|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 [Flint93a]. 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, Flint93a]
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: 220.127.116.11
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: 18.104.22.168
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.
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