ID E6Y2G1_9SPER Unreviewed; 312 AA.
AC E6Y2G1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000256|ARBA:ARBA00012526};
DE EC=2.7.7.60 {ECO:0000256|ARBA:ARBA00012526};
GN Name=MECT {ECO:0000313|EMBL:ABU48538.1};
OS Taxus x media.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Taxaceae;
OC Taxus.
OX NCBI_TaxID=85957 {ECO:0000313|EMBL:ABU48538.1};
RN [1] {ECO:0000313|EMBL:ABU48538.1}
RP NUCLEOTIDE SEQUENCE.
RA Liu W., Zhu S., Chen M., Tang J., Liao Z.;
RT "Cloning and functional characterization of 2-C-methyl-D-erythritol 4-
RT phosphate cytidyltransferase (TmMECT) gene from Taxus media.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000256|ARBA:ARBA00009789}.
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DR EMBL; EF534010; ABU48538.1; -; mRNA.
DR AlphaFoldDB; E6Y2G1; -.
DR SMR; E6Y2G1; -.
DR UniPathway; UPA00056; UER00093.
DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABU48538.1}.
FT REGION 64..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 34328 MW; D435AEBB03408D7D CRC64;
MSLVRCGRRP AISFSTHSCT PKLLRSSTSI ASSWGRGRRW VCPSSVQGPL LKCSSSHTRI
RTTLSAKPTD VDASPSQSPP APREVTKKSV SVILLAGGQG KRMGASMPKQ YLPLLGVPIA
LYSFFTFARI PEVKEIIAVC DSSYRDIFED AKESVMVNLK FASPGKERQD SVYNGLQEID
PLADLVCVHD SARPLVSPKD VEKVLQDAWV HGAAVLGVSV KATIKEANND SFVVKTLDRQ
MLWEMQTPQV VKPGLLRKGF ELVQRDSLEV TDDVSIVEHL KHPVYITQGS YTNIKVTTPD
DLLVAERILN QD
//
