ID   FUMC_COXBU              Reviewed;         459 AA.
AC   Q83CL8;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 2.
DT   16-JUN-2009, entry version 41.
DE   RecName: Full=Fumarate hydratase class II;
DE            Short=Fumarase C;
DE            EC=4.2.1.2;
GN   Name=fumC; OrderedLocusNames=CBU_1096;
OS   Coxiella burnetii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Coxiellaceae; Coxiella.
OX   NCBI_TaxID=777;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nine Mile phase I / RSA 493;
RX   MEDLINE=22608657; PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E.,
RA   Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J.,
RA   DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J.,
RA   Khouri H.M., Lee K.H., Carty H.A., Scanlan D., Heinzen R.A.,
RA   Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella
RT   burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO90609.2; -; Genomic_DNA.
DR   RefSeq; NP_820095.2; -.
DR   HSSP; P05042; 1FUR.
DR   GeneID; 1208998; -.
DR   GenomeReviews; AE016828_GR; CBU_1096.
DR   KEGG; cbu:CBU_1096; -.
DR   NMPDR; fig|227377.1.peg.1039; -.
DR   TIGR; CBU_1096; -.
DR   HOGENOM; Q83CL8; -.
DR   BioCyc; CBUR227377:CBU_1096-MON; -.
DR   BRENDA; 4.2.1.2; 256353.
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    459       Fumarate hydratase class II.
FT                                /FTId=PRO_0000161273.
FT   REGION      126    129       B site (By similarity).
FT   REGION      136    138       Substrate binding (By similarity).
FT   BINDING      97     97       Substrate (By similarity).
SQ   SEQUENCE   459 AA;  49850 MW;  15153802D24B2359 CRC64;
     MRKESDSMGT IEVPSEKYYG AQSQRSLINF AIGRETMPPE LIRAFGVLKK AAVLTNVELG
     KVSQEKANFI LKACEELIAG KLNDHFPLKI WQTGSGTQTN MNVNEVISNR AIELAGGKLG
     SKEPVHPNDH VNMSQSSNDT FPTAMHITAA EMITHQLIPN LTVLRDTLEK KSKEFSEIIK
     IGRTHLQDAV PLTLGQEFSG YVAQLNHNLE AINDVLPTLY RLALGGTAVG TGLNTHPQFA
     KKAADHIAEL TGIPFYSASN KFAALAANDE IVLVSGVLKT LACSLMKIAN DIRWLASGPR
     CGIGEIVIPE NEPGSSIMPG KVNPTQSEAM TMVCVQVIGN DTTITIAGSQ GNFELNVYKP
     VMAYNLIQSI YLLSDACRSF NDHCAVGIKP NQEKINDYLN NSLMLVTALN QIIGYDKASE
     IAKKAYKEGT TLKEAALQLG YLTASEFDKA VDPKKMVAI
//