ISPD_BURTA
ID ISPD_BURTA Reviewed; 236 AA.
AC Q2SWT6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108};
DE EC=2.7.7.60 {ECO:0000255|HAMAP-Rule:MF_00108};
DE AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000255|HAMAP-Rule:MF_00108};
DE AltName: Full=MEP cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108};
DE Short=MCT {ECO:0000255|HAMAP-Rule:MF_00108};
GN Name=ispD {ECO:0000255|HAMAP-Rule:MF_00108}; OrderedLocusNames=BTH_I2089;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00108}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00108}.
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DR EMBL; CP000086; ABC37697.1; -; Genomic_DNA.
DR RefSeq; WP_009890558.1; NZ_CP008785.1.
DR PDB; 4YS8; X-ray; 2.45 A; A/B/C/D=2-236.
DR PDB; 4ZDQ; X-ray; 2.30 A; A/B/C/D=2-236.
DR PDBsum; 4YS8; -.
DR PDBsum; 4ZDQ; -.
DR AlphaFoldDB; Q2SWT6; -.
DR SMR; Q2SWT6; -.
DR ChEMBL; CHEMBL3734645; -.
DR PRIDE; Q2SWT6; -.
DR EnsemblBacteria; ABC37697; ABC37697; BTH_I2089.
DR KEGG; bte:BTH_I2089; -.
DR HOGENOM; CLU_061281_3_0_4; -.
DR OMA; ERQHSVY; -.
DR OrthoDB; 1836139at2; -.
DR UniPathway; UPA00056; UER00093.
DR Proteomes; UP000001930; Chromosome I.
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 Gene3D; 3.90.550.10; -; 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 Pfam; PF01128; IspD; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR00453; ispD; 1.
DR PROSITE; PS01295; ISPD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isoprene biosynthesis; Nucleotidyltransferase; Transferase.
FT CHAIN 1..236
FT /note="2-C-methyl-D-erythritol 4-phosphate
FT cytidylyltransferase"
FT /id="PRO_0000237780"
FT SITE 17
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 24
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 159
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 215
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:4YS8"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT STRAND 162..172
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:4ZDQ"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:4ZDQ"
SQ SEQUENCE 236 AA; 25393 MW; A1D68FB6670B4BF4 CRC64;
MTSRLFALIP CAGTGSRSGS ALPKQYRTLA GRALLHYTLA AFDACSEFAQ TLVVISPDDA
HFDARRFAGL RFAVRRCGGA SRQASVMNGL IQLAEFGATD ADWVLVHDAA RPGITPALIR
TLIGALKDDP VGGIVALPVA DTLKRVPAGG DAIERTESRN GLWQAQTPQM FRIGMLRDAI
QRAQLEGRDL TDEASAIEWA GHTPRVVQGS LRNFKVTYPE DFDLAEAILA HPARAS
