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P0C278

- FRDA_SHEFR

UniProt

P0C278 - FRDA_SHEFR

Protein

Fumarate reductase flavoprotein subunit

Gene

fccA

Organism
Shewanella frigidimarina
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 39 (01 Oct 2014)
      Sequence version 1 (12 Dec 2006)
      Previous versions | rss
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    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.

    Catalytic activityi

    Succinate + a quinone = fumarate + a quinol.

    Cofactori

    Binds 1 FAD per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi8 – 81Iron (heme 2 axial ligand)
    Binding sitei14 – 141Heme 1 (covalent)
    Binding sitei17 – 171Heme 1 (covalent)
    Metal bindingi18 – 181Iron (heme 1 axial ligand)
    Binding sitei36 – 361Heme 2 (covalent)
    Binding sitei39 – 391Heme 2 (covalent)
    Metal bindingi40 – 401Iron (heme 2 axial ligand)
    Metal bindingi58 – 581Iron (heme 3 axial ligand)
    Metal bindingi61 – 611Iron (heme 4 axial ligand)
    Binding sitei68 – 681Heme 3 (covalent)
    Binding sitei71 – 711Heme 3 (covalent)
    Metal bindingi72 – 721Iron (heme 3 axial ligand)
    Metal bindingi75 – 751Iron (heme 1 axial ligand)
    Binding sitei82 – 821Heme 4 (covalent)
    Binding sitei85 – 851Heme 4 (covalent)
    Metal bindingi86 – 861Iron (heme 4 axial ligand)
    Binding sitei365 – 3651Substrate
    Binding sitei377 – 3771Substrate
    Active sitei402 – 4021Proton donor
    Binding sitei504 – 5041Substrate
    Binding sitei544 – 5441Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi132 – 14312FAD1 PublicationAdd
    BLAST
    Nucleotide bindingi156 – 1572FAD1 Publication
    Nucleotide bindingi164 – 1652FAD1 Publication
    Nucleotide bindingi169 – 1713FAD1 Publication
    Nucleotide bindingi549 – 5502FAD1 Publication

    GO - Molecular functioni

    1. electron carrier activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. succinate dehydrogenase activity Source: InterPro

    GO - Biological processi

    1. anaerobic electron transport chain Source: UniProtKB
    2. anaerobic respiration Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Transport

    Keywords - Ligandi

    FAD, Flavoprotein, Heme, Iron, Metal-binding

    Enzyme and pathway databases

    SABIO-RKP0C278.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate reductase flavoprotein subunit (EC:1.3.5.4)
    Alternative name(s):
    Flavocytochrome c
    Flavocytochrome c3
    Short name:
    Fcc3
    Gene namesi
    Name:fccA
    Synonyms:fcc3
    OrganismiShewanella frigidimarina
    Taxonomic identifieri56812 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

    Subcellular locationi

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: UniProtKB

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi61 – 611H → A: Reduces catalytic activity 10-fold. Reduces affinity for fumarate. 1 Publication
    Mutagenesisi61 – 611H → M: Reduces catalytic activity 5-fold. Reduces affinity for fumarate. 1 Publication
    Mutagenesisi365 – 3651H → A: Reduces catalytic activity by over 75%. 1 Publication
    Mutagenesisi378 – 3781E → D: Strongly reduced affinity for substrate. Reduces activity 10000-fold. 1 Publication
    Mutagenesisi381 – 3811R → M: Strongly reduced catalytic activity. No effect on substrate affinity. 1 Publication
    Mutagenesisi402 – 4021R → A: Loss of activity. 2 Publications
    Mutagenesisi402 – 4021R → K or Y: Reduces activity 10000-fold. 2 Publications
    Mutagenesisi504 – 5041H → A: Reduces catalytic activity by over 64%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 571571Fumarate reductase flavoprotein subunitPRO_0000010344Add
    BLAST

    Expressioni

    Inductioni

    By anaerobiosis and fumarate.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    571
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 96
    Helixi14 – 163
    Helixi30 – 4011
    Helixi43 – 475
    Turni57 – 593
    Helixi68 – 703
    Beta strandi74 – 763
    Helixi81 – 844
    Helixi107 – 1115
    Helixi112 – 1209
    Beta strandi124 – 1263
    Beta strandi128 – 1325
    Helixi136 – 14712
    Beta strandi152 – 1554
    Beta strandi157 – 1615
    Helixi165 – 1673
    Helixi178 – 1825
    Helixi189 – 19911
    Turni200 – 2023
    Helixi206 – 22520
    Beta strandi232 – 2343
    Beta strandi244 – 2474
    Turni248 – 2503
    Helixi253 – 26715
    Beta strandi271 – 28313
    Beta strandi289 – 2968
    Turni297 – 2993
    Beta strandi300 – 3056
    Beta strandi307 – 3115
    Helixi320 – 3267
    Helixi328 – 3303
    Beta strandi335 – 3373
    Helixi344 – 3518
    Beta strandi356 – 3583
    Beta strandi362 – 3698
    Turni370 – 3723
    Beta strandi373 – 3753
    Helixi379 – 3824
    Beta strandi386 – 3883
    Helixi402 – 4109
    Helixi413 – 4153
    Beta strandi417 – 4226
    Helixi423 – 4286
    Helixi432 – 4387
    Beta strandi443 – 4464
    Helixi447 – 4548
    Helixi458 – 47417
    Turni478 – 4803
    Beta strandi494 – 50613
    Beta strandi509 – 5124
    Beta strandi517 – 5193
    Beta strandi525 – 5317
    Beta strandi536 – 5405
    Helixi548 – 56720

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E39X-ray1.80A1-571[»]
    1JRXX-ray2.00A/B1-571[»]
    1JRYX-ray2.00A/B1-571[»]
    1JRZX-ray2.00A/B1-571[»]
    1KSSX-ray1.80A1-571[»]
    1KSUX-ray2.00A/B1-571[»]
    1LJ1X-ray2.00A/B1-571[»]
    1M64X-ray1.80A/B1-571[»]
    1P2EX-ray2.20A1-571[»]
    1P2HX-ray2.10A1-571[»]
    1Q9IX-ray1.60A1-571[»]
    1QJDX-ray1.80A1-571[»]
    1Y0PX-ray1.50A1-571[»]
    2B7RX-ray1.70A1-571[»]
    2B7SX-ray2.12A1-571[»]
    ProteinModelPortaliP0C278.
    SMRiP0C278. Positions 1-568.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C278.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 117117Cytochrome cAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni118 – 571454Flavoprotein-likeAdd
    BLAST

    Sequence similaritiesi

    In the C-terminal section; belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.Curated
    Contains 1 cytochrome c domain.Curated

    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.
    IPR007087. Znf_C2H2.
    [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.

    P0C278-1 [UniParc]FASTAAdd to Basket

    « Hide

    ADNLAEFHVQ NQECDSCHTP DGELSNDSLT YENTQCVSCH GTLEEVAETT    50
    KHEHYNAHAS HFPGEVACTS CHSAHEKSMV YCDSCHSFDF NMPYAKKWQR 100
    DEPTIAELAK DKSERQAALA SAPHDTVDVV VVGSGGAGFS AAISATDSGA 150
    KVILIEKEPV IGGNAKLAAG GMNAAWTDQQ KAKKITDSPE LMFEDTMKGG 200
    QNINDPALVK VLSSHSKDSV DWMTAMGADL TDVGMMGGAS VNRAHRPTGG 250
    AGVGAHVVQV LYDNAVKRNI DLRMNTRGIE VLKDDKGTVK GILVKGMYKG 300
    YYWVKADAVI LATGGFAKNN ERVAKLDPSL KGFISTNQPG AVGDGLDVAE 350
    NAGGALKDMQ YIQAHPTLSV KGGVMVTEAV RGNGAILVNR EGKRFVNEIT 400
    TRDKASAAIL AQTGKSAYLI FDDSVRKSLS KIDKYIGLGV APTADSLVKL 450
    GKMEGIDGKA LTETVARYNS LVSSGKDTDF ERPNLPRALN EGNYYAIEVT 500
    PGVHHTMGGV MIDTKAEVMN AKKQVIPGLY GAGEVTGGVH GANRLGGNAI 550
    SDIITFGRLA GEEAAKYSKK N 571
    Length:571
    Mass (Da):60,621
    Last modified:December 12, 2006 - v1
    Checksum:iD2E4FC43C9A6484C
    GO

    Mass spectrometryi

    Molecular mass is 63033±10 Da from positions 1 - 571. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ132010 Genomic DNA. Translation: CAB38558.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ132010 Genomic DNA. Translation: CAB38558.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E39 X-ray 1.80 A 1-571 [» ]
    1JRX X-ray 2.00 A/B 1-571 [» ]
    1JRY X-ray 2.00 A/B 1-571 [» ]
    1JRZ X-ray 2.00 A/B 1-571 [» ]
    1KSS X-ray 1.80 A 1-571 [» ]
    1KSU X-ray 2.00 A/B 1-571 [» ]
    1LJ1 X-ray 2.00 A/B 1-571 [» ]
    1M64 X-ray 1.80 A/B 1-571 [» ]
    1P2E X-ray 2.20 A 1-571 [» ]
    1P2H X-ray 2.10 A 1-571 [» ]
    1Q9I X-ray 1.60 A 1-571 [» ]
    1QJD X-ray 1.80 A 1-571 [» ]
    1Y0P X-ray 1.50 A 1-571 [» ]
    2B7R X-ray 1.70 A 1-571 [» ]
    2B7S X-ray 2.12 A 1-571 [» ]
    ProteinModelPortali P0C278.
    SMRi P0C278. Positions 1-568.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P0C278.

    Miscellaneous databases

    EvolutionaryTracei P0C278.

    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.
    IPR007087. Znf_C2H2.
    [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

    1. "Crystallization and preliminary X-ray analysis of flavocytochrome c(3), the fumarate reductase from Shewanella frigidimarina."
      Pealing S.L., Lysek D.A., Taylor P., Alexeev D., Reid G.A., Chapman S.K., Walkinshaw M.D.
      J. Struct. Biol. 127:76-78(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-571, CRYSTALLIZATION.
      Strain: ACAM591.
    2. "Structural and mechanistic mapping of a unique fumarate reductase."
      Taylor P., Pealing S.L., Reid G.A., Chapman S.K., Walkinshaw M.D.
      Nat. Struct. Biol. 6:1108-1112(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    3. "Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and crystallographic study."
      Doherty M.K., Pealing S.L., Miles C.S., Moysey R., Taylor P., Walkinshaw M.D., Reid G.A., Chapman S.K.
      Biochemistry 39:10695-10701(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-365 AND ALA-504 IN COMPLEX WITH FAD; FUMARATE AND HEMES, MUTAGENESIS OF HIS-365; ARG-402 AND HIS-504.
    4. "Kinetic and crystallographic analysis of the key active site acid/base arginine in a soluble fumarate reductase."
      Mowat C.G., Moysey R., Miles C.S., Leys D., Doherty M.K., Taylor P., Walkinshaw M.D., Reid G.A., Chapman S.K.
      Biochemistry 40:12292-12298(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS ALA-402; LYS-402 AND TYR-402, MUTAGENESIS OF ARG-402, ENZYME KINETICS.
    5. "Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina."
      Pankhurst K.L., Mowat C.G., Miles C.S., Leys D., Walkinshaw M.D., Reid G.A., Chapman S.K.
      Biochemistry 41:8551-8556(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-505 AND TYR-505, CHARACTERIZATION.
    6. "Engineering water to act as an active site acid catalyst in a soluble fumarate reductase."
      Mowat C.G., Pankhurst K.L., Miles C.S., Leys D., Walkinshaw M.D., Reid G.A., Chapman S.K.
      Biochemistry 41:11990-11996(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS PHE-363 AND PHE-363/ALA-402, CHARACTERIZATION, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Histidine 61: an important heme ligand in the soluble fumarate reductase from Shewanella frigidimarina."
      Rothery E.L., Mowat C.G., Miles C.S., Walkinshaw M.D., Reid G.A., Chapman S.K.
      Biochemistry 42:13160-13169(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANTS ALA-61 AND MET-61 IN COMPLEXES WITH HEME; SUBSTRATE AND FAD, MASS SPECTROMETRY, MUTAGENESIS OF HIS-61.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MUTANT CYS-251/CYS430.
    9. "A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina."
      Pankhurst K.L., Mowat C.G., Rothery E.L., Hudson J.M., Jones A.K., Miles C.S., Walkinshaw M.D., Armstrong F.A., Reid G.A., Chapman S.K.
      J. Biol. Chem. 281:20589-20597(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANTS ASP-378 AND MET-381, MUTAGENESIS OF GLU-378 AND ARG-381, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiFRDA_SHEFR
    AccessioniPrimary (citable) accession number: P0C278
    Secondary accession number(s): Q02469, Q9X969
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 39 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    The N-terminal sequence has been extracted from PDB entry 1LJ1.Curated

    Keywords - Technical termi

    3D-structure

    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