ID   FUMC_RICFE              Reviewed;         461 AA.
AC   Q4UMT4;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Fumarate hydratase class II;
DE            Short=Fumarase C;
DE            EC=4.2.1.2;
GN   Name=fumC; OrderedLocusNames=RF_0273;
OS   Rickettsia felis (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=42862;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61124.1; -; Genomic_DNA.
DR   RefSeq; YP_246289.1; -.
DR   GeneID; 3400680; -.
DR   GenomeReviews; CP000053_GR; RF_0273.
DR   KEGG; rfe:RF_0273; -.
DR   NMPDR; fig|315456.3.peg.107; -.
DR   HOGENOM; Q4UMT4; -.
DR   OMA; Q4UMT4; GSQGHFE.
DR   BioCyc; RFEL315456:RF_0273-MON; -.
DR   BRENDA; 4.2.1.2; 297363.
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    461       Fumarate hydratase class II.
FT                                /FTId=PRO_0000277939.
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   461 AA;  50726 MW;  E729AF53989939A0 CRC64;
     MKNYRTESDS FGEIQIEEKF YWGAQTQRSL ENFKIGKQKM PEILIRALAI LKKCAAQVNY
     EFGDLEAKIA TSIDKATDRI LEGEFEDNFP LVVWQTGSGT QTNMNMNEVI ASIANEELTS
     KKGGKSPVHP NDHVNKGQSS NDSFPTAMHI ATVLATKQQL IPALNNLLTS LQDKSKDWDK
     IIKIGRTHLQ DATPLTLKQE FSGYITQIEY ALERIEDALK KVYLLAQGGT AVGTAINSKI
     GFDIKFAEKV AEFTKQPFKT APNKFESLAA HDALVEFSGT LNTIAVSLMK IANDIRLLGS
     GPRCGLGELH LPENEPGSSI MPGKVNPTQV EALTMVCSQV MGNHVTVTIA GSNGHLELNV
     FKPVIIYNIL QSIELLSDSV NSFVTHCVKG LEPNIARIND LRDKSLMLVT ALNPHIGYDN
     AAKIAKEAHK HGITLKEAAK KLNLLSEEEF DKIVVPEKMI G
//