ID FUMC_STAS1 Reviewed; 461 AA. AC Q49YP8; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, 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=SSP0944; OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM OS 20229 / NCIMB 8711 / NCTC 7292 / S-41). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=342451; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41; RX PubMed=16135568; DOI=10.1073/pnas.0502950102; RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.; RT "Whole genome sequence of Staphylococcus saprophyticus reveals the RT pathogenesis of uncomplicated urinary tract infection."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005). 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; AP008934; BAE18089.1; -; Genomic_DNA. DR RefSeq; WP_011302807.1; NZ_MTGA01000033.1. DR AlphaFoldDB; Q49YP8; -. DR SMR; Q49YP8; -. DR KEGG; ssp:SSP0944; -. DR PATRIC; fig|342451.11.peg.943; -. DR eggNOG; COG0114; Bacteria. DR HOGENOM; CLU_021594_4_1_9; -. DR OrthoDB; 9802809at2; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000006371; 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 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; Lyase; Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1..461 FT /note="Fumarate hydratase class II" FT /id="PRO_0000161320" FT ACT_SITE 186 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT ACT_SITE 316 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 97..99 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 127..130 FT /ligand="substrate" FT /note="in site B" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 137..139 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 185 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 317 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 322..324 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT SITE 329 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" SQ SEQUENCE 461 AA; 50956 MW; BFFD5A5151E46EAE CRC64; MSVRIEHDTF GEIEVPADKY WGAQTERSKR NFPVGKERMP IEVVYGFAQL KRGAALANHA LGKLSDAKKD AIVYACDRVL NKELDEHFPL VVWQTGSGTQ SNMNVNEVVS YVANTYLKEQ GIDESIHPND DVNKSQSSND TFPTAMHVAL YNEVETKLEP ALKTLRDTFK QKEEQYHDII KIGRTHLQDA TPIRLGQEIS GWRYMLDKCE TLLSESKAHI LNLAIGGTAV GTGINAHPEF GDKVAKFIAE NTGYPFVSSE NKFHALTAHD EVVQLHGTLK ALATDLMKIA NDVRWLASGP RAGLAEISIP ENEPGSSIMP GKVNPTQCEM LTMVAVQVMG NDTAVGIASS QGNFELNVYK PVILLNTLQS IYLLADGMDT FNNNCAVGIE PIPENIDNYL NQSLMLVTAL NPHIGYEKAA SIAKKAHREG LTLKESAIDS GYVTEEQFEQ WIKPEDMVEP K //