ID   FUMC_STAS1              Reviewed;         461 AA.
AC   Q49YP8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-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=SSP0944;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18089.1; -; Genomic_DNA.
DR   RefSeq; YP_301034.1; -.
DR   GeneID; 3616126; -.
DR   GenomeReviews; AP008934_GR; SSP0944.
DR   KEGG; ssp:SSP0944; -.
DR   NMPDR; fig|342451.4.peg.937; -.
DR   HOGENOM; Q49YP8; -.
DR   OMA; Q49YP8; GSQGHFE.
DR   BioCyc; SSAP342451:SSP0944-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_0000161320.
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;  50956 MW;  BFFD5A5151E46EAE CRC64;
     MSVRIEHDTF GEIEVPADKY WGAQTERSKR NFPVGKERMP IEVVYGFAQL KRGAALANHA
     LGKLSDAKKD AIVYACDRVL NKELDEHFPL VVWQTGSGTQ SNMNVNEVVS YVANTYLKEQ
     GIDESIHPND DVNKSQSSND TFPTAMHVAL YNEVETKLEP ALKTLRDTFK QKEEQYHDII
     KIGRTHLQDA TPIRLGQEIS GWRYMLDKCE TLLSESKAHI LNLAIGGTAV GTGINAHPEF
     GDKVAKFIAE NTGYPFVSSE NKFHALTAHD EVVQLHGTLK ALATDLMKIA NDVRWLASGP
     RAGLAEISIP ENEPGSSIMP GKVNPTQCEM LTMVAVQVMG NDTAVGIASS QGNFELNVYK
     PVILLNTLQS IYLLADGMDT FNNNCAVGIE PIPENIDNYL NQSLMLVTAL NPHIGYEKAA
     SIAKKAHREG LTLKESAIDS GYVTEEQFEQ WIKPEDMVEP K
//