(data stored in ACNUC1104 zone)

SWISSPROT: ISPD_SACEN

ID   ISPD_SACEN              Reviewed;         224 AA.
AC   A4F6W3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108};
DE            EC=2.7.7.60 {ECO:0000255|HAMAP-Rule:MF_00108};
DE   AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000255|HAMAP-Rule:MF_00108};
DE   AltName: Full=MEP cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108};
DE            Short=MCT {ECO:0000255|HAMAP-Rule:MF_00108};
GN   Name=ispD {ECO:0000255|HAMAP-Rule:MF_00108};
GN   OrderedLocusNames=SACE_0439;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
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). {ECO:0000255|HAMAP-Rule:MF_00108}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-
CC         2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00108};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 2/6. {ECO:0000255|HAMAP-
CC       Rule:MF_00108}.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family.
CC       IspD subfamily. {ECO:0000255|HAMAP-Rule:MF_00108}.
DR   EMBL; AM420293; CAL99787.1; -; Genomic_DNA.
DR   RefSeq; WP_009947447.1; NZ_PDBV01000001.1.
DR   SMR; A4F6W3; -.
DR   STRING; 405948.SACE_0439; -.
DR   EnsemblBacteria; CAL99787; CAL99787; SACE_0439.
DR   KEGG; sen:SACE_0439; -.
DR   eggNOG; ENOG4105CE5; Bacteria.
DR   eggNOG; COG1211; LUCA.
DR   HOGENOM; HOG000218563; -.
DR   KO; K00991; -.
DR   OMA; ERQHSVY; -.
DR   OrthoDB; 1836139at2; -.
DR   BioCyc; SERY405948:SACE_RS02160-MONOMER; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000006728; Chromosome.
DR   GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02516; CDP-ME_synthetase; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_00108; IspD; 1.
DR   InterPro; IPR001228; IspD.
DR   InterPro; IPR034683; IspD/TarI.
DR   InterPro; IPR018294; ISPD_synthase_CS.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01128; IspD; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR00453; ispD; 1.
DR   PROSITE; PS01295; ISPD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F6W3.
DR   SWISS-2DPAGE; A4F6W3.
KW   Complete proteome; Isoprene biosynthesis; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN         1    224       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT                                /FTId=PRO_1000094341.
FT   SITE         15     15       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00108}.
FT   SITE         22     22       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00108}.
FT   SITE        156    156       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000255|HAMAP-
FT                                Rule:MF_00108}.
FT   SITE        209    209       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000255|HAMAP-
FT                                Rule:MF_00108}.
SQ   SEQUENCE   224 AA;  23083 MW;  35438C16643D1BE4 CRC64;
     MSVVALVPAA GRGVRLGAGV PKALVPVAGE SLLSRAVRGL HDSGRVRHVV VAAPADEVPA
     VEAELASLRS FVHVVPGGAE RTDSVRLALA EAERVVPDAR VVLVHDAARA FTPPSVVRDV
     VRAVEEGAPA VVPVLPVADT IKQVDEAGDV ETTVDRSRLR TVQTPQGFAI DVLRQAYAAA
     GDIATDDAGL VERIGGKVST VPGHPHALKI TTAFDLAIAE AVLA
//

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