(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BHP0_GEOS0

ID   A0A0F6BHP0_GEOS0        Unreviewed;       228 AA.
AC   A0A0F6BHP0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 26.
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=GY4MC1_0085 {ECO:0000313|EMBL:ADP72941.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72941.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72941.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72941.1,
RC   ECO:0000313|Proteomes:UP000002034};
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., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002293; ADP72941.1; -; Genomic_DNA.
DR   RefSeq; WP_013399824.1; NC_014650.1.
DR   EnsemblBacteria; ADP72941; ADP72941; GY4MC1_0085.
DR   KEGG; gmc:GY4MC1_0085; -.
DR   KO; K00991; -.
DR   OMA; ERQHSVY; -.
DR   OrthoDB; 1836139at2; -.
DR   BioCyc; GSP581103:G1GOQ-112-MONOMER; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000002034; 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; A0A0F6BHP0.
DR   SWISS-2DPAGE; A0A0F6BHP0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
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:ADP72941.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00108,
KW   ECO:0000256|SAAS:SAAS00981527, ECO:0000313|EMBL:ADP72941.1}.
FT   SITE         15     15       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00108}.
FT   SITE         22     22       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        208    208       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000256|HAMAP-Rule:
FT                                MF_00108}.
SQ   SEQUENCE   228 AA;  25644 MW;  E0C4D990B676A497 CRC64;
     MMYEVVIPAA GQGKRMKAGM NKQLIELRNE PLIVRTLKVF ENDEWCRGII VVINEAERTQ
     FEQLFSRFHI KKITAVVGGG KERQHSVYNG LRAVKNSDIV LIHDGARPFV TIEQIHELVN
     EAKEHGAAIP AVRVKDTIKK VCDQFVEETV ERSGLWAVQT PQAFHVSLVL RAHEQAQKDG
     YIGTDDASLV ERIGGKVKII EGDYRNIKLT TPDDLLFAEV ILSSWVSS
//

If you have problems or comments...

PBIL Back to PBIL home page