|Gene:||fumB||Accession Numbers: EG10357 (EcoCyc), b4122, ECK4115|
Fumarase B (FumB) is one of three fumarase isozymes participating in the TCA cycle. FumB belongs to the class I fumarases; like FumA, it is a homodimeric 4Fe-4S cluster-containing protein [Woods88, vanVugtLussenbu13]. Fumarase B is required for anaerobic growth on D-tartrate [Kim07] and appears to be involved in biofilm formation [Herzberg06].
The cell adapts to changing environmental oxygen conditions by utilizing different isozymes. Both FumA and FumB contain iron-sulfur centers; exposure to oxidative agents such as superoxide results in damage to the metal cofactor and loss of enzyme activity [Flint93b]. Although FumB was previously reported to have a higher affinity for malate than for fumarate [Woods88], recent kinetic data using a purified enzyme have shown it to be similar to FumA [vanVugtLussenbu13]. FumB is thought to function as an alternative enzyme during anaerobiosis [Woods87, Tseng01]. In contrast, FumC is an iron-independent enzyme and is insensitive to oxidative damage [Flint94]. FumC is made by the cells primarily as a backup enzyme if the FumA or FumB enzymes are damaged by reactive oxygen species. [Tseng97, Liochev93, Tseng01, Lara06]
Expression of all three fumarase genes is anaerobically controlled. Expression of fumB gene is four fold elevated under anaerobic cell growth conditions versus aerobic conditions [Tseng97]. In contrast, fumA expression is highest only during aerobic growth and where fumC is only weakly expressed. When cells encounter oxidative stress conditions, fumC gene expression is then significantly induced by the SoxRS regulatory system [Park95a]. The aerobic/anaerobic transcriptional regulators ArcA and Fnr function to repress fumA as well as fumC gene expression under anaerobic conditions.
Overexpression of fumB complements the fumA1 mutation [Guest83, Guest85] and a fumAC deletion [Henson87]. The expression level of fumB is highest under anaerobic growth on glycerol and fumarate [Woods87]. fumB expression is regulated in response to oxygen, iron and heme availability [Gruer94, Tseng97] and increases 9-fold upon deletion of tqsA, which increases biofilm formation [Herzberg06].
|Map Position: [4,343,703 <- 4,345,349] (93.62 centisomes, 337°)||Length: 1647 bp / 548 aa|
Molecular Weight of Polypeptide: 60.105 kD (from nucleotide sequence), 61.0 kD (experimental) [Guest85 ]
Molecular Weight of Multimer: 120.0 kD (experimental) [vanVugtLussenbu13]
Isozyme Sequence Similarity:
fumarase A monomer: YES
Unification Links: ASAP:ABE-0013501 , CGSC:18289 , EchoBASE:EB0352 , EcoGene:EG10357 , EcoliWiki:b4122 , OU-Microarray:b4122 , PortEco:fumB , PR:PRO_000022735 , Pride:P14407 , Protein Model Portal:P14407 , RefSeq:NP_418546 , RegulonDB:EG10357 , SMR:P14407 , String:511145.b4122 , UniProt:P14407
Relationship Links: InterPro:IN-FAMILY:IPR004646 , InterPro:IN-FAMILY:IPR004647 , InterPro:IN-FAMILY:IPR011167 , InterPro:IN-FAMILY:IPR020557 , Pfam:IN-FAMILY:PF05681 , Pfam:IN-FAMILY:PF05683 , Prosite:IN-FAMILY:PS00163
|Biological Process:||GO:0006099 - tricarboxylic acid cycle
GO:0006974 - cellular response to DNA damage stimulus [Khil02]
GO:0042710 - biofilm formation [Herzberg06]
GO:0006091 - generation of precursor metabolites and energy [GOA01a]
|Molecular Function:||GO:0004333 - fumarate hydratase activity
[GOA01, GOA01a, vanVugtLussenbu13, Flint93b]
GO:0042803 - protein homodimerization activity [vanVugtLussenbu13]
GO:0047808 - D(-)-tartrate dehydratase activity [GOA01, vanVugtLussenbu13, Kim07]
GO:0051539 - 4 iron, 4 sulfur cluster binding [UniProtGOA11a, vanVugtLussenbu13]
GO:0003824 - catalytic activity [GOA01a]
GO:0016829 - lyase activity [UniProtGOA11a, GOA01a]
GO:0016836 - hydro-lyase activity [GOA01a]
GO:0046872 - metal ion binding [UniProtGOA11a]
GO:0051536 - iron-sulfur cluster binding [UniProtGOA11a]
|Cellular Component:||GO:0005829 - cytosol [Lasserre06]|
|MultiFun Terms:||metabolism → energy metabolism, carbon → fermentation|
|metabolism → energy metabolism, carbon → TCA cycle|
|Growth Medium||Growth?||T (°C)||O2||pH||Osm/L||Growth Observations|
|LB enriched||Yes||37||Aerobic||6.95||Yes [Gerdes03, Comment 1]|
|LB Lennox||Yes||37||Aerobic||7||Yes [Baba06, Comment 2]|
|M9 medium with 1% glycerol||Yes||37||Aerobic||7.2||0.35||Yes [Joyce06, Comment 3]|
|MOPS medium with 0.4% glucose||Yes||37||Aerobic||7.2||0.22||Yes [Baba06, Comment 2] |
Yes [Feist07, Comment 4]
Enzymatic reaction of: fumarase B
Synonyms: fumarate hydratase B
EC Number: 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.
This reaction is reversible. [vanVugtLussenbu13]
Purification of fumarase B from E. coli W has been described [Yumoto88].
The midpoint potential of FumB at pH 8 is -283 mV [vanVugtLussenbu13].
Enzymatic reaction of: D-tartrate dehydratase (fumarase B)
EC Number: 184.108.40.206
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Reversibility of this reaction is unspecified.
10/20/97 Gene b4122 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10357; confirmed by SwissProt match.
AboAmer04: Abo-Amer AE, Munn J, Jackson K, Aktas M, Golby P, Kelly DJ, Andrews SC (2004). "DNA interaction and phosphotransfer of the C4-dicarboxylate-responsive DcuS-DcuR two-component regulatory system from Escherichia coli." J Bacteriol 186(6);1879-89. PMID: 14996819
Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554
Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909
Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938
Golby98: Golby P, Kelly DJ, Guest JR, Andrews SC (1998). "Transcriptional regulation and organization of the dcuA and dcuB genes, encoding homologous anaerobic C4-dicarboxylate transporters in Escherichia coli." J Bacteriol 1998;180(24);6586-96. PMID: 9852003
Gray66: Gray CT, Wimpenny JW, Mossman MR (1966). "Regulation of metabolism in facultative bacteria. II. Effects of aerobiosis, anaerobiosis and nutrition on the formation of Krebs cycle enzymes in Escherichia coli." Biochim Biophys Acta 117(1);33-41. PMID: 5330664
Guest85: Guest JR, Miles JS, Roberts RE, Woods SA (1985). "The fumarase genes of Escherichia coli: location of the fumB gene and discovery of a new gene (fumC)." J Gen Microbiol 131(11);2971-84. PMID: 3005475
Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394
Kim07: Kim OB, Lux S, Unden G (2007). "Anaerobic growth of Escherichia coli on D-tartrate depends on the fumarate carrier DcuB and fumarase, rather than the L-tartrate carrier TtdT and L-tartrate dehydratase." Arch Microbiol 188(6);583-9. PMID: 17643228
Korshunov02: Korshunov SS, Imlay JA (2002). "A potential role for periplasmic superoxide dismutase in blocking the penetration of external superoxide into the cytosol of Gram-negative bacteria." Mol Microbiol 43(1);95-106. PMID: 11849539
Lara06: Lara AR, Leal L, Flores N, Gosset G, Bolivar F, Ramirez OT (2006). "Transcriptional and metabolic response of recombinant Escherichia coli to spatial dissolved oxygen tension gradients simulated in a scale-down system." Biotechnol Bioeng 93(2);372-85. PMID: 16187334
Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726
Overton06: Overton TW, Griffiths L, Patel MD, Hobman JL, Penn CW, Cole JA, Constantinidou C (2006). "Microarray analysis of gene regulation by oxygen, nitrate, nitrite, FNR, NarL and NarP during anaerobic growth of Escherichia coli: new insights into microbial physiology." Biochem Soc Trans 34(Pt 1);104-7. PMID: 16417494
Park95a: Park SJ, Gunsalus RP (1995). "Oxygen, iron, carbon, and superoxide control of the fumarase fumA and fumC genes of Escherichia coli: role of the arcA, fnr, and soxR gene products." J Bacteriol 1995;177(21);6255-62. PMID: 7592392
Tseng01: Tseng CP, Yu CC, Lin HH, Chang CY, Kuo JT (2001). "Oxygen- and growth rate-dependent regulation of Escherichia coli fumarase (FumA, FumB, and FumC) activity." J Bacteriol 2001;183(2);461-7. PMID: 11133938
Tseng97: Tseng CP (1997). "Regulation of fumarase (fumB) gene expression in Escherichia coli in response to oxygen, iron and heme availability: role of the arcA, fur, and hemA gene products." FEMS Microbiol Lett 157(1);67-72. PMID: 9418241
vanVugtLussenbu13: van Vugt-Lussenburg BM, van der Weel L, Hagen WR, Hagedoorn PL (2013). "Biochemical Similarities and Differences between the Catalytic [4Fe-4S] Cluster Containing Fumarases FumA and FumB from Escherichia coli." PLoS One 8(2);e55549. PMID: 23405168
Zhang09: Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8(2);215-25. PMID: 18723842
Janausch04: Janausch IG, Garcia-Moreno I, Lehnen D, Zeuner Y, Unden G (2004). "Phosphorylation and DNA binding of the regulator DcuR of the fumarate-responsive two-component system DcuSR of Escherichia coli." Microbiology 150(Pt 4);877-83. PMID: 15073297
Kim09: Kim OB, Reimann J, Lukas H, Schumacher U, Grimpo J, Dunnwald P, Unden G (2009). "Regulation of tartrate metabolism by TtdR and relation to the DcuS-DcuR-regulated C4-dicarboxylate metabolism of Escherichia coli." Microbiology 155(Pt 11);3632-40. PMID: 19661178
Salmon05: Salmon KA, Hung SP, Steffen NR, Krupp R, Baldi P, Hatfield GW, Gunsalus RP (2005). "Global gene expression profiling in Escherichia coli K12: effects of oxygen availability and ArcA." J Biol Chem 280(15);15084-96. PMID: 15699038
Scheu12: Scheu PD, Witan J, Rauschmeier M, Graf S, Liao YF, Ebert-Jung A, Basche T, Erker W, Unden G (2012). "CitA/CitB two-component system regulating citrate fermentation in Escherichia coli and its relation to the DcuS/DcuR system in vivo." J Bacteriol 194(3);636-45. PMID: 22101843
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493