ID   FUMA_ECOL6              Reviewed;         548 AA.
AC   P0AC34; P00923; P76889;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Fumarate hydratase class I, aerobic {ECO:0000250|UniProtKB:P0AC33};
DE            EC=4.2.1.2 {ECO:0000250|UniProtKB:P0AC33};
DE   AltName: Full=Fumarase A {ECO:0000250|UniProtKB:P0AC33};
DE   AltName: Full=Oxaloacetate keto--enol-isomerase {ECO:0000250|UniProtKB:P0AC33};
DE            Short=OAAKE isomerase {ECO:0000250|UniProtKB:P0AC33};
DE   AltName: Full=Oxaloacetate tautomerase {ECO:0000250|UniProtKB:P0AC33};
DE            EC=5.3.2.2 {ECO:0000250|UniProtKB:P0AC33};
GN   Name=fumA {ECO:0000250|UniProtKB:P0AC33}; OrderedLocusNames=c2004;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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:0000250|UniProtKB:P0AC33}.
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:0000250|UniProtKB:P0AC33};
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:0000250|UniProtKB:P0AC33};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P0AC33};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:P0AC33};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC       from fumarate: step 1/1. {ECO:0000250|UniProtKB:P0AC33}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0AC33}.
CC   -!- INDUCTION: Is expressed under aerobic conditions. Is repressed by
CC       glucose and anaerobiosis. {ECO:0000250|UniProtKB:P0AC33}.
CC   -!- SIMILARITY: Belongs to the class-I fumarase family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN80464.1; -; Genomic_DNA.
DR   RefSeq; WP_000066639.1; NZ_CP051263.1.
DR   AlphaFoldDB; P0AC34; -.
DR   SMR; P0AC34; -.
DR   STRING; 199310.c2004; -.
DR   GeneID; 75204456; -.
DR   KEGG; ecc:c2004; -.
DR   eggNOG; COG1838; Bacteria.
DR   eggNOG; COG1951; Bacteria.
DR   HOGENOM; CLU_026758_0_0_6; -.
DR   BioCyc; ECOL199310:C2004-MONOMER; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050163; F:oxaloacetate tautomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.130.10; Fe-S hydro-lyase, tartrate dehydratase beta-type, catalytic domain; 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   NCBIfam; TIGR00722; ttdA_fumA_fumB; 1.
DR   NCBIfam; TIGR00723; ttdB_fumA_fumB; 1.
DR   PANTHER; PTHR30389:SF0; FUMARATE HYDRATASE CLASS I, AEROBIC; 1.
DR   PANTHER; PTHR30389; FUMARATE HYDRATASE-RELATED; 1.
DR   Pfam; PF05681; Fumerase; 1.
DR   Pfam; PF05683; Fumerase_C; 1.
DR   PIRSF; PIRSF001394; Fe_dep_fumar_hy; 1.
DR   SUPFAM; SSF117457; FumA C-terminal domain-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Isomerase; Lyase; Metal-binding;
KW   Reference proteome; Tricarboxylic acid cycle.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC33"
FT   CHAIN           2..548
FT                   /note="Fumarate hydratase class I, aerobic"
FT                   /id="PRO_0000195658"
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
//