FUMC_WIGBR
ID FUMC_WIGBR Reviewed; 464 AA.
AC Q8D2L3;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=WIGBR3410;
OS Wigglesworthia glossinidia brevipalpis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Wigglesworthia.
OX NCBI_TaxID=36870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12219091; DOI=10.1038/ng986;
RA Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA Aksoy S.;
RT "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT Wigglesworthia glossinidia.";
RL Nat. Genet. 32:402-407(2002).
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; BA000021; BAC24487.1; -; Genomic_DNA.
DR RefSeq; WP_011070145.1; NC_004344.2.
DR AlphaFoldDB; Q8D2L3; -.
DR SMR; Q8D2L3; -.
DR STRING; 36870.25166297; -.
DR EnsemblBacteria; BAC24487; BAC24487; BAC24487.
DR KEGG; wbr:fumC; -.
DR eggNOG; COG0114; Bacteria.
DR HOGENOM; CLU_021594_4_1_6; -.
DR OMA; HDSMGEV; -.
DR OrthoDB; 734949at2; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000000562; 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_0000161328"
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; 51556 MW; E8EF50597D064AB1 CRC64;
MLINRIEKDT IGEVELPKKC LWGSQTQRSI YNFNISTEKM PYELIHALVQ IKLVAAKVNK
DLKLLEEKKA DAIIKASEEI LSGKYKDSFP LVIWQTGSGT QTNMNVNEVI ANIAIKLLGG
KYGDYSIIHP NDHVNKSQSS NDVFPTAMHI SAVLSLKKNL LPNLIKLKKS FYDKSILFKD
IIKIGRTHLQ DATPLTLGQE VSSWYCMLKK NIKYIKNSIL CISEIALGGT AVGTGLNAHE
KYSLKASKLL SEINKHNFIS STNKFESLST CDAIVKVHST LKNLSISIMK ISNDIRWLSS
GPRCGIGELI IPENEPGSSI MPGKVNPTQC ESISMICCQV IGNDSAIGIG GLSGNFQLNV
FRPMIIYNFL QSVRILSDGI KSFNKKCVIG IKPNIKRIKK FLKESLMLVT SLTPHIGYDK
SAKIAKLAHN ENITLKEACL KLNYISESQF DILVRPENMI GNKN
