FUMA_ECOLI
ID FUMA_ECOLI Reviewed; 548 AA.
AC P0AC33; P00923; P76889;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Fumarate hydratase class I, aerobic {ECO:0000303|PubMed:3282546};
DE EC=4.2.1.2 {ECO:0000269|PubMed:1329945, ECO:0000269|PubMed:23405168, ECO:0000269|PubMed:8422384};
DE AltName: Full=Fumarase A {ECO:0000303|PubMed:1329945};
DE AltName: Full=Oxaloacetate keto--enol-isomerase {ECO:0000303|PubMed:8422384};
DE Short=OAAKE isomerase {ECO:0000303|PubMed:8422384};
DE AltName: Full=Oxaloacetate tautomerase {ECO:0000305|PubMed:8422384};
DE EC=5.3.2.2 {ECO:0000269|PubMed:8422384};
GN Name=fumA {ECO:0000303|PubMed:6328431}; OrderedLocusNames=b1612, JW1604;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6328431; DOI=10.1093/nar/12.8.3631;
RA Miles J.S., Guest J.R.;
RT "Complete nucleotide sequence of the fumarase gene fumA, of Escherichia
RT coli.";
RL Nucleic Acids Res. 12:3631-3642(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC STRAIN=W / ATCC 11105 / DSM 1900;
RX PubMed=1917897; DOI=10.1093/oxfordjournals.jbchem.a123448;
RA Ueda Y., Yumoto N., Tokushige M., Fukui K., Ohya-Nishiguchi H.;
RT "Purification and characterization of two types of fumarase from
RT Escherichia coli.";
RL J. Biochem. 109:728-733(1991).
RN [6]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP FUNCTION, AND INDUCTION.
RX DOI=10.1111/j.1574-6968.1987.tb02545.x;
RA Woods S.A., Guest J.R.;
RT "Differential roles of the Escherichia coli fumarases and fnr-dependent
RT expression of fumarase B and aspartase.";
RL FEMS Microbiol. Lett. 48:219-224(1987).
RN [8]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=3282546; DOI=10.1016/0167-4838(88)90050-7;
RA Woods S.A., Shwartzbach S.D., Guest J.R.;
RT "Two biochemically distinct classes of fumarase in Escherichia coli.";
RL Biochim. Biophys. Acta 954:14-26(1988).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=1329945; DOI=10.1021/bi00157a022;
RA Flint D.H., Emptage M.H., Guest J.R.;
RT "Fumarase a from Escherichia coli: purification and characterization as an
RT iron-sulfur cluster containing enzyme.";
RL Biochemistry 31:10331-10337(1992).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC STRAIN=K12;
RX PubMed=8422384; DOI=10.1021/bi00054a009;
RA Flint D.H.;
RT "Escherichia coli fumarase A catalyzes the isomerization of enol and keto
RT oxalacetic acid.";
RL Biochemistry 32:799-805(1993).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=K12;
RX PubMed=23405168; DOI=10.1371/journal.pone.0055549;
RA van Vugt-Lussenburg B.M., van der Weel L., Hagen W.R., Hagedoorn P.L.;
RT "Biochemical similarities and differences between the catalytic [4Fe-4S]
RT cluster containing fumarases FumA and FumB from Escherichia coli.";
RL PLoS ONE 8:E55549-E55549(2013).
CC -!- FUNCTION: Catalyzes the reversible hydration of fumarate to (S)-malate.
CC Functions as an aerobic enzyme in the direction of malate formation as
CC part of the citric acid cycle. Accounts for about 80% of the fumarase
CC activity when the bacteria grow aerobically. To a lesser extent, also
CC displays D-tartrate dehydratase activity in vitro, but is not able to
CC convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the
CC isomerization of enol- to keto-oxaloacetate.
CC {ECO:0000269|PubMed:1329945, ECO:0000269|PubMed:23405168,
CC ECO:0000269|PubMed:3282546, ECO:0000269|PubMed:8422384,
CC ECO:0000269|Ref.7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2;
CC Evidence={ECO:0000269|PubMed:1329945, ECO:0000269|PubMed:23405168,
CC ECO:0000269|PubMed:8422384};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxaloacetate = enol-oxaloacetate; Xref=Rhea:RHEA:16021,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:17479; EC=5.3.2.2;
CC Evidence={ECO:0000269|PubMed:8422384};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:1329945, ECO:0000269|PubMed:23405168};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000269|PubMed:1329945,
CC ECO:0000269|PubMed:23405168};
CC -!- ACTIVITY REGULATION: Is inactivated by oxygen, due to oxidation of the
CC Fe-S cluster to its [3Fe-4S] form. Both the fumarase and the isomerase
CC reactions are competitively inhibited by 3-hydroxy-2-nitropropionate.
CC The isomerase reaction is also inhibited by fumarate and malate.
CC {ECO:0000269|PubMed:1329945, ECO:0000269|PubMed:23405168,
CC ECO:0000269|PubMed:8422384}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for (S)-malate {ECO:0000269|PubMed:1329945,
CC ECO:0000269|PubMed:23405168};
CC KM=0.6 mM for fumarate {ECO:0000269|PubMed:8422384};
CC KM=0.46 mM for fumarate {ECO:0000269|PubMed:23405168};
CC KM=0.8 mM for D-tartrate {ECO:0000269|PubMed:23405168};
CC KM=0.1 mM for enol-oxaloacetate {ECO:0000269|PubMed:8422384};
CC Vmax=720 umol/min/mg enzyme for (S)-malate dehydration
CC {ECO:0000269|PubMed:23405168};
CC Vmax=1900 umol/min/mg enzyme for fumarate hydration
CC {ECO:0000269|PubMed:23405168};
CC Vmax=2.3 umol/min/mg enzyme for D-tartrate dehydration
CC {ECO:0000269|PubMed:23405168};
CC Note=kcat is 3000 sec(-1) for the hydration of fumarate and 300 sec(-
CC 1) for the isomerization of enol-oxaloacetate.
CC {ECO:0000269|PubMed:8422384};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC from fumarate: step 1/1. {ECO:0000303|PubMed:1329945,
CC ECO:0000303|PubMed:3282546}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1329945,
CC ECO:0000269|PubMed:3282546}.
CC -!- INTERACTION:
CC P0AC33; P0AC33: fumA; NbExp=2; IntAct=EBI-549075, EBI-549075;
CC -!- INDUCTION: Is expressed under aerobic conditions. Is repressed by
CC glucose and anaerobiosis. {ECO:0000269|Ref.7}.
CC -!- SIMILARITY: Belongs to the class-I fumarase family. {ECO:0000305}.
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DR EMBL; X00522; CAA25204.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15360.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74684.1; -; Genomic_DNA.
DR PIR; A03531; UFECAQ.
DR RefSeq; NP_416129.1; NC_000913.3.
DR RefSeq; WP_000066639.1; NZ_STEB01000003.1.
DR AlphaFoldDB; P0AC33; -.
DR SMR; P0AC33; -.
DR BioGRID; 4263122; 17.
DR BioGRID; 851167; 1.
DR DIP; DIP-36200N; -.
DR IntAct; P0AC33; 5.
DR STRING; 511145.b1612; -.
DR jPOST; P0AC33; -.
DR PaxDb; P0AC33; -.
DR PRIDE; P0AC33; -.
DR EnsemblBacteria; AAC74684; AAC74684; b1612.
DR EnsemblBacteria; BAA15360; BAA15360; BAA15360.
DR GeneID; 60668420; -.
DR GeneID; 946826; -.
DR KEGG; ecj:JW1604; -.
DR KEGG; eco:b1612; -.
DR PATRIC; fig|1411691.4.peg.650; -.
DR EchoBASE; EB0351; -.
DR eggNOG; COG1838; Bacteria.
DR eggNOG; COG1951; Bacteria.
DR HOGENOM; CLU_026758_0_0_6; -.
DR InParanoid; P0AC33; -.
DR OMA; AGVLPMC; -.
DR PhylomeDB; P0AC33; -.
DR BioCyc; EcoCyc:FUMA-MON; -.
DR BioCyc; MetaCyc:FUMA-MON; -.
DR BRENDA; 4.2.1.2; 2026.
DR BRENDA; 4.2.1.34; 2026.
DR SABIO-RK; P0AC33; -.
DR UniPathway; UPA00223; UER01007.
DR PRO; PR:P0AC33; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0004333; F:fumarate hydratase activity; IDA:EcoliWiki.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050163; F:oxaloacetate tautomerase activity; IDA:EcoCyc.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IMP:EcoCyc.
DR Gene3D; 3.20.130.10; -; 1.
DR InterPro; IPR004646; Fe-S_hydro-lyase_TtdA-typ_cat.
DR InterPro; IPR004647; Fe-S_hydro-lyase_TtdB-typ_cat.
DR InterPro; IPR036660; Fe-S_hydroAse_TtdB_cat_sf.
DR InterPro; IPR011167; Fe_dep_fumarate_hydratase.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR Pfam; PF05681; Fumerase; 1.
DR Pfam; PF05683; Fumerase_C; 1.
DR PIRSF; PIRSF001394; Fe_dep_fumar_hy; 1.
DR SUPFAM; SSF117457; SSF117457; 1.
DR TIGRFAMs; TIGR00722; ttdA_fumA_fumB; 1.
DR TIGRFAMs; TIGR00723; ttdB_fumA_fumB; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Isomerase; Lyase;
KW Metal-binding; Reference proteome; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..548
FT /note="Fumarate hydratase class I, aerobic"
FT /id="PRO_0000195656"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:E9AE57"
FT BINDING 224
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:E9AE57"
FT BINDING 318
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:E9AE57"
SQ SEQUENCE 548 AA; 60299 MW; 6082744088C64603 CRC64;
MSNKPFHYQA PFPLKKDDTE YYLLTSEHVS VSEFEGQEIL KVAPEALTLL ARQAFHDASF
MLRPAHQQQV ADILRDPEAS ENDKYVALQF LRNSDIAAKG VLPTCQDTGT AIIVGKKGQR
VWTGGGDEAA LARGVYNTYI EDNLRYSQNA PLDMYKEVNT GTNLPAQIDL YAVDGDEYKF
LCIAKGGGSA NKTYLYQETK ALLTPGKLKN YLVEKMRTLG TAACPPYHIA FVIGGTSAET
NLKTVKLASA KYYDELPTEG NEHGQAFRDV ELEKELLIEA QNLGLGAQFG GKYFAHDIRV
IRLPRHGASC PVGMGVSCSA DRNIKAKINR QGIWIEKLEH NPGKYIPEEL RKAGEGEAVR
VDLNRPMKEI LAQLSQYPVS TRLSLNGTII VGRDIAHAKL KERMDNGEGL PQYIKDHPIY
YAGPAKTPEG YASGSLGPTT AGRMDSYVDQ LQAQGGSMIM LAKGNRSQQV TDACKKHGGF
YLGSIGGPAA VLAQGSIKSL ECVEYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIQL
TQCTRCVK
