ID   FUMC_RICBR              Reviewed;         463 AA.
AC   Q1RHL6;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Fumarate hydratase class II;
DE            Short=Fumarase C;
DE            EC=4.2.1.2;
GN   Name=fumC; OrderedLocusNames=RBE_1067;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae
RT   in gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
CC   -!- CATALYTIC ACTIVITY: (S)-malate = fumarate + H(2)O.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: There are 2 substrate binding sites: the catalytic
CC       A site, and the non-catalytic B site that may play a role in the
CC       transfer of substrate or product between the active site and the
CC       solvent. Alternatively, the B site may bind allosteric effectors
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       Fumarase subfamily.
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DR   EMBL; CP000087; ABE05148.1; -; Genomic_DNA.
DR   RefSeq; YP_538237.1; -.
DR   GeneID; 3995904; -.
DR   GenomeReviews; CP000087_GR; RBE_1067.
DR   KEGG; rbe:RBE_1067; -.
DR   HOGENOM; Q1RHL6; -.
DR   OMA; Q1RHL6; DATPITF.
DR   BioCyc; RBEL336407:RBE_1067-MON; -.
DR   GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR   GO; GO:0004333; F:fumarate hydratase activity; IEA:HAMAP.
DR   GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP.
DR   HAMAP; MF_00743; -; 1.
DR   InterPro; IPR003031; D_crystallin.
DR   InterPro; IPR005677; Fum_hydII.
DR   InterPro; IPR018951; Fumarase_C_C.
DR   InterPro; IPR000362; Fumarate_lyase.
DR   Pfam; PF10415; FumaraseC_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; DCRYSTALLIN.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   TIGRFAMs; TIGR00979; fumC_II; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Lyase; Tricarboxylic acid cycle.
FT   CHAIN         1    463       Fumarate hydratase class II.
FT                                /FTId=PRO_0000277938.
FT   REGION      129    132       B site (By similarity).
FT   REGION      139    141       Substrate binding (By similarity).
FT   BINDING     100    100       Substrate (By similarity).
SQ   SEQUENCE   463 AA;  50903 MW;  13988722F6B3A0BC CRC64;
     MTNYRTESDS FGEIQIEDKF YWGAQTQRSL ENFKIGKQRM PEILIRSLAI LKKCAAKVNL
     EFGDLEPKIA ESIDKATSRI LNAEFSDNFP LVVWQTGSGT QTNMNMNEVI ASIANEELTG
     MKGGKSPVHP NDHVNKGQSS NDSFPTAMHI ATVLATREKL IPALNNLLTA LQNKSKDWDS
     IIKIGRTHLQ DATPLTLKQE FSGYITQIEY ALERIEDALK KVYLLAQGGT AVGTGINSRK
     GFDIKFAEEV AEFTKQPFKT APNKFESLAA HDALVEFSGT LNTIAVSLMK IANDIRLLGS
     GPRCGLGELH LPENEPGSSI MPGKVNPTQV EALTMVCTQV MGNHVTVTIA GSNGHLELNV
     FKPVIIYNIL QSIELLSDAA NSFVTHCVDG IEPNITHIND LRDKSLMLVT ALNPHIGYDN
     AAKIAKEAHK HGITLKEAAK KLNLLSEEEF NKIVVPEKMV RQS
//