ID FUMC_NEIMA Reviewed; 462 AA. AC Q9JTR0; A1ISP3; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 124. 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=NMA1670; OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / OS Z2491). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=122587; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15465 / Z2491; RX PubMed=10761919; DOI=10.1038/35006655; RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M., RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A., RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G., RA Barrell B.G.; RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis RT Z2491."; RL Nature 404:502-506(2000). 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; AL157959; CAM08803.1; -; Genomic_DNA. DR PIR; B81862; B81862. DR RefSeq; WP_002241750.1; NC_003116.1. DR AlphaFoldDB; Q9JTR0; -. DR SMR; Q9JTR0; -. DR EnsemblBacteria; CAM08803; CAM08803; NMA1670. DR KEGG; nma:NMA1670; -. DR HOGENOM; CLU_021594_4_1_4; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000000626; 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; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; L-aspartase-like; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Cytoplasm; Lyase; Tricarboxylic acid cycle. FT CHAIN 1..462 FT /note="Fumarate hydratase class II" FT /id="PRO_0000161291" FT ACT_SITE 187 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT ACT_SITE 317 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 97..99 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 128..131 FT /ligand="substrate" FT /note="in site B" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 138..140 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 186 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 318 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 323..325 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT SITE 330 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" SQ SEQUENCE 462 AA; 49391 MW; 6F63B3D506E26C85 CRC64; MNTRTEHDTM GNVEVPSEAY WGAQTQRSRN NFKIGGETLP QPLIYALALV KKAAAATNVS LGRIKPEQAD LITQAADDVL NGKLDGQFPL VVWQTGSGTQ SNMNMNEVLA NRANEIAGTG LAAYQPVHPN DHVNHAQSTN DAFPTAIHVA AAIEINRHLI PAVKALRDTL DKKAQAFAPI VKIGRTHLQD ATPLTLGQEF SGYVSQLDHG LGRLNDALKD LYELALGGTA VGTGLNSHPE YAEKAAAKLA ELSGLPFVSA PNKFEALGGR DAAVAASGAL KTLAASLNKI ANDIRWLASG PRCGLGEIKI PENEPGSSIM PGKVNPTQCE AMTMVCCQVF GNDVTIGMAG ASGNFELNVY MPVIAYNLLQ SIRLLGDACN SFNEHCAVGI EPVPEKIDYF LHHSLMLVTA LNRKIGYENA AKVAKTAYKN NKSLRETAVE LGLLTGEEFD ELVVPADMVH PR //