(data stored in SCRATCH zone)

SWISSPROT: A8LF84_FRASN

ID   A8LF84_FRASN            Unreviewed;       229 AA.
AC   A8LF84;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 83.
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=Franean1_0363 {ECO:0000313|EMBL:ABW09829.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09829.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(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: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; CP000820; ABW09829.1; -; Genomic_DNA.
DR   RefSeq; WP_012157805.1; NC_009921.1.
DR   STRING; 298653.Franean1_0363; -.
DR   EnsemblBacteria; ABW09829; ABW09829; Franean1_0363.
DR   KEGG; fre:Franean1_0363; -.
DR   eggNOG; ENOG4105CE5; Bacteria.
DR   eggNOG; COG1211; LUCA.
DR   HOGENOM; HOG000218563; -.
DR   KO; K00991; -.
DR   OMA; ERQHSVY; -.
DR   OrthoDB; 1836139at2; -.
DR   BioCyc; FSP298653:G1G9X-360-MONOMER; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000001313; 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; A8LF84.
DR   SWISS-2DPAGE; A8LF84.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001313};
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:ABW09829.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001313};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00108,
KW   ECO:0000256|SAAS:SAAS00981527, ECO:0000313|EMBL:ABW09829.1}.
FT   SITE         17     17       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00108}.
FT   SITE         24     24       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00108}.
FT   SITE        152    152       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000256|HAMAP-Rule:
FT                                MF_00108}.
FT   SITE        205    205       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000256|HAMAP-Rule:
FT                                MF_00108}.
SQ   SEQUENCE   229 AA;  23777 MW;  779E39DB266B2E52 CRC64;
     MSTRVGALVP AAGRGERLGG GTPKALRPLG GRPMLLRAVE TLLSSTLVSQ VVVAAPPTLV
     EVVGQILGPR VRVVPGGAER VDSVRAALEA LDDDIGVVLV HDAARPLTPA KLVDAVATTV
     LDGHPAVIPV LPVTDTVKEV DADGRVVRTP PRDVLRAVQT PQGFRRDILH TAYANRDLPV
     TDDAGLVEAL GVPVTTIPGA EEAFKVTRPA DLVLAEALLA QFAPGDGQR
//

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