Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fumarate reductase flavoprotein subunit

Gene

fccA

Organism
Shewanella frigidimarina
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

Caution

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FADNote: Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi8Iron (heme 2 axial ligand)1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei14Heme 1 (covalent)1
Binding sitei17Heme 1 (covalent)1
Metal bindingi18Iron (heme 1 axial ligand)1
Binding sitei36Heme 2 (covalent)1
Binding sitei39Heme 2 (covalent)1
Metal bindingi40Iron (heme 2 axial ligand)1
Metal bindingi58Iron (heme 3 axial ligand)1
Metal bindingi61Iron (heme 4 axial ligand)1
Binding sitei68Heme 3 (covalent)1
Binding sitei71Heme 3 (covalent)1
Metal bindingi72Iron (heme 3 axial ligand)1
Metal bindingi75Iron (heme 1 axial ligand)1
Binding sitei82Heme 4 (covalent)1
Binding sitei85Heme 4 (covalent)1
Metal bindingi86Iron (heme 4 axial ligand)1
Binding sitei365Substrate1
Binding sitei377Substrate1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei402Proton donor1
Binding sitei504Substrate1
Binding sitei544Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi132 – 143FAD1 PublicationAdd BLAST12
Nucleotide bindingi156 – 157FAD1 Publication2
Nucleotide bindingi164 – 165FAD1 Publication2
Nucleotide bindingi169 – 171FAD1 Publication3
Nucleotide bindingi549 – 550FAD1 Publication2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Transport
LigandFAD, Flavoprotein, Heme, Iron, Metal-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0C278

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Fumarate reductase flavoprotein subunit (EC:1.3.5.4)
Alternative name(s):
Flavocytochrome c
Flavocytochrome c3
Short name:
Fcc3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:fccA
Synonyms:fcc3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiShewanella frigidimarina
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri56812 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi61H → A: Reduces catalytic activity 10-fold. Reduces affinity for fumarate. 1 Publication1
Mutagenesisi61H → M: Reduces catalytic activity 5-fold. Reduces affinity for fumarate. 1 Publication1
Mutagenesisi365H → A: Reduces catalytic activity by over 75%. 1 Publication1
Mutagenesisi378E → D: Strongly reduced affinity for substrate. Reduces activity 10000-fold. 1 Publication1
Mutagenesisi381R → M: Strongly reduced catalytic activity. No effect on substrate affinity. 1 Publication1
Mutagenesisi402R → A: Loss of activity. 2 Publications1
Mutagenesisi402R → K or Y: Reduces activity 10000-fold. 2 Publications1
Mutagenesisi504H → A: Reduces catalytic activity by over 64%. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB04734 Citraconic acid
DB03147 Flavin adenine dinucleotide
DB01677 Fumarate
DB03343 Malate Like Intermediate

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000103441 – 571Fumarate reductase flavoprotein subunitAdd BLAST571

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By anaerobiosis and fumarate.

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1571
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P0C278

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0C278

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0C278

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni118 – 571Flavoprotein-likeAdd BLAST454

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1053 LUCA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.50.50.60, 1 hit
3.90.700.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003953 FAD-binding_2
IPR036188 FAD/NAD-bd_sf
IPR010960 Flavocytochrome_c
IPR011031 Multihaem_cyt
IPR036280 Multihaem_cyt_sf
IPR027477 Succ_DH/fumarate_Rdtase_cat_sf
IPR012286 Tetrahaem_cytochrome
IPR013087 Znf_C2H2_type

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF14537 Cytochrom_c3_2, 1 hit
PF00890 FAD_binding_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48695 SSF48695, 1 hit
SSF51905 SSF51905, 1 hit
SSF56425 SSF56425, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01813 flavo_cyto_c, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51008 MULTIHEME_CYTC, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P0C278-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
ADNLAEFHVQ NQECDSCHTP DGELSNDSLT YENTQCVSCH GTLEEVAETT
60 70 80 90 100
KHEHYNAHAS HFPGEVACTS CHSAHEKSMV YCDSCHSFDF NMPYAKKWQR
110 120 130 140 150
DEPTIAELAK DKSERQAALA SAPHDTVDVV VVGSGGAGFS AAISATDSGA
160 170 180 190 200
KVILIEKEPV IGGNAKLAAG GMNAAWTDQQ KAKKITDSPE LMFEDTMKGG
210 220 230 240 250
QNINDPALVK VLSSHSKDSV DWMTAMGADL TDVGMMGGAS VNRAHRPTGG
260 270 280 290 300
AGVGAHVVQV LYDNAVKRNI DLRMNTRGIE VLKDDKGTVK GILVKGMYKG
310 320 330 340 350
YYWVKADAVI LATGGFAKNN ERVAKLDPSL KGFISTNQPG AVGDGLDVAE
360 370 380 390 400
NAGGALKDMQ YIQAHPTLSV KGGVMVTEAV RGNGAILVNR EGKRFVNEIT
410 420 430 440 450
TRDKASAAIL AQTGKSAYLI FDDSVRKSLS KIDKYIGLGV APTADSLVKL
460 470 480 490 500
GKMEGIDGKA LTETVARYNS LVSSGKDTDF ERPNLPRALN EGNYYAIEVT
510 520 530 540 550
PGVHHTMGGV MIDTKAEVMN AKKQVIPGLY GAGEVTGGVH GANRLGGNAI
560 570
SDIITFGRLA GEEAAKYSKK N
Length:571
Mass (Da):60,621
Last modified:December 12, 2006 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD2E4FC43C9A6484C
GO

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

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

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ132010 Genomic DNA Translation: CAB38558.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132010 Genomic DNA Translation: CAB38558.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB04734 Citraconic acid
DB03147 Flavin adenine dinucleotide
DB01677 Fumarate
DB03343 Malate Like Intermediate

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG1053 LUCA

Enzyme and pathway databases

SABIO-RKiP0C278

Miscellaneous databases

EvolutionaryTraceiP0C278

Family and domain databases

Gene3Di3.50.50.60, 1 hit
3.90.700.10, 1 hit
InterProiView protein in InterPro
IPR003953 FAD-binding_2
IPR036188 FAD/NAD-bd_sf
IPR010960 Flavocytochrome_c
IPR011031 Multihaem_cyt
IPR036280 Multihaem_cyt_sf
IPR027477 Succ_DH/fumarate_Rdtase_cat_sf
IPR012286 Tetrahaem_cytochrome
IPR013087 Znf_C2H2_type
PfamiView protein in Pfam
PF14537 Cytochrom_c3_2, 1 hit
PF00890 FAD_binding_2, 1 hit
SUPFAMiSSF48695 SSF48695, 1 hit
SSF51905 SSF51905, 1 hit
SSF56425 SSF56425, 1 hit
TIGRFAMsiTIGR01813 flavo_cyto_c, 1 hit
PROSITEiView protein in PROSITE
PS51008 MULTIHEME_CYTC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFRDA_SHEFR
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0C278
Secondary accession number(s): Q02469, Q9X969
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: December 5, 2018
This is version 62 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again