ISPD_NEIG1
ID ISPD_NEIG1 Reviewed; 229 AA.
AC Q5F829;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=NGO0972;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) 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: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; AE004969; AAW89658.1; -; Genomic_DNA.
DR RefSeq; WP_003693342.1; NC_002946.2.
DR RefSeq; YP_208070.1; NC_002946.2.
DR PDB; 1VGW; X-ray; 2.35 A; A/B/C/D/E/F=2-229.
DR PDB; 1VGZ; X-ray; 3.00 A; A/B=2-229.
DR PDBsum; 1VGW; -.
DR PDBsum; 1VGZ; -.
DR AlphaFoldDB; Q5F829; -.
DR SMR; Q5F829; -.
DR STRING; 242231.NGO_0972; -.
DR EnsemblBacteria; AAW89658; AAW89658; NGO_0972.
DR KEGG; ngo:NGO_0972; -.
DR PATRIC; fig|242231.10.peg.1138; -.
DR HOGENOM; CLU_061281_3_0_4; -.
DR OMA; ERQHSVY; -.
DR UniPathway; UPA00056; UER00093.
DR EvolutionaryTrace; Q5F829; -.
DR Proteomes; UP000000535; 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 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;
KW Reference proteome; Transferase.
FT CHAIN 1..229
FT /note="2-C-methyl-D-erythritol 4-phosphate
FT cytidylyltransferase"
FT /id="PRO_0000237799"
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 158
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 212
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:1VGW"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:1VGW"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1VGW"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:1VGW"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1VGW"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:1VGW"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1VGW"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1VGW"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:1VGW"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1VGW"
FT STRAND 144..156
FT /evidence="ECO:0007829|PDB:1VGW"
FT STRAND 161..171
FT /evidence="ECO:0007829|PDB:1VGW"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:1VGW"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:1VGW"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1VGW"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1VGW"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:1VGW"
SQ SEQUENCE 229 AA; 24467 MW; 49E86A75051231A9 CRC64;
MKRKNIALIP AAGIGVRFGA DKPKQYVEIG SKTVLEHVLG IFERHEAVDL TVVVVSPEDT
FADKVQTAFP QVRVWKNGGQ TRAETVRNGV AKLLETGLAA ETDNILVHDA ARCCLPSEAL
ARLIEQAGNA AEGGILAVPV ADTLKRAESG QISATVDRSG LWQAQTPQLF QAGLLHRALA
AENLGGITDE ASAVEKLGVR PLLIQGDARN LKLTQPQDAY IVRLLLNAV
