(data stored in SCRATCH zone)

SWISSPROT: A5GRS8_SYNR3

ID   A5GRS8_SYNR3            Unreviewed;       233 AA.
AC   A5GRS8;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 82.
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   ECO:0000313|EMBL:CAK27587.1};
GN   OrderedLocusNames=SynRCC307_0684 {ECO:0000313|EMBL:CAK27587.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27587.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK27587.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RA   Genoscope;
RL   Submitted (MAY-2006) 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; CT978603; CAK27587.1; -; Genomic_DNA.
DR   STRING; 316278.SynRCC307_0684; -.
DR   EnsemblBacteria; CAK27587; CAK27587; SynRCC307_0684.
DR   KEGG; syr:SynRCC307_0684; -.
DR   eggNOG; ENOG4105CE5; Bacteria.
DR   eggNOG; COG1211; LUCA.
DR   HOGENOM; HOG000218563; -.
DR   KO; K00991; -.
DR   OMA; ERQHSVY; -.
DR   BioCyc; SSP316278:G1GJL-676-MONOMER; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000001115; 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; A5GRS8.
DR   SWISS-2DPAGE; A5GRS8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
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:CAK27587.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00108,
KW   ECO:0000256|SAAS:SAAS00981527, ECO:0000313|EMBL:CAK27587.1}.
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        160    160       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000256|HAMAP-Rule:
FT                                MF_00108}.
FT   SITE        216    216       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000256|HAMAP-Rule:
FT                                MF_00108}.
SQ   SEQUENCE   233 AA;  24981 MW;  98D2726D5777F01D CRC64;
     MDLNRGRLHL LIVAAGSGRR MGAEGNKLLL PLQGRPLLAW TLESALASDA IAWLGVVGQA
     CDRQAIEALL QSLQPRQPWC WIQGGATRQQ SVACGLAALP AEAEHVLIHD GARCLAEPAL
     FDRCAEALQR NGQALIAATP VVDTIKQVDG QGRIVATPPR SELWAAQTPQ GFPVAQLHQA
     HQQAEQAGWE VTDDAALFER LGWPVQVLEA SSANLKITTP LDLELAAALL RAR
//

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