ID B4RG74_PHEZH Unreviewed; 463 AA. AC B4RG74; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 18-JUN-2025, entry version 90. 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:ACG77198.1}; GN OrderedLocusNames=PHZ_c0784 {ECO:0000313|EMBL:ACG77198.1}; OS Phenylobacterium zucineum (strain HLK1). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Caulobacterales; Caulobacteraceae; Phenylobacterium. OX NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG77198.1, ECO:0000313|Proteomes:UP000001868}; RN [1] {ECO:0000313|EMBL:ACG77198.1, ECO:0000313|Proteomes:UP000001868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLK1 {ECO:0000313|EMBL:ACG77198.1, RC ECO:0000313|Proteomes:UP000001868}; RX PubMed=18700039; DOI=10.1186/1471-2164-9-386; RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.; RT "Complete genome of Phenylobacterium zucineum - a novel facultative RT intracellular bacterium isolated from human erythroleukemia cell line RT K562."; RL BMC Genomics 9:386-386(2008). 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; CP000747; ACG77198.1; -; Genomic_DNA. DR RefSeq; WP_012521346.1; NC_011144.1. DR AlphaFoldDB; B4RG74; -. DR STRING; 450851.PHZ_c0784; -. DR KEGG; pzu:PHZ_c0784; -. DR eggNOG; COG0114; Bacteria. DR HOGENOM; CLU_021594_4_1_5; -. DR OrthoDB; 9802809at2; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000001868; 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:UP000001868}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP- KW Rule:MF_00743}. FT DOMAIN 12..342 FT /note="Fumarate lyase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00206" FT DOMAIN 408..460 FT /note="Fumarase C C-terminal" FT /evidence="ECO:0000259|Pfam:PF10415" FT ACT_SITE 188 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT ACT_SITE 318 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 98..100 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 129..132 FT /ligand="substrate" FT /note="in site B" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 139..141 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 187 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 319 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT BINDING 324..326 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" FT SITE 331 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743" SQ SEQUENCE 463 AA; 49806 MW; 5A73A6AB80464391 CRC64; MTATRTETDT FGPIEVPSDR YWGAQTQRSI GNFRIGWEKQ PKPVIRALGV VKRAAAEANM ELGKLDPEIG KHIVAAAQEV IDGKLDDHFP LVVWQTGSGT QSNMNANEVI SNRAIEMMGG QMGSKKPVHP NDHVNMSQSS NDTYPTAMHI AAAEEVARSV MPALEHLHAA LKYKAEEFAH IIKIGRTHTQ DATPLTLGQE FGGYAHQVAM SVRRIKETLY GLYELAQGGT AVGTGLNAPV GFAELVAEKI AKITHLPFVT APNKFEALAA HDAMVFSHGA INTAAAALFK IANDIRFLGS GPRSGLGELA LPENEPGSSI MPGKVNPTQA EALTMVCAHI MGNQTAMTVA GSQGHFELNV FNPVMAYNFL QSCRLISDAA ISFTDNMVKG IEAREDNIKA NLERSLMLVT ALAPKIGYDN AAKIAKLAHK NGTTLREEAV GGGYVTNEEF DEVVRPEKMI SPG //