ISPE_SYNE7
ID ISPE_SYNE7 Reviewed; 314 AA.
AC Q31RH7;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061};
DE Short=CMK {ECO:0000255|HAMAP-Rule:MF_00061};
DE EC=2.7.1.148 {ECO:0000255|HAMAP-Rule:MF_00061};
DE AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061};
GN Name=ispE {ECO:0000255|HAMAP-Rule:MF_00061};
GN OrderedLocusNames=Synpcc7942_0310;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group
CC of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000255|HAMAP-
CC Rule:MF_00061}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-
CC erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823,
CC ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00061};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 3/6. {ECO:0000255|HAMAP-Rule:MF_00061}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00061}.
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DR EMBL; CP000100; ABB56342.1; -; Genomic_DNA.
DR RefSeq; WP_011243515.1; NC_007604.1.
DR AlphaFoldDB; Q31RH7; -.
DR SMR; Q31RH7; -.
DR STRING; 1140.Synpcc7942_0310; -.
DR PRIDE; Q31RH7; -.
DR EnsemblBacteria; ABB56342; ABB56342; Synpcc7942_0310.
DR KEGG; syf:Synpcc7942_0310; -.
DR eggNOG; COG1947; Bacteria.
DR HOGENOM; CLU_053057_1_1_3; -.
DR OMA; RWPSPAK; -.
DR OrthoDB; 1938933at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0310-MON; -.
DR UniPathway; UPA00056; UER00094.
DR GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR HAMAP; MF_00061; IspE; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR004424; IspE.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF010376; IspE; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00154; ispE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Isoprene biosynthesis; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..314
FT /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT /id="PRO_0000235145"
FT ACT_SITE 11
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT ACT_SITE 137
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT BINDING 95..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
SQ SEQUENCE 314 AA; 33747 MW; 73A524A99939DD89 CRC64;
MKTLTLVAPA KINFYLEILG DRPDGFHELA MVMQSIALGD RLHLRQRQGQ GFQLGCDRAD
LEVDERNLIL KAAQRLQRSF PQIGGVDFFL EKRIPIGAGL AGGSTDGAAA LVGLDIFSGL
GLTQPELEAI AAELGSDMPF CVAGGTQLCT SRGEQLTPLP PLPSLSLVLA KFESLSVSTP
WAYGRYREQF GDRYLQTEPA RRDRLQALHA GPLLQAMSAG DPVAIAQHLR NDLEAVVLPE
YPQVAELRSV LGNCSGILAA QMSGSGPSVF GIAENPTAAQ AAVEQVRQAI ADPDLKLWVT
QTISHGIQTE TLLR
