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Database: UniProt
Entry: F3KPK9_9BURK
LinkDB: F3KPK9_9BURK
Original site: F3KPK9_9BURK 
ID   F3KPK9_9BURK            Unreviewed;       331 AA.
AC   F3KPK9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
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:EGI78267.1};
GN   Synonyms=ispE {ECO:0000256|HAMAP-Rule:MF_00061};
GN   ORFNames=HGR_01844 {ECO:0000313|EMBL:EGI78267.1};
OS   Hylemonella gracilis ATCC 19624.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hylemonella.
OX   NCBI_TaxID=887062 {ECO:0000313|EMBL:EGI78267.1, ECO:0000313|Proteomes:UP000016368};
RN   [1] {ECO:0000313|EMBL:EGI78267.1, ECO:0000313|Proteomes:UP000016368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19624 {ECO:0000313|EMBL:EGI78267.1,
RC   ECO:0000313|Proteomes:UP000016368};
RX   PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA   Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA   Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA   Jensen G.J.;
RT   "Structural diversity of bacterial flagellar motors.";
RL   EMBO J. 30:2972-2981(2011).
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:EGI78267.1}.
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DR   EMBL; AEGR01000024; EGI78267.1; -; Genomic_DNA.
DR   RefSeq; WP_006296344.1; NZ_AEGR01000024.1.
DR   AlphaFoldDB; F3KPK9; -.
DR   STRING; 887062.HGR_01844; -.
DR   eggNOG; COG1947; Bacteria.
DR   OrthoDB; 9809438at2; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000016368; 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};
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW   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:UP000016368};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00061}.
FT   DOMAIN          91..147
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          241..299
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        141
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
FT   BINDING         99..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
SQ   SEQUENCE   331 AA;  35498 MW;  B62C048CF8C9898E CRC64;
     MPTSLHDVSA PAKLNLFLHV TGRRADGYHL LQSVFTLIDW ADTLHFETRA HRQHDGGLSR
     EDLTTPLPAD DLVLRAARAL QAATGHAGGA HIAIAKHIPA QAGLGGGSSD AASTLLALNR
     LWKLKLSLEQ LAAIGLTLGA DVPYFLHSAH AKQATAWVEG VGERITPLPA NLEPARLLPG
     HALLVVKPDA GLETAAIFRD PALKRDSFAA TITGFAADPG VGSASEEKPN DVEHNRDRGA
     QSFRKFLLED SRNDLQPVAQ RLCPGVTQAL EWLNSLGLSG RMTGSGSAVF AWVAPEMHVR
     ARFSSTAIAV PDQMQSRWCR SLDVHPLAHW A
//
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