ID A0A059G2T5_9PROT Unreviewed; 464 AA. AC A0A059G2T5; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 24-JUL-2024, entry version 40. DE RecName: Full=Fumarate hydratase class II {ECO:0000256|HAMAP-Rule:MF_00743}; DE Short=Fumarase C {ECO:0000256|HAMAP-Rule:MF_00743}; DE EC=4.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00743}; DE AltName: Full=Aerobic fumarase {ECO:0000256|HAMAP-Rule:MF_00743}; DE AltName: Full=Iron-independent fumarase {ECO:0000256|HAMAP-Rule:MF_00743}; GN Name=fumC {ECO:0000256|HAMAP-Rule:MF_00743, GN ECO:0000313|EMBL:KDA01034.1}; GN ORFNames=HOC_17531 {ECO:0000313|EMBL:KDA01034.1}; OS Hyphomonas oceanitis SCH89. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales; OC Hyphomonadaceae; Hyphomonas. OX NCBI_TaxID=1280953 {ECO:0000313|EMBL:KDA01034.1, ECO:0000313|Proteomes:UP000024942}; RN [1] {ECO:0000313|EMBL:KDA01034.1, ECO:0000313|Proteomes:UP000024942} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCH89 {ECO:0000313|EMBL:KDA01034.1, RC ECO:0000313|Proteomes:UP000024942}; RX PubMed=25070064; DOI=10.1007/s10482-014-0236-y; RA Li C., Lai Q., Li G., Dong C., Wang J., Liao Y., Shao Z.; RT "Hyphomonas beringensis sp. nov. and Hyphomonas chukchiensis sp. nov., RT isolated from surface seawater of the Bering Sea and Chukchi Sea."; RL Antonie Van Leeuwenhoek 106:657-665(2014). CC -!- FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific CC interconversion of fumarate to L-malate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00743}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate CC from fumarate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00743}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00743}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00743}. CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase CC subfamily. {ECO:0000256|ARBA:ARBA00009084, ECO:0000256|HAMAP- CC Rule:MF_00743}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KDA01034.1}. 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; ARYL01000038; KDA01034.1; -; Genomic_DNA. DR RefSeq; WP_035540977.1; NZ_ARYL01000038.1. DR AlphaFoldDB; A0A059G2T5; -. DR STRING; 1280953.HOC_17531; -. DR PATRIC; fig|1280953.3.peg.3508; -. DR eggNOG; COG0114; Bacteria. DR OrthoDB; 9802809at2; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000024942; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro. DR GO; GO:0006108; P:malate metabolic process; IEA:TreeGrafter. 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 {ECO:0000256|HAMAP-Rule:MF_00743}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00743, ECO:0000313|EMBL:KDA01034.1}; KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}. FT DOMAIN 14..344 FT /note="Fumarate lyase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00206" FT DOMAIN 410..461 FT /note="Fumarase C C-terminal" FT /evidence="ECO:0000259|Pfam:PF10415" FT ACT_SITE 190 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT ACT_SITE 320 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 100..102 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 131..134 FT /ligand="substrate" FT /note="in site B" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 141..143 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 189 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 321 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 326..328 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT SITE 333 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" SQ SEQUENCE 464 AA; 49611 MW; 0457ACADE5A7612C CRC64; MVNTPTRTET DTMGPVEVAN DRYWGAQAER SLGNFKIGWE KQPEPIVRAL GIVKKAAAQA NMDLGKMDPE LGKVIVQVAD EVIDGKLNDH FPLVVWQTGS GTQSNMNANE VISNRAIEIL GGEMGSKKPV HPNDHVNMSQ SSNDTFPTAM HIACAEEVTH RLVPALKHLH AALDAKAKAW VDIIKIGRTH TQDATPVTLG QEFSGYAQQV ENGIARIEST LPMLMQLAQG GTAVGTGLAS PVGFAEKVAE KIAGITGLKF TSAPNKFEAL AAHDAMVFTH GAINTVAMSC FKIANDIRFL GSGPRSGLGE LALPENEPGS SIMPGKVNPT QCEALTQVCA HIHGNNAAIG FAGSQGHFEL NVFNPMMAYN FLQSTRLLAD AAISFTDNCV VGIEPRLENI ATGLKNSLML VTPLKEKYGY DRAAKIAKTA HKNGTTLREE AIKDGIPGED FDNIVDPSKM ISPG //