ID   ISPD1_STAAS             Reviewed;         238 AA.
AC   Q6GCM3;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase 1;
DE            EC=2.7.7.60;
DE   AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase 1;
DE   AltName: Full=MEP cytidylyltransferase 1;
DE            Short=MCT 1;
GN   Name=ispD1; OrderedLocusNames=SAS0227;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-
CC       methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-
CC       phosphate (MEP) (By similarity).
CC   -!- CATALYTIC ACTIVITY: CTP + 2-C-methyl-D-erythritol 4-phosphate =
CC       diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl-PP biosynthesis via
CC       DXP pathway; isopentenyl-PP from 1-deoxy-D-xylulose 5-phosphate:
CC       step 2/6.
CC   -!- SIMILARITY: Belongs to the ispD family.
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DR   EMBL; BX571857; CAG41996.1; -; Genomic_DNA.
DR   RefSeq; YP_042350.1; -.
DR   GeneID; 2861974; -.
DR   GenomeReviews; BX571857_GR; SAS0227.
DR   KEGG; sas:SAS0227; -.
DR   HOGENOM; Q6GCM3; -.
DR   OMA; Q6GCM3; GELFNIK.
DR   BioCyc; SAUR282459:SAS0227-MON; -.
DR   GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidyl...; IEA:HAMAP.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00108; -; 1.
DR   InterPro; IPR001228; ISPD_synthase.
DR   InterPro; IPR018294; ISPD_synthase_CS.
DR   Pfam; PF01128; IspD; 1.
DR   PROSITE; PS01295; ISPD; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isoprene biosynthesis; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN         1    238       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase 1.
FT                                /FTId=PRO_0000075621.
FT   SITE         14     14       Transition state stabilizer (By
FT                                similarity).
FT   SITE         22     22       Transition state stabilizer (By
FT                                similarity).
FT   SITE        160    160       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        217    217       Positions MEP for the nucleophilic attack
FT                                (By similarity).
SQ   SEQUENCE   238 AA;  26627 MW;  F21440DA33D18AA7 CRC64;
     MIYAGILAGG IGSRMGNVPL PKQFLDIDNK PILIHTIEKF ILVSEFNEII IATPAQWISH
     TQDILKKYNI TDQRVKVVAG GTDRNETIMN IIDYIRNVNG INNDDVIVTH DAVRPFLTQR
     IIKENIEVAE KYGAVDTVIE AIDTIVMSKD KQNIHSIPVR NEMYQGQTPQ SFNIKLLQDS
     YRALSSAQKE ILSDACKIIV ESGHPVKLVR GELYNIKVTT PYDLKVANAI IQGDIADD
//