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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

(S)-malate = fumarate + H2O.UniRule annotation2 Publications

Enzyme 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
  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

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 I, aerobic (fumA), Fumarate hydratase class II (fumC)
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
Binding sitei126SubstrateCombined sources2 Publications1
Binding sitei187SubstrateUniRule annotation1
Active sitei188Proton donor/acceptorUniRule annotation1 Publication1
Active sitei318UniRule annotation1
Binding sitei319SubstrateUniRule annotation1
Sitei331Important for catalytic activityUniRule annotation1 Publication1

GO - Molecular functioni

  • fumarate hydratase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionAllosteric enzyme, Lyase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

BioCyciEcoCyc:FUMC-MONOMER
MetaCyc:FUMC-MONOMER
BRENDAi4.2.1.2 2026
SABIO-RKiP05042
UniPathwayiUPA00223; 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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10358 fumC

Subcellular locationi

  • Cytoplasm UniRule annotationCurated

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene show an increase of biofilm formation.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001612751 – 467Fumarate hydratase class IIAdd BLAST467

Proteomic databases

EPDiP05042
PaxDbiP05042
PRIDEiP05042

Expressioni

Inductioni

Under conditions of iron limitation and oxidative stress.2 Publications

Interactioni

Subunit structurei

Homotetramer.UniRule annotation6 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

1467
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Beta strandi12 – 16Combined sources5
Helixi24 – 32Combined sources9
Helixi42 – 61Combined sources20
Helixi67 – 81Combined sources15
Turni82 – 85Combined sources4
Helixi86 – 88Combined sources3
Beta strandi92 – 95Combined sources4
Helixi100 – 117Combined sources18
Helixi130 – 134Combined sources5
Turni135 – 137Combined sources3
Helixi140 – 158Combined sources19
Helixi160 – 177Combined sources18
Turni178 – 180Combined sources3
Beta strandi182 – 187Combined sources6
Beta strandi190 – 196Combined sources7
Helixi197 – 222Combined sources26
Turni230 – 232Combined sources3
Helixi242 – 254Combined sources13
Helixi264 – 269Combined sources6
Helixi272 – 298Combined sources27
Beta strandi302 – 305Combined sources4
Beta strandi308 – 310Combined sources3
Helixi328 – 352Combined sources25
Helixi362 – 386Combined sources25
Helixi388 – 390Combined sources3
Helixi395 – 404Combined sources10
Helixi406 – 408Combined sources3
Helixi409 – 413Combined sources5
Turni414 – 416Combined sources3
Helixi418 – 431Combined sources14
Helixi435 – 441Combined sources7
Helixi447 – 453Combined sources7
Helixi456 – 458Combined sources3

3D structure databases

ProteinModelPortaliP05042
SMRiP05042
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05042

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni98 – 100Substrate bindingUniRule annotationCombined sources3 Publications3
Regioni129 – 132Substrate binding (B site)Combined sources3 Publications4
Regioni139 – 141Substrate bindingUniRule annotationCombined sources3 Publications3
Regioni324 – 326Substrate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C9Q Bacteria
COG0114 LUCA
HOGENOMiHOG000061736
InParanoidiP05042
KOiK01679
OMAiVSFTDNC
PhylomeDBiP05042

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

Sequencei

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
Checksum:i3D67E3C0F0FDF40B
GO

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

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiFUMC_ECOLI
AccessioniPrimary (citable) accession number: P05042
Secondary accession number(s): P76891
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: March 28, 2018
This is version 170 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

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