ID FUMC_PROMP Reviewed; 461 AA. AC Q7V024; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, 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}; GN OrderedLocusNames=PMM1466; OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / OS MED4). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=59919; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1986 / NIES-2087 / MED4; RX PubMed=12917642; DOI=10.1038/nature01947; RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C., RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., RA Chisholm S.W.; RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche RT differentiation."; RL Nature 424:1042-1047(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; BX548174; CAE19925.1; -; Genomic_DNA. DR RefSeq; WP_011133094.1; NC_005072.1. DR AlphaFoldDB; Q7V024; -. DR SMR; Q7V024; -. DR STRING; 59919.PMM1466; -. DR KEGG; pmm:PMM1466; -. DR eggNOG; COG0114; Bacteria. DR HOGENOM; CLU_021594_4_1_3; -. DR OrthoDB; 9802809at2; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000001026; 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 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..461 FT /note="Fumarate hydratase class II" FT /id="PRO_0000161298" FT ACT_SITE 189 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT ACT_SITE 319 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 99..101 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 130..133 FT /ligand="substrate" FT /note="in site B" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 140..142 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 188 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 320 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 325..327 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT SITE 332 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" SQ SEQUENCE 461 AA; 50624 MW; D696F9A39BF50149 CRC64; MTKNFRFEKD SMGQIKVPSE ALWGAQTQRS IINFSIGEEL IPIELIYSLT VIKRAAAISN FKLGLINNVK KDLIIEACTE ILDGKHDSQF PLKIWQTGSG TQTNMNINEV ISNIAALKTN SGLGSHHPIH PNDDVNKSQS TNDTFPAAIQ ISVVTQIIKK LVPSIKELTK VLDSKSNKWK DLIKIGRTHF QDAVPISLGQ EVSAWSKQLK DAEDALIISL NELCFLPLGG TAVGTGINCP KDFSKESIKS ISEYTGLFFY KSKNHFSLMA SHDRLAQVMG QIKILASALF KISNDIKILS SGPRSGIYEL IIPKNEPGSS IMPGKVNPTQ CEALSMVCTQ VMGFEYAVSI ANASGTLQMN EYKPLIGFNI LTSIKLLNHA ISNFRLKLVE GIQPNPKTIK ANLENSLMLV TALVPKIGYE KAAEIANLAF NESINLKEAT IKLGYLTANE FEDAINTNKM I //