ID A0A249L585_9ACTN Unreviewed; 306 AA.
AC A0A249L585;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=B1sIIB91_05100 {ECO:0000313|EMBL:ASY24260.1};
OS Candidatus Nanopelagicus abundans.
OC Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC Candidatus Nanopelagicaceae; Nanopelagicus.
OX NCBI_TaxID=1884916 {ECO:0000313|EMBL:ASY24260.1, ECO:0000313|Proteomes:UP000217210};
RN [1] {ECO:0000313|EMBL:ASY24260.1, ECO:0000313|Proteomes:UP000217210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-IIB-91 {ECO:0000313|EMBL:ASY24260.1};
RA Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT "High microdiversification within the ubiquitous acI lineage of
RT Actinobacteria.";
RL Submitted (JUL-2016) 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: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}.
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DR EMBL; CP016779; ASY24260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249L585; -.
DR KEGG; nab:B1sIIB91_05100; -.
DR OrthoDB; 3173073at2; -.
DR UniPathway; UPA00056; UER00094.
DR Proteomes; UP000217210; 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 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; 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:UP000217210};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00061}.
FT DOMAIN 94..151
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 209..282
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT ACT_SITE 13
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
FT ACT_SITE 143
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
FT BINDING 101..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
SQ SEQUENCE 306 AA; 31330 MW; 97B5D3635AA63C83 CRC64;
MRSRGVIARV PAKVNLQLAV GPLGTDGFHE VTTVFQAISL FDDVTVETAA ENNGISIQVT
GQTSTGVPSD SSNLAVKAAT LMIKNYDLPS DINIKLKKEI PVAGGMAGGS ADAAGVIVGL
DSLFELGLSR DEMEMVGSKI GTDVPFSICG GVAIGTGRGD QITPALFKGS YNWVLALSGQ
GLATPSVYAE CDRLREGLSI STPVVSEHLM QALRAGDAKA LGKSLSNDLQ PAACSLRPAL
RLVLDVGLDY GALGGIVSGS GPTVAFLVKD EEHAMDLTVA LSSSGVISSV VRASGAVAGA
RIIESF
//
