ISPD_THET8
ID ISPD_THET8 Reviewed; 213 AA.
AC Q5SLX2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108};
DE EC=2.7.7.60 {ECO:0000255|HAMAP-Rule:MF_00108};
DE AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000255|HAMAP-Rule:MF_00108};
DE AltName: Full=MEP cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108};
DE Short=MCT {ECO:0000255|HAMAP-Rule:MF_00108};
GN Name=ispD {ECO:0000255|HAMAP-Rule:MF_00108}; OrderedLocusNames=TTHA0171;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RG Southeast collaboratory for structural genomics (SECSG);
RT "Crystal structure of 2-C-methyl-D-erythritol 4-phosphate
RT cytidylyltransferase from Thermus thermophilus HB8.";
RL Submitted (JUN-2007) to the PDB data bank.
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:0000255|HAMAP-Rule:MF_00108}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00108};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 2/6. {ECO:0000255|HAMAP-Rule:MF_00108}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00108}.
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; AP008226; BAD69994.1; -; Genomic_DNA.
DR RefSeq; WP_011174170.1; NC_006461.1.
DR RefSeq; YP_143437.1; NC_006461.1.
DR PDB; 2PX7; X-ray; 2.20 A; A/B=1-213.
DR PDBsum; 2PX7; -.
DR AlphaFoldDB; Q5SLX2; -.
DR SMR; Q5SLX2; -.
DR STRING; 300852.55771553; -.
DR EnsemblBacteria; BAD69994; BAD69994; BAD69994.
DR GeneID; 3169663; -.
DR KEGG; ttj:TTHA0171; -.
DR PATRIC; fig|300852.9.peg.169; -.
DR eggNOG; COG1211; Bacteria.
DR HOGENOM; CLU_061281_2_2_0; -.
DR OMA; ERQHSVY; -.
DR PhylomeDB; Q5SLX2; -.
DR UniPathway; UPA00056; UER00093.
DR EvolutionaryTrace; Q5SLX2; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; Isoprene biosynthesis; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..213
FT /note="2-C-methyl-D-erythritol 4-phosphate
FT cytidylyltransferase"
FT /id="PRO_0000075640"
FT SITE 15
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 21
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 138
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 194
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:2PX7"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2PX7"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:2PX7"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:2PX7"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2PX7"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:2PX7"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2PX7"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:2PX7"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:2PX7"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:2PX7"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:2PX7"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2PX7"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2PX7"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:2PX7"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2PX7"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2PX7"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:2PX7"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:2PX7"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:2PX7"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:2PX7"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:2PX7"
SQ SEQUENCE 213 AA; 22423 MW; 1CA594359920EF7A CRC64;
MEVSVLIPAA GNGLRLGRGP KAFLQVGGRT LLEWTLAAFR DAAEVLVALP PGAEPPKGLG
AVFLEGGATR QASVARLLEA ASLPLVLVHD VARPFVSRGL VARVLEAAQR SGAAVPVLPV
PDTLMAPEGE AYGRVVPREA FRLVQTPQGF FTALLREAHA YARRKGLEAS DDAQLVQALG
YPVALVEGEA TAFKITHPQD LVLAEALARV WSA
