ID FUMC_RICCN Reviewed; 463 AA. AC Q92GW0; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 117. 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=RC1012; OS Rickettsia conorii (strain ATCC VR-613 / Malish 7). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=272944; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-613 / Malish 7; RX PubMed=11557893; DOI=10.1126/science.1061471; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(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}. 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; AE006914; AAL03550.1; -; Genomic_DNA. DR PIR; D97826; D97826. DR RefSeq; WP_010977593.1; NC_003103.1. DR AlphaFoldDB; Q92GW0; -. DR SMR; Q92GW0; -. DR GeneID; 928156; -. DR KEGG; rco:RC1012; -. DR HOGENOM; CLU_021594_4_1_5; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000000816; 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; Tricarboxylic acid cycle. FT CHAIN 1..463 FT /note="Fumarate hydratase class II" FT /id="PRO_0000161306" FT REGION 121..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 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 463 AA; 50839 MW; BA74C64811FC5359 CRC64; MKNYRTESDS FGEIQIEEKF YWGAQTQRSL ENFKIGKQKM PEILIRALAI LKKCAAQVNH EFGDLEAKIA ISIDKATDRI LEGEFEDNFP LVVWQTGSGT QTNMNMNEVI ASIANEELTG KKGGKSPVHP NDHVNKGQSS NDSFPTAMHI ATVLATKQQL IPALNNILTS LQDKSKDWDK IIKIGRTHLQ DATPLTLKQE FSGYITQIEY ALERIENALQ KVYLLAQGGT AVGTGINSKI GFDIKFAEKV AEFTKQPFKT APNKFESLAA HDALVEFSGT LNTIAVSLMK IANDIRLLGS GPRCGLGELH LPENEPGSSI MPGKVNPTQV EALTMVCSQV MGNHVTVTIA GSNGHLELNV FKPVIIYNIL QSIELLSDSV NSFVTHCVKG LEPNIARIND LRDKSLMLVT ALNPHIGYDN AAKIAKEAHK HGITLKEAAK KLNLLSEAKF DKIVVPEKMV SQS //