ID A0A2M6VGL8_9BURK Unreviewed; 249 AA.
AC A0A2M6VGL8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ORFNames=B9Z42_03695 {ECO:0000313|EMBL:PIT77579.1};
OS Limnohabitans sp. B9-3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1100707 {ECO:0000313|EMBL:PIT77579.1, ECO:0000313|Proteomes:UP000228506};
RN [1] {ECO:0000313|EMBL:PIT77579.1, ECO:0000313|Proteomes:UP000228506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B9-3 {ECO:0000313|EMBL:PIT77579.1,
RC ECO:0000313|Proteomes:UP000228506};
RA Kasalicky V., Mehrshad M., Andrei S.-A., Salcher M., Kratochvilova H.,
RA Simek K., Ghai R.;
RT "Unexpected and diverse lifestyles within the genus Limnohabitans.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002459, ECO:0000256|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:0000256|ARBA:ARBA00001282, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00004787, ECO:0000256|HAMAP-
CC Rule:MF_00108}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000256|ARBA:ARBA00009789, ECO:0000256|HAMAP-
CC Rule:MF_00108}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIT77579.1}.
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; NESI01000002; PIT77579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M6VGL8; -.
DR OrthoDB; 9806837at2; -.
DR UniPathway; UPA00056; UER00093.
DR Proteomes; UP000228506; Unassembled WGS sequence.
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 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 NCBIfam; TIGR00453; ispD; 1.
DR PANTHER; PTHR32125; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR32125:SF4; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR Pfam; PF01128; IspD; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS01295; ISPD; 1.
PE 3: Inferred from homology;
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW Rule:MF_00108};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00108}; Reference proteome {ECO:0000313|Proteomes:UP000228506};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00108}.
FT SITE 34
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT SITE 41
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT SITE 176
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT SITE 229
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
SQ SEQUENCE 249 AA; 26555 MW; F6952EB21D1200E9 CRC64;
MGARFNPSVW SMSLINSTPA RFHVLIPCAG SGSRAGTPQP KQYQIVAGLP MVVHTLRAFG
AVPRLACGLV VVSPNDLLMA GTLEAYPQPA FEVVRVGGAT RAQSVLAGLH ALRERGAQQH
DWVLVHDAAR CLVTPAQINA LMDACQDDAV GGLLAHQLAD TLKAAQSGRA ASTVDRSDKW
LAQTPQMFRL GMLTQALEQA GDAVTDESSA LEAMGLQPRL VQASAQNFKV TYAEDFALAE
AILKIRFEE
//