ISPD_AQUAE
ID ISPD_AQUAE Reviewed; 213 AA.
AC O67343;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase;
DE EC=2.7.7.60;
DE AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase;
DE AltName: Full=MEP cytidylyltransferase;
DE Short=MCT;
GN Name=ispD; OrderedLocusNames=aq_1323;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-
CC erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-
CC 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 -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 2/6.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000305}.
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DR EMBL; AE000657; AAC07307.1; -; Genomic_DNA.
DR PIR; D70414; D70414.
DR RefSeq; NP_213907.1; NC_000918.1.
DR RefSeq; WP_010880845.1; NC_000918.1.
DR AlphaFoldDB; O67343; -.
DR SMR; O67343; -.
DR STRING; 224324.aq_1323; -.
DR EnsemblBacteria; AAC07307; AAC07307; aq_1323.
DR KEGG; aae:aq_1323; -.
DR PATRIC; fig|224324.8.peg.1031; -.
DR eggNOG; COG1211; Bacteria.
DR HOGENOM; CLU_061281_2_2_0; -.
DR InParanoid; O67343; -.
DR OMA; ERQHSVY; -.
DR OrthoDB; 1836139at2; -.
DR UniPathway; UPA00056; UER00093.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IBA:GO_Central.
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;
KW Isoprene biosynthesis; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..213
FT /note="2-C-methyl-D-erythritol 4-phosphate
FT cytidylyltransferase"
FT /id="PRO_0000075545"
FT SITE 14
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 19
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 138
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000250"
FT SITE 194
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000250"
SQ SEQUENCE 213 AA; 23819 MW; BE4AF0AD573D0AA9 CRC64;
MYTAIILAAG RGSRIGFRKQ FATLCGKPLF MHSLEKVLDI FEEVILVLPE DFLDKVKVHP
KVKKVAGGPE RQDSVFNALL QATGDIVVIH DSARPLATKK MFLEVAQLGD YHGKVVASPA
RDTLKEVVEG KVIKTLNRSL IWHAQTPQAF RRDILLECHM RAKAEGFVGT DDASLLERYG
YSVGVVEGSY WNVKITYPED LEMVKKIMGC EED
