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Database: UniProt
Entry: A0A0M0KU54_9BACI
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ID   A0A0M0KU54_9BACI        Unreviewed;       289 AA.
AC   A0A0M0KU54;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=ipk {ECO:0000313|EMBL:KOO42349.1};
GN   Synonyms=ispE {ECO:0000256|HAMAP-Rule:MF_00061};
GN   ORFNames=AMD01_18430 {ECO:0000313|EMBL:KOO42349.1};
OS   Priestia koreensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=284581 {ECO:0000313|EMBL:KOO42349.1, ECO:0000313|Proteomes:UP000037558};
RN   [1] {ECO:0000313|Proteomes:UP000037558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16467 {ECO:0000313|Proteomes:UP000037558};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-14210 dsm16467.";
RL   Submitted (AUG-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOO42349.1}.
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DR   EMBL; LILC01000025; KOO42349.1; -; Genomic_DNA.
DR   RefSeq; WP_053402915.1; NZ_LILC01000025.1.
DR   AlphaFoldDB; A0A0M0KU54; -.
DR   STRING; 284581.AMD01_18430; -.
DR   PATRIC; fig|284581.3.peg.1778; -.
DR   OrthoDB; 9809438at2; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000037558; Unassembled WGS sequence.
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:UP000037558};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00061}.
FT   DOMAIN          87..144
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          197..273
FT                   /note="GHMP kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08544"
FT   ACT_SITE        10
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
FT   BINDING         94..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
SQ   SEQUENCE   289 AA;  31599 MW;  D2930E97189A289A CRC64;
     MKLMVKAPAK INLSLDVLHK RPDGYHEVKM VMTTIDLADR IELAKRNDSK IIVQSQNRFV
     PDDQRNLAYQ AAHLLKERFN VSSGVTINIE KNIPVAAGLA GGSSDAAATL RGLNTLWELG
     LSLDELADIG AEIGSDVSFC VYGGTALATG RGEVIEHIET PPNCWVILAK PETGVSTAEV
     YRNLRLGNVE HPDVDGMVSA INEQNYADMC KLVGNVLESV TLNMHPEVAL IKDQMKRFGA
     DAVLMSGSGP TVFCLVKYDS RMQRIYNGLR GFCSKVYAVR LLGERLPLD
//
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