ID A0A059G2T5_9RHOB Unreviewed; 464 AA. AC A0A059G2T5; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 21. 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; Proteobacteria; Alphaproteobacteria; Rhodobacterales; 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: (S)-malate = fumarate + H(2)O. CC {ECO:0000256|HAMAP-Rule:MF_00743}. CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)- CC malate 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 CC A site, and the non-catalytic B site that may play a role in the CC transfer of substrate or product between the active site and the CC solvent. 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. CC Fumarase subfamily. {ECO:0000256|HAMAP-Rule:MF_00743}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; KDA01034; KDA01034; HOC_17531. DR PATRIC; fig|1280953.3.peg.3508; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000024942; Unassembled WGS sequence. DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro. DR GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.275.10; -; 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; PTHR11444; 1. DR Pfam; PF10415; FumaraseC_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; SSF48557; 1. DR TIGRFAMs; TIGR00979; fumC_II; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000024942}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00743, ECO:0000256|SAAS:SAAS00674282, KW ECO:0000313|EMBL:KDA01034.1}; KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}. FT DOMAIN 14 344 Lyase_1. {ECO:0000259|Pfam:PF00206}. FT DOMAIN 410 461 FumaraseC_C. {ECO:0000259|Pfam:PF10415}. FT REGION 100 102 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00743}. FT REGION 131 134 Substrate binding (B site). FT {ECO:0000256|HAMAP-Rule:MF_00743}. FT REGION 141 143 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00743}. FT REGION 326 328 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00743}. FT ACT_SITE 190 190 Proton donor/acceptor. FT {ECO:0000256|HAMAP-Rule:MF_00743}. FT ACT_SITE 320 320 {ECO:0000256|HAMAP-Rule:MF_00743}. FT BINDING 189 189 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00743}. FT BINDING 321 321 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00743}. FT SITE 333 333 Important for catalytic activity. FT {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 //