ISPE_GLUDA
ID ISPE_GLUDA Reviewed; 305 AA.
AC A9HAC0; B5ZHI5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061};
DE Short=CMK {ECO:0000255|HAMAP-Rule:MF_00061};
DE EC=2.7.1.148 {ECO:0000255|HAMAP-Rule:MF_00061};
DE AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061};
GN Name=ispE {ECO:0000255|HAMAP-Rule:MF_00061};
GN OrderedLocusNames=GDI0728, Gdia_1283;
OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS / CIP 103539 / LMG 7603 / PAl5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=272568;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A.,
RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA Figueiredo D., Montano H., Junior J., de Souza Filho G.,
RA Martin Quintana Flores V., Ferreira B., Branco A., Gonzalez P.,
RA Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M.,
RA Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A.,
RA Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T.,
RA Rael Pereira A., Silva R., Rondinelli E., von Kruger W., Martins O.,
RA Baldani J.I., Ferreira P.C.;
RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT Gluconacetobacter diazotrophicus Pal5.";
RL BMC Genomics 10:450-450(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX PubMed=21304715; DOI=10.4056/sigs.972221;
RA Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.;
RT "Two genome sequences of the same bacterial strain, Gluconacetobacter
RT diazotrophicus PAl 5, suggest a new standard in genome sequence
RT submission.";
RL Stand. Genomic Sci. 2:309-317(2010).
CC -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group
CC of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00061}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00061}.
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DR EMBL; AM889285; CAP54671.1; -; Genomic_DNA.
DR EMBL; CP001189; ACI51065.1; -; Genomic_DNA.
DR RefSeq; WP_012223358.1; NC_010125.1.
DR AlphaFoldDB; A9HAC0; -.
DR SMR; A9HAC0; -.
DR STRING; 272568.GDI0728; -.
DR PRIDE; A9HAC0; -.
DR EnsemblBacteria; ACI51065; ACI51065; Gdia_1283.
DR EnsemblBacteria; CAP54671; CAP54671; GDI0728.
DR KEGG; gdi:GDI0728; -.
DR KEGG; gdj:Gdia_1283; -.
DR eggNOG; COG1947; Bacteria.
DR HOGENOM; CLU_053057_1_0_5; -.
DR OMA; RWPSPAK; -.
DR UniPathway; UPA00056; UER00094.
DR Proteomes; UP000000736; Chromosome.
DR Proteomes; UP000001176; 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; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR43527:SF2; PTHR43527:SF2; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF010376; IspE; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00154; ispE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Isoprene biosynthesis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..305
FT /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT /id="PRO_0000335715"
FT ACT_SITE 17
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT ACT_SITE 154
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT BINDING 111..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT CONFLICT 51
FT /note="R -> H (in Ref. 2; ACI51065)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="A -> V (in Ref. 2; ACI51065)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="L -> P (in Ref. 2; ACI51065)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="A -> P (in Ref. 2; ACI51065)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="A -> V (in Ref. 2; ACI51065)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="G -> A (in Ref. 2; ACI51065)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 31481 MW; BF9839CBF565F43E CRC64;
MTDPTGTGTL HESAHAKINL YLHVTGRRPD GYHLLDSLAV FAGAADRLTL RPGAAGQGEA
VALDIAGAFG AGLVADTDSN LVLQAARRLR AEMGVTDRLA PMRIVLEKSL PVASGIGGGS
ADAAAALRLL LRAWPGEALP RARLMALAVE LGADVPVCID QRAARMGGVG ERLAPAPALP
NCGMMLVNCG EAVPTPAVFR ARAPVFTPAA SLPSAWPDVG AMVRDLAALT NDLQDAACEL
CPTIRTVLQV LDAAPGCRLA RMSGSGATCF ALFDSPQGAR DAMTAVERPG WWVWAGGLHG
MPAET
