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UniProtKB - P05042 (FUMC_ECOLI)

Protein

Fumarate hydratase class II

Gene

fumC

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

Involved in the TCA cycle. FumC seems to be a backup enzyme for FumA under conditions of iron limitation and oxidative stress (PubMed:7592392). Catalyzes the stereospecific interconversion of fumarate to L-malate (PubMed:1917897, PubMed:3282546).1 Publication3 Publications

Miscellaneous

There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors.UniRule annotation2 Publications

<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 describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by ATP, citrate and S-2,3-dicarboxyaziridine.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 1149 sec(-1) for fumarate (at pH 7.9). Kcat is 595.2 sec(-1) for S-malate (at pH 7.9).1 Publication
  1. KM=50 µM for L-malate (at pH 7.3 and 30 degrees Celsius)1 Publication
  2. KM=207 µM for fumarate (at pH 7.9)1 Publication
  3. KM=390 µM for fumarate1 Publication
  4. KM=857 µM for S-malate (at pH 7.9)1 Publication
  5. KM=2.94 mM for S-malate1 Publication
  1. Vmax=1 µmol/min/mg enzyme for fumarate1 Publication
  2. Vmax=1 µmol/min/mg enzyme for S-malate1 Publication
  3. Vmax=344.8 µmol/min/mg enzyme for fumarate (at pH 7.9)1 Publication
  4. Vmax=176.8 µmol/min/mg enzyme for S-malate (at pH 7.9)1 Publication

pH dependencei

Optimum pH is 8.1 Publication

Temperature dependencei

Thermostable.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.UniRule annotationCurated
Proteins known to be involved in this subpathway in this organism are:
  1. Fumarate hydratase class II (fumC), Fumarate hydratase class I, aerobic (fumA)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from fumarate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei126SubstrateCombined sources2 Publications1
Binding sitei187SubstrateUniRule annotation1
<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 sitei188Proton donor/acceptorUniRule annotation1 Publication1
Active sitei318UniRule annotation1
Binding sitei319SubstrateUniRule annotation1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei331Important for catalytic activityUniRule annotation1 Publication1

<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

  • fumarate hydratase activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • fumarate metabolic process Source: GO_Central
  • malate metabolic process Source: GO_Central
  • response to oxidative stress Source: EcoCyc
  • tricarboxylic acid cycle Source: GO_Central
View the complete GO annotation on QuickGO ...

<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 functionAllosteric enzyme, Lyase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:FUMC-MONOMER
MetaCyc:FUMC-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		4.2.1.2 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P05042

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi
UPA00223;UER01007

<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 hydratase class II1 PublicationUniRule annotation (EC:4.2.1.2UniRule annotation2 Publications)
Short name:
Fumarase C1 PublicationUniRule annotation
Alternative name(s):
Aerobic fumarase1 PublicationUniRule annotation
Iron-independent fumarase1 PublicationUniRule annotation
<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:fumC1 PublicationUniRule annotation
Ordered Locus Names:b1611, JW1603
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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		EG10358 fumC

<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

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cytoplasm

<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

Cells lacking this gene show an increase of biofilm formation.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>Mutagenesisi126R → A: 10-fold decrease of fumarase activity. 1 Publication1
Mutagenesisi127K → D: No effect. 1 Publication1
Mutagenesisi129H → N: No effect on fumarase activity and essentially same conformation compared to the wild-type, but appears to dramatically reduce binding of ligands at the B-site. 2 Publications1
Mutagenesisi188H → N: 200-fold decrease of fumarase activity. 1 Publication1
Mutagenesisi315E → Q: There is essentially no effect on the affinity values for both S-malate and fumarate. In contrast, the catalytic efficiency values have been lowered by 10-fold in both directions. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB03452 3-Trimethylsilylsuccinic Acid
DB04272 Citric Acid
DB03499 Malate Ion
DB02749 Pyromellitic Acid

<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_00001612751 – 467Fumarate hydratase class IIAdd BLAST467

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P05042

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

More...PaxDbi		P05042

PRoteomics IDEntifications database

More...PRIDEi		P05042

<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

Under conditions of iron limitation and oxidative stress.2 Publications

<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

Homotetramer.UniRule annotation6 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4263123, 11 interactors

Database of interacting proteins

More...DIPi		DIP-9719N

Protein interaction database and analysis system

More...IntActi		P05042, 14 interactors

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_1744

<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

1467
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		P05042

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

More...SMRi		P05042

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		P05042

<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>Regioni98 – 100Substrate bindingUniRule annotationCombined sources3 Publications3
Regioni129 – 132Substrate binding (B site)Combined sources3 Publications4
Regioni139 – 141Substrate bindingUniRule annotationCombined sources3 Publications3
Regioni324 – 326Substrate bindingUniRule annotation3

<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

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105C9Q Bacteria
COG0114 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000061736

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P05042

KEGG Orthology (KO)

More...KOi		K01679

Database for complete collections of gene phylogenies

More...PhylomeDBi		P05042

Family and domain databases

Conserved Domains Database

More...CDDi		cd01362 Fumarase_classII, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.275.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00743 FumaraseC, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR005677 Fum_hydII
IPR024083 Fumarase/histidase_N
IPR018951 Fumarase_C_C
IPR020557 Fumarate_lyase_CS
IPR000362 Fumarate_lyase_fam
IPR022761 Fumarate_lyase_N
IPR008948 L-Aspartase-like

The PANTHER Classification System

More...PANTHERi		PTHR11444 PTHR11444, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF10415 FumaraseC_C, 1 hit
PF00206 Lyase_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00149 FUMRATELYASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48557 SSF48557, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00979 fumC_II, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00163 FUMARATE_LYASES, 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.

P05042-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNTVRSEKDS MGAIDVPADK LWGAQTQRSL EHFRISTEKM PTSLIHALAL 
        60         70         80         90        100
TKRAAAKVNE DLGLLSEEKA SAIRQAADEV LAGQHDDEFP LAIWQTGSGT 
       110        120        130        140        150
QSNMNMNEVL ANRASELLGG VRGMERKVHP NDDVNKSQSS NDVFPTAMHV 
       160        170        180        190        200
AALLALRKQL IPQLKTLTQT LNEKSRAFAD IVKIGRTHLQ DATPLTLGQE 
       210        220        230        240        250
ISGWVAMLEH NLKHIEYSLP HVAELALGGT AVGTGLNTHP EYARRVADEL 
       260        270        280        290        300
AVITCAPFVT APNKFEALAT CDALVQAHGA LKGLAASLMK IANDVRWLAS 
       310        320        330        340        350
GPRCGIGEIS IPENEPGSSI MPGKVNPTQC EALTMLCCQV MGNDVAINMG 
       360        370        380        390        400
GASGNFELNV FRPMVIHNFL QSVRLLADGM ESFNKHCAVG IEPNRERINQ 
       410        420        430        440        450
LLNESLMLVT ALNTHIGYDK AAEIAKKAHK EGLTLKAAAL ALGYLSEAEF 
       460 
DSWVRPEQMV GSMKAGR
Length:467
Mass (Da):50,489
Last modified:August 13, 1987 - 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:i3D67E3C0F0FDF40B
GO

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
X04065 Genomic DNA Translation: CAA27698.1
U00096 Genomic DNA Translation: AAC74683.1
AP009048 Genomic DNA Translation: BAA15349.1
X00522 Genomic DNA Translation: CAA25205.1

Protein sequence database of the Protein Information Resource

More...PIRi		S07138 UFEC

NCBI Reference Sequences

More...RefSeqi		NP_416128.1, NC_000913.3
WP_001099085.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC74683; AAC74683; b1611
BAA15349; BAA15349; BAA15349

Database of genes from NCBI RefSeq genomes

More...GeneIDi		946147

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW1603
eco:b1611

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.651

<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
X04065 Genomic DNA Translation: CAA27698.1
U00096 Genomic DNA Translation: AAC74683.1
AP009048 Genomic DNA Translation: BAA15349.1
X00522 Genomic DNA Translation: CAA25205.1
PIRiS07138 UFEC
RefSeqiNP_416128.1, NC_000913.3
WP_001099085.1, NZ_LN832404.1

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
1FUOX-ray1.98A/B1-467[»]
1FUPX-ray2.30A/B1-467[»]
1FUQX-ray2.00A/B1-467[»]
1FURX-ray1.95A/B1-467[»]
1KQ7X-ray2.60A/B1-467[»]
1YFEX-ray2.19A1-467[»]
2FUSX-ray2.20A/B1-467[»]
ProteinModelPortaliP05042
SMRiP05042
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263123, 11 interactors
DIPiDIP-9719N
IntActiP05042, 14 interactors
STRINGi316385.ECDH10B_1744

Chemistry databases

DrugBankiDB03452 3-Trimethylsilylsuccinic Acid
DB04272 Citric Acid
DB03499 Malate Ion
DB02749 Pyromellitic Acid

Proteomic databases

EPDiP05042
PaxDbiP05042
PRIDEiP05042

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74683; AAC74683; b1611
BAA15349; BAA15349; BAA15349
GeneIDi946147
KEGGiecj:JW1603
eco:b1611
PATRICifig|1411691.4.peg.651

Organism-specific databases

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

More...EchoBASEi		EB0353
EcoGeneiEG10358 fumC

Phylogenomic databases

eggNOGiENOG4105C9Q Bacteria
COG0114 LUCA
HOGENOMiHOG000061736
InParanoidiP05042
KOiK01679
PhylomeDBiP05042

Enzyme and pathway databases

UniPathwayi
UPA00223;UER01007

BioCyciEcoCyc:FUMC-MONOMER
MetaCyc:FUMC-MONOMER
BRENDAi4.2.1.2 2026
SABIO-RKiP05042

Miscellaneous databases

EvolutionaryTraceiP05042

Protein Ontology

More...PROi		PR:P05042

Family and domain databases

CDDicd01362 Fumarase_classII, 1 hit
Gene3Di1.10.275.10, 1 hit
HAMAPiMF_00743 FumaraseC, 1 hit
InterProiView protein in InterPro
IPR005677 Fum_hydII
IPR024083 Fumarase/histidase_N
IPR018951 Fumarase_C_C
IPR020557 Fumarate_lyase_CS
IPR000362 Fumarate_lyase_fam
IPR022761 Fumarate_lyase_N
IPR008948 L-Aspartase-like
PANTHERiPTHR11444 PTHR11444, 1 hit
PfamiView protein in Pfam
PF10415 FumaraseC_C, 1 hit
PF00206 Lyase_1, 1 hit
PRINTSiPR00149 FUMRATELYASE
SUPFAMiSSF48557 SSF48557, 1 hit
TIGRFAMsiTIGR00979 fumC_II, 1 hit
PROSITEiView protein in PROSITE
PS00163 FUMARATE_LYASES, 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 nameiFUMC_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: P05042
Secondary accession number(s): P76891
<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: August 13, 1987
Last sequence update: August 13, 1987
Last modified: December 5, 2018
This is version 173 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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