FUMC_LISMO
ID FUMC_LISMO Reviewed; 455 AA.
AC Q8Y551;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
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}; Synonyms=citG;
GN OrderedLocusNames=lmo2225;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(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; AL591982; CAD00303.1; -; Genomic_DNA.
DR PIR; AI1352; AI1352.
DR RefSeq; NP_465749.1; NC_003210.1.
DR RefSeq; WP_003731883.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y551; -.
DR SMR; Q8Y551; -.
DR STRING; 169963.lmo2225; -.
DR PaxDb; Q8Y551; -.
DR EnsemblBacteria; CAD00303; CAD00303; CAD00303.
DR GeneID; 987997; -.
DR KEGG; lmo:lmo2225; -.
DR PATRIC; fig|169963.11.peg.2277; -.
DR eggNOG; COG0114; Bacteria.
DR HOGENOM; CLU_021594_4_1_9; -.
DR OMA; HDSMGEV; -.
DR PhylomeDB; Q8Y551; -.
DR BioCyc; LMON169963:LMO2225-MON; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR GO; GO:0004333; F:fumarate hydratase activity; IBA:GO_Central.
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 Gene3D; 1.10.275.10; -; 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; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR PANTHER; PTHR11444; PTHR11444; 1.
DR Pfam; PF10415; FumaraseC_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00979; fumC_II; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lyase; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..455
FT /note="Fumarate hydratase class II"
FT /id="PRO_0000161286"
FT ACT_SITE 181
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT ACT_SITE 311
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 96..98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 122..125
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 132..134
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 317..319
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT SITE 324
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
SQ SEQUENCE 455 AA; 49626 MW; 5AF66C261A8F844A CRC64;
MERIERDTLG EISVDATKYW GAQTERSKRN FAIGDNPMPI EIIYAFAQLK KATAKVNAAE
GKLAEEKAIA IGQVCDQIIQ GELDEHFPLV VWQTGSGTQS NMNVNEVIAH VANLTLGEGQ
IHPNDDVNMS QSSNDTFPTA MHIAAYGALV TKLLPEITKM EAVLTEKKNK YMHLVKIGRT
HLQDATPLTL GQEISGWEAC LTNNKNYLET SMKAILPLAI GGTAVGTGLN ASRDFGDKVA
EELMKQTGYP FTSDSNKYFA LTSHSPINFV HGAIRSLASD LMKIANDIRL LASGPRSGIG
ELEIPANEPG SSIMPGKVNP TQCEAITMVA AQVMGNDVTI NVAASQGNFE LNVYKPVIIF
NFLESIKLLA DSMRSFRVHC LEGLTANEKV IETKVNDSLM LVTALNPHIG YEKAAKIAKL
AFDENTTLKE AAIKTGFVTE KEFDLWINPL KMTNL
