ID C6XT77_PEDHD Unreviewed; 267 AA. AC C6XT77; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 04-NOV-2026, entry version 91. DE RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase {ECO:0000256|ARBA:ARBA00017473, ECO:0000256|HAMAP-Rule:MF_00061}; DE Short=CMK {ECO:0000256|HAMAP-Rule:MF_00061}; DE EC=2.7.1.148 {ECO:0000256|ARBA:ARBA00012052, ECO:0000256|HAMAP-Rule:MF_00061}; DE AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase {ECO:0000256|ARBA:ARBA00032554, ECO:0000256|HAMAP-Rule:MF_00061}; GN Name=ispE {ECO:0000256|HAMAP-Rule:MF_00061}; GN OrderedLocusNames=Phep_1424 {ECO:0000313|EMBL:ACU03638.1}; OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 OS / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3). OC Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia; OC Sphingobacteriales; Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU03638.1, ECO:0000313|Proteomes:UP000000852}; RN [1] {ECO:0000313|EMBL:ACU03638.1, ECO:0000313|Proteomes:UP000000852} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / RC NCIMB 9290 / NRRL B-14731 / HIM 762-3 RC {ECO:0000313|Proteomes:UP000000852}; RX PubMed=21304637; DOI=10.4056/sigs.22138; RA Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A., RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.C., Saunders E., Chertkov O., RA Brettin T., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of Pedobacter heparinus type strain (HIM 762- RT 3)."; RL Stand. Genomic Sci. 1:54-62(2009). CC -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group CC of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00061}. CC -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily. CC {ECO:0000256|ARBA:ARBA00009684, ECO:0000256|HAMAP-Rule:MF_00061}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001681; ACU03638.1; -; Genomic_DNA. DR RefSeq; WP_012781582.1; NC_013061.1. DR AlphaFoldDB; C6XT77; -. DR STRING; 485917.Phep_1424; -. DR KEGG; phe:Phep_1424; -. DR eggNOG; COG1947; Bacteria. DR HOGENOM; CLU_053057_1_1_10; -. DR OMA; AACLEMS; -. DR OrthoDB; 9809438at2; -. DR UniPathway; UPA00056; UER00094. DR Proteomes; UP000000852; Chromosome. 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 phosphate pathway; IEA:UniProtKB-UniRule. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 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_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR NCBIfam; TIGR00154; ispE; 1. DR PANTHER; PTHR43527; 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR43527:SF2; 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE, CHLOROPLASTIC; 1. DR Pfam; PF08544; GHMP_kinases_C; 1. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PIRSF; PIRSF010376; IspE; 1. DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00061}; Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00061}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00061}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00061}; Reference proteome {ECO:0000313|Proteomes:UP000000852}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00061}. FT DOMAIN 63..137 FT /note="GHMP kinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00288" FT DOMAIN 199..256 FT /note="GHMP kinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF08544" FT ACT_SITE 8 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00061" FT ACT_SITE 132 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00061" FT BINDING 90..100 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00061" SQ SEQUENCE 267 AA; 29510 MW; 8256E1FAF169DF0C CRC64; MLAFANAKIN LGLNVTRKRP DGYHDIETVF YPVKLNDVVE ITDSENTICL VKGIDVPGDT RDNLCLKAFN LLKKDFDLPA QQITLLKNIP VGAGLGGGSS DAAQLIRLVN DKFKLGLSVV KMQNYARELG ADCAFFIENR PVYAFGKGDE FQPIAIDLSN YYVVLVKPPV HVSTAAAYAG IKPVIPSRSV KDLIHLPLKT WKQHLENDFE STVFSKYPEI ELVKKKLYQS GALFALMSGS GASVFAIFEH EVSLPELENG NKVFYNI //