ID W5W6J1_9PSEU Unreviewed; 228 AA.
AC W5W6J1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=KALB_427 {ECO:0000313|EMBL:AHH93804.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH93804.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHH93804.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH93804.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
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}.
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DR EMBL; CP007155; AHH93804.1; -; Genomic_DNA.
DR RefSeq; WP_025354082.1; NZ_CP007155.1.
DR AlphaFoldDB; W5W6J1; -.
DR STRING; 1449976.KALB_427; -.
DR KEGG; kal:KALB_427; -.
DR PATRIC; fig|1449976.3.peg.433; -.
DR eggNOG; COG1211; Bacteria.
DR HOGENOM; CLU_061281_1_1_11; -.
DR OrthoDB; 9802561at2; -.
DR UniPathway; UPA00056; UER00093.
DR Proteomes; UP000019225; 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 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:UP000019225};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00108}.
FT SITE 15
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT SITE 22
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT SITE 156
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT SITE 208
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
SQ SEQUENCE 228 AA; 23371 MW; E709C6158BAFCA80 CRC64;
MSVVALVPAA GRGERLGAEL PKALVPVCGA PLLVHAVRGL LAAGCVQHVV VAAPAAHLDV
VTEALAVFAP AVHVVPGGGE RSDSVRLALD EAMTRVPDAS VVLVHDAARA FTPPEVVRAV
VDAVRAGSAA VIPVLPVADT VKQVDADGLV VATPDRSALR VVQTPQGFEP ALLRRAHEGA
TGATDDAGLV ERLGEPVHTV PGHPHAMKIT TPFDLVLAEA LFTKEAHE
//
