ID FUMC_CHLCV Reviewed; 460 AA. AC Q822D5; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 116. 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=CCA_00748; OS Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC) OS (Chlamydophila caviae). OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=227941; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC; RX PubMed=12682364; DOI=10.1093/nar/gkg321; RA Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., RA Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., RA Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., RA Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M., RA Fraser C.M.; RT "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): RT examining the role of niche-specific genes in the evolution of the RT Chlamydiaceae."; RL Nucleic Acids Res. 31:2134-2147(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; AE015925; AAP05489.1; -; Genomic_DNA. DR RefSeq; WP_011006703.1; NC_003361.3. DR AlphaFoldDB; Q822D5; -. DR SMR; Q822D5; -. DR STRING; 227941.CCA_00748; -. DR KEGG; cca:CCA_00748; -. DR eggNOG; COG0114; Bacteria. DR HOGENOM; CLU_021594_4_1_0; -. DR OrthoDB; 9802809at2; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000002193; 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..460 FT /note="Fumarate hydratase class II" FT /id="PRO_0000161266" FT ACT_SITE 185 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT ACT_SITE 315 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 95..97 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 126..129 FT /ligand="substrate" FT /note="in site B" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 136..138 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 184 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 316 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 321..323 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT SITE 328 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" SQ SEQUENCE 460 AA; 50259 MW; 8F68DE2F0046AFDA CRC64; MRQENDSLGI VEVPEDKLYG AQTARSQKYF SWAPEVMPKE VIRALVLIKQ CAAKANHDLG FLDSKYCDMI VSAASEILEG GFEEHFPLKV WQTGSGTQSN MNVNEVIANL AIQRHGGVVG SKTPIHPNDH VNKSQSSNDV FPTAMHIAAV INLKKKLIPA MDHLQRALDA KVAEFRDCVK IGRTHLMDAV PMTLGQEFSG YSNQIRQSLE RVAFSLTHMY ELAIGGTAVG TGLNVPNGFI DKVIHYLRQE TGEPFVAASN YFSALSNHDT LVNAHGVLAT LACALTKIAT DLSFLGSGPR CGLGELLFPE NEPGSSIMPG KINPTQCEAL QMVCAQVIGN NQAVIMGGSR GNFELNVMKP VIIYNFLQSV DILAGGMQAF ADYFVSGLRV NKPRLKEYLD NSLMLVTALT PVLGYDKCSK MALKAFHDNI NLKEACIQMG YLSAEEFDRL VVPESMVGKF //