 3 axial ligand)
Metal bindingi88 – 881Iron (heme 4 axial ligand)
Binding sitei95 – 951Heme 3 (covalent)
Binding sitei98 – 981Heme 3 (covalent)
Metal bindingi99 – 991Iron (heme 3 axial ligand)
Metal bindingi102 – 1021Iron (heme 1 axial ligand)
Binding sitei109 – 1091Heme 4 (covalent)
Binding sitei112 – 1121Heme 4 (covalent)
Metal bindingi113 – 1131Iron (heme 4 axial ligand)
Binding sitei389 – 3891Substrate
Binding sitei401 – 4011Substrate
Active sitei426 – 4261Proton donor By similarity
Binding sitei528 – 5281Substrate
Binding sitei569 – 5691Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi156 – 16712FAD
Add
BLAST
Nucleotide bindingi180 – 1812FAD
Nucleotide bindingi187 – 1893FAD
Nucleotide bindingi193 – 1953FAD
Nucleotide bindingi572 – 5754FAD

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. succinate dehydrogenase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Transport

    Keywords - Ligandi

    FAD, Flavoprotein, Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate reductase flavoprotein subunit (EC:1.3.5.4)
    Alternative name(s):
    Flavocytochrome c
    Short name:
    FL cyt
    Gene namesi
    Ordered Locus Names:SO_0970
    OrganismiShewanella oneidensis (strain MR-1)
    Taxonomic identifieri211586 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
    ProteomesiUP000008186: Chromosome

    Subcellular locationi

    Periplasm By similarity

    GO - Cellular componenti

    1. periplasmic space Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525 Inferred
    Add
    BLAST
    Chaini26 – 596571Fumarate reductase flavoprotein subunit
    PRO_0000010345Add
    BLAST

    Expressioni

    Inductioni

    By anaerobiosis and fumarate.1 Publication

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi211586.SO_0970.

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 334
    Turni34 – 385
    Turni41 – 433
    Beta strandi44 – 485
    Helixi57 – 6711
    Helixi70 – 767
    Beta strandi79 – 813
    Beta strandi86 – 883
    Helixi95 – 973
    Beta strandi101 – 1033
    Helixi108 – 1114
    Turni132 – 1354
    Helixi136 – 1449
    Beta strandi152 – 1565
    Helixi160 – 17011
    Beta strandi171 – 1733
    Beta strandi176 – 1794
    Beta strandi181 – 1855
    Helixi189 – 1913
    Beta strandi200 – 2023
    Helixi205 – 2073
    Helixi214 – 22310
    Turni224 – 2263
    Helixi230 – 2389
    Helixi240 – 24910
    Beta strandi256 – 2583
    Beta strandi268 – 2714
    Turni272 – 2743
    Helixi277 – 29115
    Beta strandi295 – 30713
    Beta strandi309 – 3113
    Beta strandi313 – 3208
    Turni321 – 3233
    Beta strandi324 – 3296
    Beta strandi331 – 3355
    Helixi344 – 3507
    Helixi352 – 3543
    Beta strandi359 – 3613
    Helixi368 – 3758
    Beta strandi386 – 3938
    Turni394 – 3974
    Helixi403 – 4064
    Beta strandi410 – 4123
    Helixi426 – 4349
    Helixi437 – 4393
    Beta strandi441 – 4455
    Helixi447 – 4504
    Helixi455 – 4617
    Beta strandi466 – 4705
    Helixi471 – 4788
    Helixi482 – 49514
    Turni502 – 5043
    Beta strandi515 – 53016
    Beta strandi533 – 5364
    Beta strandi541 – 55616
    Helixi558 – 5603
    Beta strandi561 – 5633
    Turni564 – 5674
    Helixi573 – 59119

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D4CX-ray2.90A/B/C/D25-596[»]
    1D4DX-ray2.50A25-596[»]
    1D4EX-ray2.80A25-596[»]
    ProteinModelPortaliP83223.
    SMRiP83223. Positions 26-595.

    Miscellaneous databases

    EvolutionaryTraceiP83223.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 141116Cytochrome c
    Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni142 – 596455Flavoprotein-like
    Add
    BLAST

    Sequence similaritiesi

    In the C-terminal section; belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1053.
    HOGENOMiHOG000227327.
    KOiK00244.
    OMAiCDSCHSF.
    OrthoDBiEOG6XHC2W.
    PhylomeDBiP83223.

    Family and domain databases

    Gene3Di1.10.1130.10. 1 hit.
    3.90.700.10. 1 hit.
    InterProiIPR003953. FAD_bind_dom.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR010960. Flavocytochrome_c.
    IPR011031. Multihaem_cyt.
    IPR027477. Succ_DH/fumarate_Rdtase_cat.
    IPR012286. Tetrahaem_cytochrome.
    [Graphical view]
    PfamiPF00890. FAD_binding_2. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.
    SUPFAMiSSF56425. SSF56425. 1 hit.
    TIGRFAMsiTIGR01813. flavo_cyto_c. 1 hit.
    PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P83223-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFTRKIQKTA LAMLISGAMA GTAYAAPEVL ADFHGEMGGC DSCHVSDKGG    50
    VTNDNLTHEN GQCVSCHGDL KELAAAAPKD KVSPHKSHLI GEIACTSCHK 100
    GHEKSVAYCD ACHSFGFDMP FGGKWERKFV PVDADKAAQD KAIAAGVKET 150
    TDVVIIGSGG AGLAAAVSAR DAGAKVILLE KEPIPGGNTK LAAGGMNAAE 200
    TKPQAKLGIE DKKQIMIDDT MKGGRNINDP ELVKVLANNS SDSIDWLTSM 250
    GADMTDVGRM GGASVNRSHR PTGGAGVGAH VAQVLWDNAV KRGTDIRLNS 300
    RVVRILEDAS GKVTGVLVKG EYTGYYVIKA DAVVIAAGGF AKNNERVSKY 350
    DPKLKGFKAT NHPGATGDGL DVALQAGAAT RDLEYIQAHP TYSPAGGVMI 400
    TEAVRGNGAI VVNREGNRFM NEITTRDKAS AAILQQKGES AYLVFDDSIR 450
    KSLKAIEGYV HLNIVKEGKT IEELAKQIDV PAAELAKTVT AYNGFVKSGK 500
    DAQFERPDLP RELVVAPFYA LEIAPAVHHT MGGLVIDTKA EVKSEKTGKP 550
    ITGLYAAGEV TGGVHGANRL GGNAISDIVT YGRIAGASAA KFAKDN 596
    Length:596
    Mass (Da):62,448
    Last modified:November 25, 2002 - v2
    Checksum:i74CB81FE89790463
    GO

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711K → E1 Publication
    Sequence conflicti282 – 2821A → S1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014299 Genomic DNA. Translation: AAN54044.1.
    RefSeqiNP_716599.1. NC_004347.2.
    WP_011071245.1. NC_004347.2.

    Genome annotation databases

    EnsemblBacteriaiAAN54044; AAN54044; SO_0970.
    GeneIDi1168814.
    KEGGison:SO_0970.
    PATRICi23521593. VBISheOne101494_0930.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014299 Genomic DNA. Translation: AAN54044.1 .
    RefSeqi NP_716599.1. NC_004347.2.
    WP_011071245.1. NC_004347.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D4C X-ray 2.90 A/B/C/D 25-596 [» ]
    1D4D X-ray 2.50 A 25-596 [» ]
    1D4E X-ray 2.80 A 25-596 [» ]
    ProteinModelPortali P83223.
    SMRi P83223. Positions 26-595.
    ModBasei Search...

    Protein-protein interaction databases

    STRINGi 211586.SO_0970.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN54044 ; AAN54044 ; SO_0970 .
    GeneIDi 1168814.
    KEGGi son:SO_0970.
    PATRICi 23521593. VBISheOne101494_0930.

    Phylogenomic databases

    eggNOGi COG1053.
    HOGENOMi HOG000227327.
    KOi K00244.
    OMAi CDSCHSF.
    OrthoDBi EOG6XHC2W.
    PhylomeDBi P83223.

    Miscellaneous databases

    EvolutionaryTracei P83223.

    Family and domain databases

    Gene3Di 1.10.1130.10. 1 hit.
    3.90.700.10. 1 hit.
    InterProi IPR003953. FAD_bind_dom.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR010960. Flavocytochrome_c.
    IPR011031. Multihaem_cyt.
    IPR027477. Succ_DH/fumarate_Rdtase_cat.
    IPR012286. Tetrahaem_cytochrome.
    [Graphical view ]
    Pfami PF00890. FAD_binding_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    SUPFAMi SSF56425. SSF56425. 1 hit.
    TIGRFAMsi TIGR01813. flavo_cyto_c. 1 hit.
    PROSITEi PS51008. MULTIHEME_CYTC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification of a small tetraheme cytochrome c and a flavocytochrome c as two of the principal soluble cytochromes c in Shewanella oneidensis strain MR1."
      Tsapin A.I., Vandenberghe I., Nealson K.H., Scott J.H., Meyer T.E., Cusanovich M.A., Harada E., Kaizu T., Akutsu H., Leys D., Van Beeumen J.J.
      Appl. Environ. Microbiol. 67:3236-3244(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      Strain: MR-1.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MR-1.
    3. "Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1."
      Leys D., Tsapin A.S., Nealson K.H., Meyer T.E., Cusanovich M.A., Van Beeumen J.J.
      Nat. Struct. Biol. 6:1113-1117(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FAD; HEMES AND SUBSTRATE.
      Strain: MR-1.

    Entry informationi

    Entry nameiFRDA_SHEON
    AccessioniPrimary (citable) accession number: P83223
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 27, 2002
    Last sequence update: November 25, 2002
    Last modified: September 3, 2014
    This is version 103 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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