FUMC_PASMU
ID FUMC_PASMU Reviewed; 464 AA.
AC Q9CMK1;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
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}; OrderedLocusNames=PM0823;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
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DR EMBL; AE004439; AAK02907.1; -; Genomic_DNA.
DR RefSeq; WP_005722516.1; NC_002663.1.
DR AlphaFoldDB; Q9CMK1; -.
DR SMR; Q9CMK1; -.
DR STRING; 747.DR93_1663; -.
DR EnsemblBacteria; AAK02907; AAK02907; PM0823.
DR GeneID; 62226360; -.
DR KEGG; pmu:PM0823; -.
DR HOGENOM; CLU_021594_4_1_6; -.
DR OMA; HDSMGEV; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000000809; 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; 1.10.275.10; -; 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 Cytoplasm; Lyase; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..464
FT /note="Fumarate hydratase class II"
FT /id="PRO_0000161294"
FT ACT_SITE 188
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT ACT_SITE 318
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 98..100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 129..132
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 139..141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 324..326
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT SITE 331
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
SQ SEQUENCE 464 AA; 50419 MW; 0814F76FB379F1A1 CRC64;
MTFRIEKDTM GEVQVPADKY WAAQTERSRN NFKIGPEASM PKEIIEAFGY LKKAAAYANH
DLGVLPVEKR DLIAQACDEI LANKLDDQFP LVIWQTGSGT QSNMNLNEVI SNRAHVLNGG
KLGEKSIIHP NDDVNKSQSS NDTYPTAMHI AAYKKVVEVT IPCVERLQKT LAQKADAFKD
VVKIGRTHLM DATPLTLGQE FSAYAAQLDF GLRALKNTLP HLAQLALGGT AVGTGLNTPK
GYDVKVADYI AKFTGLPFIT AENKFEALAT HDAVVETHGA LKQLAVSLYK IANDIRLLAS
GPRSGIGEIL IPENEPGSSI MPGKVNPTQC EAMTMVCAQV LGNDTTISFA GTQGHFQLNV
FKPVMAANFL QSAQLLADAC VSFDEHCAVG IEPNFPRIKK QLDDSLMLVT ALNTHIGYEN
AAKIAKTAHK NGTTLKEEAI NLGLVTAEQF DEWVRPEDMV GSLK
