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Database: UniProt
Entry: D5SR99_PLAL2
LinkDB: D5SR99_PLAL2
Original site: D5SR99_PLAL2 
ID   D5SR99_PLAL2            Unreviewed;       308 AA.
AC   D5SR99;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 75.
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=Plim_2769 {ECO:0000313|EMBL:ADG68592.1};
OS   Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS   (Planctomyces limnophilus).
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctopirus.
OX   NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG68592.1, ECO:0000313|Proteomes:UP000002220};
RN   [1] {ECO:0000313|EMBL:ADG68592.1, ECO:0000313|Proteomes:UP000002220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290
RC   {ECO:0000313|Proteomes:UP000002220};
RX   PubMed=21304691; DOI=10.4056/sigs.1052813;
RA   Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT   290).";
RL   Stand. Genomic Sci. 3:47-56(2010).
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; CP001744; ADG68592.1; -; Genomic_DNA.
DR   RefSeq; WP_013111023.1; NC_014148.1.
DR   AlphaFoldDB; D5SR99; -.
DR   STRING; 521674.Plim_2769; -.
DR   KEGG; plm:Plim_2769; -.
DR   eggNOG; COG1947; Bacteria.
DR   HOGENOM; CLU_053057_1_1_0; -.
DR   OMA; RWPSPAK; -.
DR   OrthoDB; 9809438at2; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000002220; 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:UP000002220};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00061}.
FT   DOMAIN          110..168
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          222..294
FT                   /note="GHMP kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08544"
FT   ACT_SITE        17
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
FT   ACT_SITE        160
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
FT   BINDING         118..128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
SQ   SEQUENCE   308 AA;  33156 MW;  F244AF08128FA9D4 CRC64;
     MQLQQSENRL IVQAPAKLNL SLRILARRPD GFHEIETVMV SIQHYDTLSF APSSQTDISF
     RFEDLTHHPL ATTTHSFADE TALVPQDHTN LVVRAALLLK EYAKVDCGAE ILLQKRIPAA
     AGLAGGSSNA AATLAALNQL WNLRLTLQEL SQLASQLGSD IPFFLCGKPM AVCRGRGEII
     EPVELQEKLW FVVAKPPAGL STALVYRHCQ PTQNSPSIAP LLSNLAKGDQ ISAAHALHNG
     LQAAAVELCP AIRQLESTFA NLDVIAHQMS GSGTAYFGWC RSEAAAHTAA QQLTHLGLAQ
     VFVACSGL
//
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