UniProtKB - P05042 (FUMC_ECOLI)
Protein
Fumarate hydratase class II
Gene
fumC
Organism
Escherichia coli (strain K12)
Status
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
Catalytic activityi
- EC:4.2.1.2UniRule annotation2 Publications
Activity regulationi
Inhibited by ATP, citrate and S-2,3-dicarboxyaziridine.1 Publication
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
- KM=50 µM for L-malate (at pH 7.3 and 30 degrees Celsius)1 Publication
- KM=207 µM for fumarate (at pH 7.9)1 Publication
- KM=390 µM for fumarate1 Publication
- KM=857 µM for S-malate (at pH 7.9)1 Publication
- KM=2.94 mM for S-malate1 Publication
- Vmax=1 µmol/min/mg enzyme for fumarate1 Publication
- Vmax=1 µmol/min/mg enzyme for S-malate1 Publication
- Vmax=344.8 µmol/min/mg enzyme for fumarate (at pH 7.9)1 Publication
- 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
: tricarboxylic acid cycle Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.UniRule annotationCuratedProteins known to be involved in this subpathway in this organism are:
- Fumarate hydratase class II (fumC), Fumarate hydratase class II (fumC), Fumarate hydratase class I, aerobic (fumA), Fumarate hydratase class II (fumC)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 126 | SubstrateCombined sources2 Publications | 1 | |
Binding sitei | 187 | SubstrateUniRule annotation | 1 | |
Active sitei | 188 | Proton donor/acceptorUniRule annotation1 Publication | 1 | |
Active sitei | 318 | UniRule annotation | 1 | |
Binding sitei | 319 | SubstrateUniRule annotation | 1 | |
Sitei | 331 | Important for catalytic activityUniRule annotation1 Publication | 1 |
GO - Molecular functioni
- fumarate hydratase activity Source: UniProtKB
- identical protein binding Source: EcoCyc
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
Keywordsi
Molecular function | Allosteric enzyme, Lyase |
Biological process | Tricarboxylic acid cycle |
Enzyme and pathway databases
BioCyci | EcoCyc:FUMC-MONOMER MetaCyc:FUMC-MONOMER |
BRENDAi | 4.2.1.2, 2026 |
SABIO-RKi | P05042 |
UniPathwayi | UPA00223;UER01007 |
Names & Taxonomyi
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 |
Gene namesi | Name:fumC1 PublicationUniRule annotation Ordered Locus Names:b1611, JW1603 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotationCurated
Other locations
- tricarboxylic acid cycle enzyme complex Source: InterPro
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
Cells lacking this gene show an increase of biofilm formation.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 126 | R → A: 10-fold decrease of fumarase activity. 1 Publication | 1 | |
Mutagenesisi | 127 | K → D: No effect. 1 Publication | 1 | |
Mutagenesisi | 129 | H → 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 Publications | 1 | |
Mutagenesisi | 188 | H → N: 200-fold decrease of fumarase activity. 1 Publication | 1 | |
Mutagenesisi | 315 | E → 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 Publication | 1 |
Chemistry databases
DrugBanki | DB03452, 3-Trimethylsilylsuccinic Acid DB04272, Citric acid DB03499, D-Malic acid DB02749, Pyromellitic Acid |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000161275 | 1 – 467 | Fumarate hydratase class IIAdd BLAST | 467 |
Proteomic databases
jPOSTi | P05042 |
PaxDbi | P05042 |
PRIDEi | P05042 |
Expressioni
Inductioni
Under conditions of iron limitation and oxidative stress.2 Publications
Interactioni
Subunit structurei
Homotetramer.
UniRule annotation6 PublicationsGO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4263123, 11 interactors |
DIPi | DIP-9719N |
IntActi | P05042, 14 interactors |
STRINGi | 511145.b1611 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P05042 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P05042 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 98 – 100 | Substrate bindingUniRule annotationCombined sources3 Publications | 3 | |
Regioni | 129 – 132 | Substrate binding (B site)Combined sources3 Publications | 4 | |
Regioni | 139 – 141 | Substrate bindingUniRule annotationCombined sources3 Publications | 3 | |
Regioni | 324 – 326 | Substrate bindingUniRule annotation | 3 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0114, Bacteria |
HOGENOMi | CLU_021594_4_1_6 |
InParanoidi | P05042 |
PhylomeDBi | P05042 |
Family and domain databases
CDDi | cd01362, Fumarase_classII, 1 hit |
Gene3Di | 1.10.275.10, 1 hit |
HAMAPi | MF_00743, FumaraseC, 1 hit |
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 |
PANTHERi | PTHR11444, PTHR11444, 1 hit |
Pfami | View protein in Pfam PF10415, FumaraseC_C, 1 hit PF00206, Lyase_1, 1 hit |
PRINTSi | PR00149, FUMRATELYASE |
SUPFAMi | SSF48557, SSF48557, 1 hit |
TIGRFAMsi | TIGR00979, fumC_II, 1 hit |
PROSITEi | View protein in PROSITE PS00163, FUMARATE_LYASES, 1 hit |
i Sequence
Sequence statusi: Complete.
P05042-1 [UniParc]FASTAAdd to basket
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
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 |
PIRi | S07138, UFEC |
RefSeqi | NP_416128.1, NC_000913.3 WP_001099085.1, NZ_SSZK01000001.1 |
Genome annotation databases
EnsemblBacteriai | AAC74683; AAC74683; b1611 BAA15349; BAA15349; BAA15349 |
GeneIDi | 57731005 946147 |
KEGGi | ecj:JW1603 eco:b1611 |
PATRICi | fig|1411691.4.peg.651 |
Similar proteinsi
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 |
PIRi | S07138, UFEC |
RefSeqi | NP_416128.1, NC_000913.3 WP_001099085.1, NZ_SSZK01000001.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1FUO | X-ray | 1.98 | A/B | 1-467 | [»] | |
1FUP | X-ray | 2.30 | A/B | 1-467 | [»] | |
1FUQ | X-ray | 2.00 | A/B | 1-467 | [»] | |
1FUR | X-ray | 1.95 | A/B | 1-467 | [»] | |
1KQ7 | X-ray | 2.60 | A/B | 1-467 | [»] | |
1YFE | X-ray | 2.19 | A | 1-467 | [»] | |
2FUS | X-ray | 2.20 | A/B | 1-467 | [»] | |
6NZ9 | X-ray | 1.53 | A/B | 1-467 | [»] | |
6NZA | X-ray | 1.41 | A/B | 1-467 | [»] | |
6NZB | X-ray | 1.37 | A/B | 1-467 | [»] | |
6NZC | X-ray | 1.40 | A/B | 1-467 | [»] | |
6OS7 | X-ray | 1.36 | A/B | 1-467 | [»] | |
6P3C | X-ray | 1.46 | A/B | 1-467 | [»] | |
SMRi | P05042 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263123, 11 interactors |
DIPi | DIP-9719N |
IntActi | P05042, 14 interactors |
STRINGi | 511145.b1611 |
Chemistry databases
DrugBanki | DB03452, 3-Trimethylsilylsuccinic Acid DB04272, Citric acid DB03499, D-Malic acid DB02749, Pyromellitic Acid |
Proteomic databases
jPOSTi | P05042 |
PaxDbi | P05042 |
PRIDEi | P05042 |
Genome annotation databases
EnsemblBacteriai | AAC74683; AAC74683; b1611 BAA15349; BAA15349; BAA15349 |
GeneIDi | 57731005 946147 |
KEGGi | ecj:JW1603 eco:b1611 |
PATRICi | fig|1411691.4.peg.651 |
Organism-specific databases
EchoBASEi | EB0353 |
Phylogenomic databases
eggNOGi | COG0114, Bacteria |
HOGENOMi | CLU_021594_4_1_6 |
InParanoidi | P05042 |
PhylomeDBi | P05042 |
Enzyme and pathway databases
UniPathwayi | UPA00223;UER01007 |
BioCyci | EcoCyc:FUMC-MONOMER MetaCyc:FUMC-MONOMER |
BRENDAi | 4.2.1.2, 2026 |
SABIO-RKi | P05042 |
Miscellaneous databases
EvolutionaryTracei | P05042 |
PROi | PR:P05042 |
Family and domain databases
CDDi | cd01362, Fumarase_classII, 1 hit |
Gene3Di | 1.10.275.10, 1 hit |
HAMAPi | MF_00743, FumaraseC, 1 hit |
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 |
PANTHERi | PTHR11444, PTHR11444, 1 hit |
Pfami | View protein in Pfam PF10415, FumaraseC_C, 1 hit PF00206, Lyase_1, 1 hit |
PRINTSi | PR00149, FUMRATELYASE |
SUPFAMi | SSF48557, SSF48557, 1 hit |
TIGRFAMsi | TIGR00979, fumC_II, 1 hit |
PROSITEi | View protein in PROSITE PS00163, FUMARATE_LYASES, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | FUMC_ECOLI | |
Accessioni | P05042Primary (citable) accession number: P05042 Secondary accession number(s): P76891 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 13, 1987 |
Last sequence update: | August 13, 1987 | |
Last modified: | April 7, 2021 | |
This is version 190 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families