ID   FUMC_STAHJ              Reviewed;         461 AA.
AC   Q4L7F5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Fumarate hydratase class II;
DE            Short=Fumarase C;
DE            EC=4.2.1.2;
GN   Name=fumC; OrderedLocusNames=SH1111;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(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; AP006716; BAE04420.1; -; Genomic_DNA.
DR   RefSeq; YP_253026.1; -.
DR   GeneID; 3482341; -.
DR   GenomeReviews; AP006716_GR; SH1111.
DR   KEGG; sha:SH1111; -.
DR   NMPDR; fig|279808.3.peg.2090; -.
DR   HOGENOM; Q4L7F5; -.
DR   OMA; Q4L7F5; GSQGHFE.
DR   BioCyc; SHAE279808:SH1111-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    461       Fumarate hydratase class II.
FT                                /FTId=PRO_0000161319.
FT   REGION      127    130       B site (By similarity).
FT   REGION      137    139       Substrate binding (By similarity).
FT   BINDING      99     99       Substrate (By similarity).
SQ   SEQUENCE   461 AA;  51059 MW;  632E3F6C5B5A0ED8 CRC64;
     MSVRIEHDTF GEIEVPGDKY WGAQTERSKR NFPVGKERMP IEVVYGFAQL KRGAALANHE
     LGKLSDAKKD AIVYACDLIL KGELDEHFPL VVWQTGSGTQ SNMNVNEVVS FVANKYLKEQ
     GIDESIHPND DVNKSQSSND TFPTAMHVAL YHEVETKLEP ALKHLRDTFK EKEDKYQSII
     KIGRTHLQDA TPIKLGQEIS GWRYMLDKCE ELLAESKKHI LSLAIGGTAV GTGINAHPEF
     GNKVAKFISE NTGYNFVSSE NKFHALTSHD EVVQLHGTLK ALAADLMKIA NDIRWLASGP
     RAGLAEISIP ENEPGSSIMP GKVNPTQCEM LTMVAVQVMG NDTTVGIASS QGNFELNVFK
     PVILHNTLQS IYLLADGMQT FNDNCAVGIE PIEENINNYL NQSLMLVTAL NPHIGYEKAA
     QIAKKAHKEG LTLKESAIQS GHVTEEQFEE WIKPEDMVDP H
//