ID   FUMA_SALTY              Reviewed;         580 AA.
AC   P40720;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 141.
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=STM1468;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RC   STRAIN=C5;
RX   PubMed=1879695; DOI=10.1016/0378-1119(91)90406-2;
RA   Collins L.V., Hackett J.;
RT   "Sequence of the phosphomannose isomerase-encoding gene of Salmonella
RT   typhimurium.";
RL   Gene 103:135-136(1991).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE006468; AAL20388.1; -; Genomic_DNA.
DR   EMBL; X57117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_460429.2; NC_003197.2.
DR   AlphaFoldDB; P40720; -.
DR   SMR; P40720; -.
DR   STRING; 99287.STM1468; -.
DR   PaxDb; 99287-STM1468; -.
DR   GeneID; 1252986; -.
DR   KEGG; stm:STM1468; -.
DR   PATRIC; fig|99287.12.peg.1550; -.
DR   HOGENOM; CLU_026758_0_0_6; -.
DR   PhylomeDB; P40720; -.
DR   UniPathway; UPA00223; UER01007.
DR   PHI-base; PHI:10046; -.
DR   Proteomes; UP000001014; 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   CHAIN           1..580
FT                   /note="Fumarate hydratase class I, aerobic"
FT                   /id="PRO_0000195659"
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   580 AA;  63825 MW;  DF36C9E67D6FBE39 CRC64;
     MSNKPFFYQD PFPLKKDDTE YYLLTSEHVS VAEFEGQEIL KVAPEALTLL ARQAFHDASF
     MLRPAHQQQV ADILRDPQAS ENDKYVALQF LRNSDIAAKG VLPTCQDTGT AIIVGKKGQR
     VWTGGGDEAA LARGVYNTYI EDNLRYSQNA ALDMYKEVNT GTNLPAQIDL YSVDGDEYKF
     LCIAKGGGSA NKTYLYQETK ALLTPGKLKN YLVDKMRTLG TAACPPYHIA FVIGGTSAEA
     NLKTVKLASA KYYDALPTEG NEHGQAFRDI ELEKELLLEA QNLGLGAQFG GKYFAHDIRV
     IRLPRHGASC PVGMGVSCSA DRNIKAKINR DGIWIEKLER NPGKYIPEAL RQAGEGEAVR
     VDLNRPMSEI LQQLSQYPVS TRLSLNGTII VGRDIAHAKL KERMDRGEGL PQYIKDHPIY
     YAGPAKTPEG YASGSLGPTT AGRMDSYVDQ LQSQGGSMIM LAKGNRSQQV TDACKKHGGF
     YLGSIGGPAA VLAQGSIKRL ECVEYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIQS
     SQCGAALSNV AALRGGNMIR YFAGERRKRL IRSTPLCCYR
//