ID A0A120F9Q8_9ACTN Unreviewed; 504 AA.
AC A0A120F9Q8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=GA0070623_1802 {ECO:0000313|EMBL:SCG50341.1};
OS Micromonospora rifamycinica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=291594 {ECO:0000313|EMBL:SCG50341.1, ECO:0000313|Proteomes:UP000198226};
RN [1] {ECO:0000313|EMBL:SCG50341.1, ECO:0000313|Proteomes:UP000198226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44983 {ECO:0000313|EMBL:SCG50341.1,
RC ECO:0000313|Proteomes:UP000198226};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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|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|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:0000256|HAMAP-Rule:MF_00108}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00108}.
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DR EMBL; LT607752; SCG50341.1; -; Genomic_DNA.
DR RefSeq; WP_067303414.1; NZ_LT607752.1.
DR AlphaFoldDB; A0A120F9Q8; -.
DR OrthoDB; 9802561at2; -.
DR UniPathway; UPA00056; UER00093.
DR Proteomes; UP000198226; Chromosome i.
DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 CDD; cd05233; SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00108; IspD; 1.
DR InterPro; IPR012115; CDP-ribitol_syn.
DR InterPro; IPR001228; IspD.
DR InterPro; IPR034683; IspD/TarI.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
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; PF00106; adh_short; 1.
DR Pfam; PF01128; IspD; 1.
DR PIRSF; PIRSF036586; CDP-ribitol_syn; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00108};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00108};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00108}.
FT SITE 36
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT SITE 43
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT SITE 175
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT SITE 234
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
SQ SEQUENCE 504 AA; 53986 MW; 760C4187B04E3567 CRC64;
MTQDHTTGPD ATPETPAPWR PSRTVAVVLA GGTGTRLGLG IPKQLLKIAG KPIIEHTLAV
FEAAPEIDEI IVLMATGHVA DAQQIVDKAG FRKVSKVIEG GDTRNATTRI ALDAVGGGDV
NILFHDAVRP LVSARIVREC VNALWSYSAV DVAIPSADTI IQVDEDECIT DIPVRSRLRR
GQTPQAFRSG TIREAYRRAE GDPDFAATDD CGVVLRYLPG TPIKVIDGSD ENIKVTHPVD
VHLADKLFQL AAAQAPRLSH RSYTEELAGR TIVIFGGSYG IGHDLAELAR GYGAQVFPFS
RSSTGTHVEQ TGDVEAALKT AFEATGRIDH VVVTAGILEK GALAEMDEET MDRVLQVNFV
GPVIAARQSL PYLQQTKGQL LLYTSSSYTR GRAQYALYSS TKAALVNLTQ ALSDEWAEFG
VRVNCINPER TATPMRTKAF GEEPEHTLLA AEAVAQSSLD VLISDLTGQV IDVRRAPGEP
APAPVPAQPT TAEHDRLPNG VDAG
//
