(data stored in SCRATCH zone)

SWISSPROT: E3J8M3_FRAIE

ID   E3J8M3_FRAIE            Unreviewed;       235 AA.
AC   E3J8M3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAY-2019, entry version 57.
DE   RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_00108};
DE            EC=2.7.7.60 {ECO:0000256|HAMAP-Rule:MF_00108};
DE   AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000256|HAMAP-Rule:MF_00108};
DE   AltName: Full=MEP cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_00108};
DE            Short=MCT {ECO:0000256|HAMAP-Rule:MF_00108};
GN   Name=ispD {ECO:0000256|HAMAP-Rule:MF_00108};
GN   OrderedLocusNames=FraEuI1c_0380 {ECO:0000313|EMBL:ADP78466.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78466.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78466.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00108,
CC       ECO:0000256|SAAS:SAAS00786778}.
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:0000256|HAMAP-Rule:MF_00108,
CC         ECO:0000256|SAAS:SAAS01130198};
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:0000256|HAMAP-
CC       Rule:MF_00108, ECO:0000256|SAAS:SAAS01130190}.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family.
CC       IspD subfamily. {ECO:0000256|HAMAP-Rule:MF_00108,
CC       ECO:0000256|SAAS:SAAS00888088}.
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DR   EMBL; CP002299; ADP78466.1; -; Genomic_DNA.
DR   RefSeq; WP_013421588.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0380; -.
DR   EnsemblBacteria; ADP78466; ADP78466; FraEuI1c_0380.
DR   KEGG; fri:FraEuI1c_0380; -.
DR   eggNOG; ENOG4105CE5; Bacteria.
DR   eggNOG; COG1211; LUCA.
DR   HOGENOM; HOG000218563; -.
DR   KO; K00991; -.
DR   OMA; ERQHSVY; -.
DR   OrthoDB; 1836139at2; -.
DR   BioCyc; FSP298654:G1GOT-381-MONOMER; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000002484; 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; E3J8M3.
DR   SWISS-2DPAGE; E3J8M3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00108,
KW   ECO:0000256|SAAS:SAAS01130196};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00108,
KW   ECO:0000256|SAAS:SAAS00981526, ECO:0000313|EMBL:ADP78466.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00108,
KW   ECO:0000256|SAAS:SAAS00981527, ECO:0000313|EMBL:ADP78466.1}.
FT   SITE         20     20       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00108}.
FT   SITE         27     27       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00108}.
FT   SITE        155    155       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000256|HAMAP-Rule:
FT                                MF_00108}.
FT   SITE        210    210       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000256|HAMAP-Rule:
FT                                MF_00108}.
SQ   SEQUENCE   235 AA;  24232 MW;  617769354BD26711 CRC64;
     MTGPEARVAV VVPAAGRGER LGGGVPKALR PLGGRPMLVH AVQALAAADL VSQIVVAAPP
     TLVEVVSRLL GPDVRVLAGG AERVDSVRGA LRALDDDIRV VLVHDAARPL TPPSLVDAVA
     AAVLGGQPAV IPVLPVADTV KEVDAQGRVL RTPTRDGLRA VQTPQGFRRE VLEAAYANSD
     DGPAVTDDAG LVERLGVPVT TIPGAEEAFK VTRPIDLVFA EALLARRPLA ESGRS
//

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