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Protein

Fumarate reductase flavoprotein subunit

Gene

frdA

Organism
Escherichia coli (strain K12)
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

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.1 Publication

<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 covalently per subunit. Flavinylated by SdhE, about 5% flavinylation occurs in the absence of SdhE (PubMed:24374335, PubMed:26644464).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei2331
Active sitei2491

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 bindingi9 – 23FADSequence analysisAdd BLAST15

<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

  • electron transfer activity Source: EcoCyc
  • FAD binding Source: EcoCyc
  • flavin adenine dinucleotide binding Source: GO_Central
  • fumarate reductase (menaquinone) Source: UniProtKB-EC
  • succinate dehydrogenase activity Source: EcoCyc

GO - Biological processi

  • anaerobic respiration Source: EcoCyc
  • bacterial-type flagellum assembly Source: EcoCyc
  • bacterial-type flagellum-dependent cell motility Source: EcoCyc
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • fermentation Source: EcoCyc

<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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:FUM-FLAVO
MetaCyc:FUM-FLAVO

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.3.5.4 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00363

<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)
<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:frdA
Ordered Locus Names:b4154, JW4115
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10330 frdA

<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

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

No anaerobic growth on glycerol fumarate medium.1 Publication

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>Mutagenesisi45H → R: Inactivates enzyme. 1 Publication1
Mutagenesisi45H → S, C or Y: Decreased ability (greater than 70%) to reduce fumarate. 1 Publication1
Mutagenesisi131K → M: Increased cross-linking to SdhE, FrdA is slightly less flavinylated. 1 Publication1
Mutagenesisi177M → A: No longer forms cross-link to SdhE, FrdA is still flavinylated. 1 Publication1
Mutagenesisi178E → A: Decreased cross-linking to SdhE, FrdA is still flavinylated. 1 Publication1
Mutagenesisi207G → M: Increased cross-linking to SdhE, FrdA is flavinylated. 1 Publication1
Mutagenesisi233H → S: Severely affects succinate oxidation, decreases fumarate oxidation by 75%. 1 Publication1
Mutagenesisi240S → M: Increased cross-linking to SdhE, FrdA is flavinylated. 1 Publication1
Mutagenesisi248C → S or A: Does not inactivate enzyme. 1 Publication1
Mutagenesisi249R → H or L: Inactivates enzyme. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB07918 2-HEPTYL-4-HYDROXY QUINOLINE N-OXIDE
DB00730 Thiabendazole

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
<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_00001586602 – 602Fumarate reductase flavoprotein subunitAdd BLAST601

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei45Tele-8alpha-FAD histidine1

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P00363

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P00363

PRoteomics IDEntifications database

More...
PRIDEi
P00363

<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

Fumarate dehydrogenase forms part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, and two hydrophobic anchor proteins. Can be cross-linked to SdhE (PubMed:26644464).1 Publication1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4260883, 174 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1967 Plasma membrane fumarate reductase complex

Database of interacting proteins

More...
DIPi
DIP-9681N

Protein interaction database and analysis system

More...
IntActi
P00363, 15 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_4349

<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

1602
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1KF6X-ray2.70A/M1-602[»]
1KFYX-ray3.60A/M1-602[»]
1L0VX-ray3.30A/M1-602[»]
2B76X-ray3.30A/M1-602[»]
3CIRX-ray3.65A/M1-602[»]
3P4PX-ray2.80A/M1-577[»]
3P4QX-ray3.35A/M1-577[»]
3P4RX-ray3.05A/M1-577[»]
3P4SX-ray3.10A/M1-577[»]
4KX6X-ray2.95A/M1-577[»]
5VPNX-ray4.22A/E1-585[»]
6AWFX-ray3.35A/E1-602[»]
6B58X-ray2.61A/C1-577[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P00363

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

More...
SMRi
P00363

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
P00363

<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

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C00 Bacteria
COG1053 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000160475

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00363

KEGG Orthology (KO)

More...
KOi
K00244

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P00363

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
IPR003952 FRD_SDH_FAD_BS
IPR037099 Fum_R/Succ_DH_flav-like_C_sf
IPR015939 Fum_Rdtase/Succ_DH_flav-like_C
IPR005884 Fum_red_fp
IPR027477 Succ_DH/fumarate_Rdtase_cat_sf
IPR014006 Succ_Dhase_FrdA_Gneg

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00890 FAD_binding_2, 1 hit
PF02910 Succ_DH_flav_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46977 SSF46977, 1 hit
SSF51905 SSF51905, 1 hit
SSF56425 SSF56425, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01176 fum_red_Fp, 1 hit
TIGR01812 sdhA_frdA_Gneg, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00504 FRD_SDH_FAD_BINDING, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P00363-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQTFQADLAI VGAGGAGLRA AIAAAQANPN AKIALISKVY PMRSHTVAAE
60 70 80 90 100
GGSAAVAQDH DSFEYHFHDT VAGGDWLCEQ DVVDYFVHHC PTEMTQLELW
110 120 130 140 150
GCPWSRRPDG SVNVRRFGGM KIERTWFAAD KTGFHMLHTL FQTSLQFPQI
160 170 180 190 200
QRFDEHFVLD ILVDDGHVRG LVAMNMMEGT LVQIRANAVV MATGGAGRVY
210 220 230 240 250
RYNTNGGIVT GDGMGMALSH GVPLRDMEFV QYHPTGLPGS GILMTEGCRG
260 270 280 290 300
EGGILVNKNG YRYLQDYGMG PETPLGEPKN KYMELGPRDK VSQAFWHEWR
310 320 330 340 350
KGNTISTPRG DVVYLDLRHL GEKKLHERLP FICELAKAYV GVDPVKEPIP
360 370 380 390 400
VRPTAHYTMG GIETDQNCET RIKGLFAVGE CSSVGLHGAN RLGSNSLAEL
410 420 430 440 450
VVFGRLAGEQ ATERAATAGN GNEAAIEAQA AGVEQRLKDL VNQDGGENWA
460 470 480 490 500
KIRDEMGLAM EEGCGIYRTP ELMQKTIDKL AELQERFKRV RITDTSSVFN
510 520 530 540 550
TDLLYTIELG HGLNVAECMA HSAMARKESR GAHQRLDEGC TERDDVNFLK
560 570 580 590 600
HTLAFRDADG TTRLEYSDVK ITTLPPAKRV YGGEADAADK AEAANKKEKA

NG
Length:602
Mass (Da):65,972
Last modified:January 23, 2007 - v3
<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:i3306D7FF6E198AE9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti386L → P in AAA23437 (PubMed:7037404).Curated1

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
J01611 Genomic DNA Translation: AAA23437.1
U14003 Genomic DNA Translation: AAA97053.1
U00096 Genomic DNA Translation: AAC77114.1
AP009048 Genomic DNA Translation: BAE78158.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A00376 RDECFF

NCBI Reference Sequences

More...
RefSeqi
NP_418578.1, NC_000913.3
WP_001192973.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC77114; AAC77114; b4154
BAE78158; BAE78158; BAE78158

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948667

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW4115
eco:b4154

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2544

<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
J01611 Genomic DNA Translation: AAA23437.1
U14003 Genomic DNA Translation: AAA97053.1
U00096 Genomic DNA Translation: AAC77114.1
AP009048 Genomic DNA Translation: BAE78158.1
PIRiA00376 RDECFF
RefSeqiNP_418578.1, NC_000913.3
WP_001192973.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KF6X-ray2.70A/M1-602[»]
1KFYX-ray3.60A/M1-602[»]
1L0VX-ray3.30A/M1-602[»]
2B76X-ray3.30A/M1-602[»]
3CIRX-ray3.65A/M1-602[»]
3P4PX-ray2.80A/M1-577[»]
3P4QX-ray3.35A/M1-577[»]
3P4RX-ray3.05A/M1-577[»]
3P4SX-ray3.10A/M1-577[»]
4KX6X-ray2.95A/M1-577[»]
5VPNX-ray4.22A/E1-585[»]
6AWFX-ray3.35A/E1-602[»]
6B58X-ray2.61A/C1-577[»]
ProteinModelPortaliP00363
SMRiP00363
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260883, 174 interactors
ComplexPortaliCPX-1967 Plasma membrane fumarate reductase complex
DIPiDIP-9681N
IntActiP00363, 15 interactors
STRINGi316385.ECDH10B_4349

Chemistry databases

DrugBankiDB07918 2-HEPTYL-4-HYDROXY QUINOLINE N-OXIDE
DB00730 Thiabendazole

Proteomic databases

jPOSTiP00363
PaxDbiP00363
PRIDEiP00363

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77114; AAC77114; b4154
BAE78158; BAE78158; BAE78158
GeneIDi948667
KEGGiecj:JW4115
eco:b4154
PATRICifig|1411691.4.peg.2544

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0326
EcoGeneiEG10330 frdA

Phylogenomic databases

eggNOGiENOG4105C00 Bacteria
COG1053 LUCA
HOGENOMiHOG000160475
InParanoidiP00363
KOiK00244
PhylomeDBiP00363

Enzyme and pathway databases

BioCyciEcoCyc:FUM-FLAVO
MetaCyc:FUM-FLAVO
BRENDAi1.3.5.4 2026
SABIO-RKiP00363

Miscellaneous databases

EvolutionaryTraceiP00363

Protein Ontology

More...
PROi
PR:P00363

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
IPR003952 FRD_SDH_FAD_BS
IPR037099 Fum_R/Succ_DH_flav-like_C_sf
IPR015939 Fum_Rdtase/Succ_DH_flav-like_C
IPR005884 Fum_red_fp
IPR027477 Succ_DH/fumarate_Rdtase_cat_sf
IPR014006 Succ_Dhase_FrdA_Gneg
PfamiView protein in Pfam
PF00890 FAD_binding_2, 1 hit
PF02910 Succ_DH_flav_C, 1 hit
SUPFAMiSSF46977 SSF46977, 1 hit
SSF51905 SSF51905, 1 hit
SSF56425 SSF56425, 1 hit
TIGRFAMsiTIGR01176 fum_red_Fp, 1 hit
TIGR01812 sdhA_frdA_Gneg, 1 hit
PROSITEiView protein in PROSITE
PS00504 FRD_SDH_FAD_BINDING, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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_ECOLI
<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: P00363
Secondary accession number(s): Q2M6E8
<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: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 191 of the entry and version 3 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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