ISPE_LEPIN
ID ISPE_LEPIN Reviewed; 297 AA.
AC Q8EZM8;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
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}; OrderedLocusNames=LA_3824;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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; AE010300; AAN51022.1; -; Genomic_DNA.
DR RefSeq; NP_714004.1; NC_004342.2.
DR RefSeq; WP_000625236.1; NC_004342.2.
DR AlphaFoldDB; Q8EZM8; -.
DR SMR; Q8EZM8; -.
DR STRING; 189518.LA_3824; -.
DR EnsemblBacteria; AAN51022; AAN51022; LA_3824.
DR KEGG; lil:LA_3824; -.
DR PATRIC; fig|189518.3.peg.3792; -.
DR HOGENOM; CLU_053057_1_1_12; -.
DR InParanoid; Q8EZM8; -.
DR OMA; RWPSPAK; -.
DR UniPathway; UPA00056; UER00094.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IBA:GO_Central.
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; IPR004424; IspE.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR43527:SF2; PTHR43527:SF2; 1.
DR Pfam; PF08544; GHMP_kinases_C; 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 Reference proteome; Transferase.
FT CHAIN 1..297
FT /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT /id="PRO_0000189229"
FT ACT_SITE 6
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT ACT_SITE 144
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
SQ SEQUENCE 297 AA; 33271 MW; 51AA1F018DAA7872 CRC64;
MISPAKINLG LEIPFKRLDG FHEIRSVFLK ISWGDDIEIE PASNGVFELF SNNEIILEKR
KLYDQVSERG DIKNNILYKT FIKARSLFPE LPGVKIHLTK RISPAGGLGG GSTNAASLLN
FLFSWRPFFT SDEMFVLAAE IGSDVPFFLG EGHAFVTGKG EILEEIEVHH GQGILALTPQ
VMNTSEMYSL LKKPLQESAS QKNGNTLSKN LISILKNGDW SSLQGRLWND FEPVAFQLHP
ELGVLKDKFL EFGSSYCSLT GSGSSMYGLV QGLEIQEELL QRLRQEFSNL TFVRFNF