ID   FUMC_SALTY              Reviewed;         467 AA.
AC   Q8ZPL7;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   04-NOV-2026, entry version 129.
DE   RecName: Full=Fumarate hydratase class II {ECO:0000255|HAMAP-Rule:MF_00743};
DE            Short=Fumarase C {ECO:0000255|HAMAP-Rule:MF_00743};
DE            EC=4.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00743};
DE   AltName: Full=Aerobic fumarase {ECO:0000255|HAMAP-Rule:MF_00743};
DE   AltName: Full=Iron-independent fumarase {ECO:0000255|HAMAP-Rule:MF_00743};
GN   Name=fumC {ECO:0000255|HAMAP-Rule:MF_00743};
GN   OrderedLocusNames=STM1469;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; 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).
CC   -!- FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific
CC       interconversion of fumarate to L-malate. {ECO:0000255|HAMAP-
CC       Rule:MF_00743}.
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:0000255|HAMAP-Rule:MF_00743};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC       from fumarate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00743}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00743}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00743}.
CC   -!- MISCELLANEOUS: There are 2 substrate-binding sites: the catalytic A
CC       site, and the non-catalytic B site that may play a role in the transfer
CC       of substrate or product between the active site and the solvent.
CC       Alternatively, the B site may bind allosteric effectors.
CC       {ECO:0000255|HAMAP-Rule:MF_00743}.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00743}.
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DR   EMBL; AE006468; AAL20389.1; -; Genomic_DNA.
DR   RefSeq; NP_460430.1; NC_003197.2.
DR   RefSeq; WP_000259121.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZPL7; -.
DR   SMR; Q8ZPL7; -.
DR   STRING; 99287.STM1469; -.
DR   PaxDb; 99287-STM1469; -.
DR   GeneID; 1252987; -.
DR   KEGG; stm:STM1469; -.
DR   PATRIC; fig|99287.12.peg.1551; -.
DR   HOGENOM; CLU_021594_4_1_6; -.
DR   OMA; AAACFKI; -.
DR   PhylomeDB; Q8ZPL7; -.
DR   BioCyc; SENT99287:STM1469-MONOMER; -.
DR   UniPathway; UPA00223; UER01007.
DR   PHI-base; PHI:10048; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004333; F:fumarate hydratase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0006106; P:fumarate metabolic process; IBA:GO_Central.
DR   GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   CDD; cd01362; Fumarase_classII; 1.
DR   FunFam; 1.10.40.30:FF:000002; Fumarate hydratase class II; 1.
DR   FunFam; 1.10.275.10:FF:000001; Fumarate hydratase, mitochondrial; 1.
DR   FunFam; 1.20.200.10:FF:000001; Fumarate hydratase, mitochondrial; 1.
DR   Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR   HAMAP; MF_00743; FumaraseC; 1.
DR   InterPro; IPR005677; Fum_hydII.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR018951; Fumarase_C_C.
DR   InterPro; IPR022761; Fumarate-Lyase-like_N.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   NCBIfam; TIGR00979; fumC_II; 1.
DR   NCBIfam; NF008909; PRK12273.1; 1.
DR   PANTHER; PTHR11444; ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR11444:SF1; FUMARATE HYDRATASE, MITOCHONDRIAL; 1.
DR   Pfam; PF10415; FumaraseC_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lyase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..467
FT                   /note="Fumarate hydratase class II"
FT                   /id="PRO_0000161309"
FT   ACT_SITE        188
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   ACT_SITE        318
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         98..100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         129..132
FT                   /ligand="substrate"
FT                   /note="in site B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         139..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         324..326
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   SITE            331
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
SQ   SEQUENCE   467 AA;  50303 MW;  8DE917F2A5CCE248 CRC64;
     MVTVRREKDS MGAIEVPADK LWGAQTQRSL EHFRISTEKM PVSLIHALAL TKRAAAKVNQ
     DLGLLAAEKA SAIIQAADEV LAGKHADEFP LAIWQTGSGT QSNMNMNEVL ANRASEILGG
     VRGMERKVHP NDDVNKSQSS NDVFPTAMHV AALLALREHL IPQLSALTDT LRDKSHAFAD
     IVKIGRTHLQ DATPLTLGQE ISGWVAMLEH NLRHIEHSLP HVAELALGGT AVGTGLNTHP
     EYARRVAEEL ATITAAPFVT APNKFEALAT CDALVQAHGA LKGLAASLMK IANDVRWLAS
     GPRCGIGEIA IPENEPGSSI MPGKVNPTQC EAVTMLCCQV MGNDVAINMG GASGNFELNV
     YRPMVIHNFL QTVRLLADGM ESFNKHCASG IEPNRERITQ LLNESLMLVT ALNTHIGYDK
     AAEIAKKAHK EGLTLKASAV ALGYLSDEEF DAWVRPELMV GSMTPGR
//