ID A0A1E3G0Q9_9BACT Unreviewed; 457 AA.
AC A0A1E3G0Q9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=A4H02_08645 {ECO:0000313|EMBL:ODN29812.1};
OS Fervidobacterium thailandense.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=1008305 {ECO:0000313|EMBL:ODN29812.1, ECO:0000313|Proteomes:UP000094570};
RN [1] {ECO:0000313|Proteomes:UP000094570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FC2004 {ECO:0000313|Proteomes:UP000094570};
RA Gonzalez J.M., Cuecas A., Kanoksilapatham W.;
RT "The genome sequence project of a novel Fervidobacterium isolate from a hot
RT spring in Thailand.";
RL Submitted (APR-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|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:ODN29812.1}.
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DR EMBL; LWAF01000018; ODN29812.1; -; Genomic_DNA.
DR RefSeq; WP_069293784.1; NZ_LWAF01000018.1.
DR AlphaFoldDB; A0A1E3G0Q9; -.
DR STRING; 1008305.A4H02_08645; -.
DR UniPathway; UPA00056; UER00093.
DR Proteomes; UP000094570; Unassembled WGS sequence.
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; IPR018294; ISPD_synthase_CS.
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 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; PF13561; adh_short_C2; 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.
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00108}.
FT SITE 19
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT SITE 26
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT SITE 157
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT SITE 214
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
SQ SEQUENCE 457 AA; 51333 MW; 0A8824C4E94449AE CRC64;
MFDGKRVYAF ILAAGSSERF GMDIPKQYVR ISGKTVLEHT LEVFENNEFI DEIYLIVNPQ
HRDLVEEIMV RNFFKKVSKI LNGGKTRQES TKVAISALED LDSYVLVHDA VRPFVSHRII
NAVLDKLKEF ESVDVAIPAT DTIIKVSQNL ISEVPNRHEL MLGQTPQGFR AGVLKKAYEI
FDRNPIAATD DCTLVLKYNL GRVYVVEGER FNIKITYPED LYLVDKIFQV RTAGVTNLET
ADLRSLKEKV LVVFGGNTGI GLKICELAQK YGAKAYAFSR RNACDVSSPD DVRKALREVN
DREGKIDFVV DSAAVLSLST LDSSSYDSIL TQIMTNYFGA IVIAKESFPF LQKTKGALLL
FASSSYTRGR KLYSIYSSTK AALVNLAQAL SEEWAVHNCR VNVINPERTN TELRRKNFGL
EDPSSLLDPH VVAEVALKVL LSNFTGQVID IRKQDYF
//
