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Protein

Fumarate hydratase class I, aerobic

Gene

fumA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate.5 Publications

Catalytic activityi

(S)-malate = fumarate + H2O.3 Publications
Keto-oxaloacetate = enol-oxaloacetate.1 Publication

Cofactori

[4Fe-4S] cluster2 PublicationsNote: Binds 1 [4Fe-4S] cluster per subunit.2 Publications

Enzyme regulationi

Is inactivated by oxygen, due to oxidation of the Fe-S cluster to its [3Fe-4S] form. Both the fumarase and the isomerase reactions are competitively inhibited by 3-hydroxy-2-nitropropionate. The isomerase reaction is also inhibited by fumarate and malate.3 Publications

Kineticsi

kcat is 3000 sec(-1) for the hydration of fumarate and 300 sec(-1) for the isomerization of enol-oxaloacetate.1 Publication

  1. KM=0.7 mM for (S)-malate1 Publication
  2. KM=0.7 mM for (S)-malate1 Publication
  3. KM=0.6 mM for fumarate1 Publication
  4. KM=0.46 mM for fumarate1 Publication
  5. KM=0.8 mM for D-tartrate1 Publication
  6. KM=0.1 mM for enol-oxaloacetate1 Publication
  1. Vmax=720 µmol/min/mg enzyme for (S)-malate dehydration1 Publication
  2. Vmax=1900 µmol/min/mg enzyme for fumarate hydration1 Publication
  3. Vmax=2.3 µmol/min/mg enzyme for D-tartrate dehydration1 Publication

Pathway:itricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.2 Publications
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.

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • fumarate hydratase activity Source: EcoliWiki
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • oxaloacetate tautomerase activity Source: EcoCyc

GO - Biological processi

  • tricarboxylic acid cycle Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:FUMA-MONOMER.
ECOL316407:JW1604-MONOMER.
MetaCyc:FUMA-MONOMER.
RETL1328306-WGS:GSTH-2399-MONOMER.
SABIO-RKP0AC33.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class I, aerobic1 Publication (EC:4.2.1.23 Publications)
Alternative name(s):
Fumarase A1 Publication
Oxaloacetate keto--enol-isomerase1 Publication
Short name:
OAAKE isomerase1 Publication
Oxaloacetate tautomerase1 Publication (EC:5.3.2.21 Publication)
Gene namesi
Name:fumA1 Publication
Ordered Locus Names:b1612, JW1604
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10356. fumA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 548547Fumarate hydratase class I, aerobicPRO_0000195656Add
BLAST

Proteomic databases

PaxDbiP0AC33.
PRIDEiP0AC33.

Expressioni

Inductioni

Is expressed under aerobic conditions. Is repressed by glucose and anaerobiosis.1 Publication

Interactioni

Subunit structurei

Homodimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-549075,EBI-549075

Protein-protein interaction databases

DIPiDIP-36200N.
IntActiP0AC33. 5 interactions.
MINTiMINT-1310290.
STRINGi511145.b1612.

Structurei

3D structure databases

ProteinModelPortaliP0AC33.
SMRiP0AC33. Positions 356-537.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-I fumarase family.Curated

Phylogenomic databases

eggNOGiCOG1838.
HOGENOMiHOG000009338.
InParanoidiP0AC33.
KOiK01676.
OMAiQIQTSQC.
OrthoDBiEOG6TXR10.
PhylomeDBiP0AC33.

Family and domain databases

Gene3Di3.20.130.10. 1 hit.
InterProiIPR004646. Fe-S_hydro-lyase_TtdA-typ_cat.
IPR004647. Fe-S_hydro-lyase_TtdB-typ_cat.
IPR011167. Fe_dep_fumarate_hydratase.
IPR020557. Fumarate_lyase_CS.
[Graphical view]
PfamiPF05681. Fumerase. 1 hit.
PF05683. Fumerase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF001394. Fe_dep_fumar_hy. 1 hit.
SUPFAMiSSF117457. SSF117457. 1 hit.
TIGRFAMsiTIGR00722. ttdA_fumA_fumB. 1 hit.
TIGR00723. ttdB_fumA_fumB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AC33-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNKPFHYQA PFPLKKDDTE YYLLTSEHVS VSEFEGQEIL KVAPEALTLL
60 70 80 90 100
ARQAFHDASF MLRPAHQQQV ADILRDPEAS ENDKYVALQF LRNSDIAAKG
110 120 130 140 150
VLPTCQDTGT AIIVGKKGQR VWTGGGDEAA LARGVYNTYI EDNLRYSQNA
160 170 180 190 200
PLDMYKEVNT GTNLPAQIDL YAVDGDEYKF LCIAKGGGSA NKTYLYQETK
210 220 230 240 250
ALLTPGKLKN YLVEKMRTLG TAACPPYHIA FVIGGTSAET NLKTVKLASA
260 270 280 290 300
KYYDELPTEG NEHGQAFRDV ELEKELLIEA QNLGLGAQFG GKYFAHDIRV
310 320 330 340 350
IRLPRHGASC PVGMGVSCSA DRNIKAKINR QGIWIEKLEH NPGKYIPEEL
360 370 380 390 400
RKAGEGEAVR VDLNRPMKEI LAQLSQYPVS TRLSLNGTII VGRDIAHAKL
410 420 430 440 450
KERMDNGEGL PQYIKDHPIY YAGPAKTPEG YASGSLGPTT AGRMDSYVDQ
460 470 480 490 500
LQAQGGSMIM LAKGNRSQQV TDACKKHGGF YLGSIGGPAA VLAQGSIKSL
510 520 530 540
ECVEYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIQL TQCTRCVK
Length:548
Mass (Da):60,299
Last modified:January 23, 2007 - v2
Checksum:i6082744088C64603
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00522 Genomic DNA. Translation: CAA25204.1.
AP009048 Genomic DNA. Translation: BAA15360.1.
U00096 Genomic DNA. Translation: AAC74684.1.
PIRiA03531. UFECAQ.
RefSeqiNP_416129.1. NC_000913.3.
WP_000066639.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC74684; AAC74684; b1612.
BAA15360; BAA15360; BAA15360.
GeneIDi946826.
KEGGieco:b1612.
PATRICi32118526. VBIEscCol129921_1683.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00522 Genomic DNA. Translation: CAA25204.1.
AP009048 Genomic DNA. Translation: BAA15360.1.
U00096 Genomic DNA. Translation: AAC74684.1.
PIRiA03531. UFECAQ.
RefSeqiNP_416129.1. NC_000913.3.
WP_000066639.1. NZ_CP010445.1.

3D structure databases

ProteinModelPortaliP0AC33.
SMRiP0AC33. Positions 356-537.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36200N.
IntActiP0AC33. 5 interactions.
MINTiMINT-1310290.
STRINGi511145.b1612.

Proteomic databases

PaxDbiP0AC33.
PRIDEiP0AC33.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74684; AAC74684; b1612.
BAA15360; BAA15360; BAA15360.
GeneIDi946826.
KEGGieco:b1612.
PATRICi32118526. VBIEscCol129921_1683.

Organism-specific databases

EchoBASEiEB0351.
EcoGeneiEG10356. fumA.

Phylogenomic databases

eggNOGiCOG1838.
HOGENOMiHOG000009338.
InParanoidiP0AC33.
KOiK01676.
OMAiQIQTSQC.
OrthoDBiEOG6TXR10.
PhylomeDBiP0AC33.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciEcoCyc:FUMA-MONOMER.
ECOL316407:JW1604-MONOMER.
MetaCyc:FUMA-MONOMER.
RETL1328306-WGS:GSTH-2399-MONOMER.
SABIO-RKP0AC33.

Miscellaneous databases

PROiP0AC33.

Family and domain databases

Gene3Di3.20.130.10. 1 hit.
InterProiIPR004646. Fe-S_hydro-lyase_TtdA-typ_cat.
IPR004647. Fe-S_hydro-lyase_TtdB-typ_cat.
IPR011167. Fe_dep_fumarate_hydratase.
IPR020557. Fumarate_lyase_CS.
[Graphical view]
PfamiPF05681. Fumerase. 1 hit.
PF05683. Fumerase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF001394. Fe_dep_fumar_hy. 1 hit.
SUPFAMiSSF117457. SSF117457. 1 hit.
TIGRFAMsiTIGR00722. ttdA_fumA_fumB. 1 hit.
TIGR00723. ttdB_fumA_fumB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequence of the fumarase gene fumA, of Escherichia coli."
    Miles J.S., Guest J.R.
    Nucleic Acids Res. 12:3631-3642(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Purification and characterization of two types of fumarase from Escherichia coli."
    Ueda Y., Yumoto N., Tokushige M., Fukui K., Ohya-Nishiguchi H.
    J. Biochem. 109:728-733(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
    Strain: W / ATCC 11105 / DSM 1900.
  6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12.
    Strain: K12 / EMG2.
  7. "Differential roles of the Escherichia coli fumarases and fnr-dependent expression of fumarase B and aspartase."
    Woods S.A., Guest J.R.
    FEMS Microbiol. Lett. 48:219-224(1987)
    Cited for: FUNCTION, INDUCTION.
  8. "Two biochemically distinct classes of fumarase in Escherichia coli."
    Woods S.A., Shwartzbach S.D., Guest J.R.
    Biochim. Biophys. Acta 954:14-26(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
    Strain: K12.
  9. "Fumarase a from Escherichia coli: purification and characterization as an iron-sulfur cluster containing enzyme."
    Flint D.H., Emptage M.H., Guest J.R.
    Biochemistry 31:10331-10337(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
    Strain: K12.
  10. "Escherichia coli fumarase A catalyzes the isomerization of enol and keto oxalacetic acid."
    Flint D.H.
    Biochemistry 32:799-805(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    Strain: K12.
  11. "Biochemical similarities and differences between the catalytic [4Fe-4S] cluster containing fumarases FumA and FumB from Escherichia coli."
    van Vugt-Lussenburg B.M., van der Weel L., Hagen W.R., Hagedoorn P.L.
    PLoS ONE 8:E55549-E55549(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    Strain: K12.

Entry informationi

Entry nameiFUMA_ECOLI
AccessioniPrimary (citable) accession number: P0AC33
Secondary accession number(s): P00923, P76889
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.