ID B6JB65_AFIC5 Unreviewed; 468 AA. AC B6JB65; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 28-JAN-2026, entry version 105. 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:AEI07392.1}; GN OrderedLocusNames=OCA5_c26980 {ECO:0000313|EMBL:AEI07392.1}; OS Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5) OS (Oligotropha carboxidovorans). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Nitrobacteraceae; Afipia. OX NCBI_TaxID=504832 {ECO:0000313|EMBL:AEI07392.1, ECO:0000313|Proteomes:UP000007730}; RN [1] {ECO:0000313|EMBL:AEI07392.1, ECO:0000313|Proteomes:UP000007730} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5 RC {ECO:0000313|Proteomes:UP000007730}; RX PubMed=21742883; DOI=10.1128/JB.05619-11; RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., RA Meyer O.; RT "Complete genome sequences of the chemolithoautotrophic Oligotropha RT carboxidovorans strains OM4 and OM5."; RL J. Bacteriol. 193:5043-5043(2011). 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 --------------------------------------------------------------------------- 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; CP002826; AEI07392.1; -; Genomic_DNA. DR RefSeq; WP_012562435.1; NC_011386.1. DR AlphaFoldDB; B6JB65; -. DR STRING; 504832.OCA5_c26980; -. DR KEGG; oca:OCAR_5274; -. DR KEGG; ocg:OCA5_c26980; -. DR PATRIC; fig|504832.7.peg.2852; -. DR eggNOG; COG0114; Bacteria. DR HOGENOM; CLU_021594_4_1_5; -. DR OrthoDB; 9802809at2; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000007730; Chromosome. 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 FunFam; 1.10.40.30:FF:000002; Fumarate hydratase class II; 1. DR FunFam; 1.10.275.10:FF:000001; Fumarate hydratase, mitochondrial; 1. DR FunFam; 1.20.200.10:FF:000001; Fumarate hydratase, mitochondrial; 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 NCBIfam; NF008909; PRK12273.1; 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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00743}; KW Reference proteome {ECO:0000313|Proteomes:UP000007730}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP- KW Rule:MF_00743}. FT DOMAIN 16..346 FT /note="Fumarate lyase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00206" FT DOMAIN 412..464 FT /note="Fumarase C C-terminal" FT /evidence="ECO:0000259|Pfam:PF10415" FT ACT_SITE 192 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT ACT_SITE 322 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 102..104 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 133..136 FT /ligand="substrate" FT /note="in site B" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 143..145 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 323 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 328..330 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT SITE 335 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" SQ SEQUENCE 468 AA; 50052 MW; EB47D0BBAC5FF57B CRC64; MAPTNKTTRT ETDTFGPIEV AADRYWGAQT ERSRNNFKIG TEHMPLPLIR AMAIVKLAAA KTNLDLKLID KKLADAIIAA AQEIIDGKLN DHFPLVVWQT GSGTQTNMNL NEVISNRANE MLGGERGTKK PVHPNDHVNM GQSSNDAFPT AMHIAAAEEI AHTLIPALEE LLAALRAKQK EFASIVKIGR THTQDATPLT LGQEFSGYAA QVESGIARIK ESAKSLNLLA QGGTAVGTGL NAKPGFAEGF AKHAAAITGL PFVTAPNKFE ALASNDSYVY VHGAINATAT GLFKIANDIR LLGSGPRSGL GELILPENEP GSSIMPGKVN PTQCEALTMV CCQIFGNQTT LTTAGSQGHF ELNVYKPVMV FAMLTSIRLM ADAARSFTQN CVIGIRADEK RIGDLMQRSL MLVTALAPKI GYDNAAKIAK TAHANGTTLK EEALRLGFVT AEEFDSIVRP EKMTSSSN //