ID FUMC_NITEU Reviewed; 462 AA. AC Q82SM5; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 121. 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}; OrderedLocusNames=NE2286; OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC OS 14298). OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=228410; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298; RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003; RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.; RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate RT chemolithoautotroph Nitrosomonas europaea."; RL J. Bacteriol. 185:2759-2773(2003). 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}. 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; AL954747; CAD86198.1; -; Genomic_DNA. DR RefSeq; WP_011112773.1; NC_004757.1. DR AlphaFoldDB; Q82SM5; -. DR SMR; Q82SM5; -. DR STRING; 228410.NE2286; -. DR KEGG; neu:NE2286; -. DR eggNOG; COG0114; Bacteria. DR HOGENOM; CLU_021594_4_1_4; -. DR OrthoDB; 9802809at2; -. DR PhylomeDB; Q82SM5; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000001416; Chromosome. DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro. DR GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule. DR CDD; cd01362; Fumarase_classII; 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; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR NCBIfam; TIGR00979; fumC_II; 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..462 FT /note="Fumarate hydratase class II" FT /id="PRO_0000161292" FT REGION 120..141 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 462 AA; 49530 MW; D20178003603A48A CRC64; MDQYREEHDA IGTVQVPASA LWGAQTQRSL NNFNISGERM PSALIHALAL VKRAAASVNH DLGLLDENIA RAIITAADEV LAGEHAGEFP LVVWQTGSGT QTNMNMNEVL ANRASEILGG TRGKGRKVHP NDHVNKGQSS NDVFPTAMHI AAVEAIRNRL IPALEALRKT LSSKSAAFSD IVKIGRTHLQ DATPLTLGQE FSGYVSQLDH GLAHLESALP HLLELALGGT AVGTGLNTHP EFARRVAAEI ARLSGYPFIT AANKFEALAA HDALVHAHGV LKTLAAILIK IANDVRWLAS GPRCGIGEIL IPENEPGSSI MPGKVNPTQS EAVVMLACQV MGNDVAINLG GAMGNFELNT MKPLIIHNFL QSTRLLADGA ESFNTHCAAG ITANTVRIKQ HLQESLMLVT ALNPHIGYDK AAEIAKKAHH EMLTLKEAAI RLGYVTAEQF DVWVDPQKMT EV //