ISPE_AQUAE
ID ISPE_AQUAE Reviewed; 268 AA.
AC O67060;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
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}; OrderedLocusNames=aq_915;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC07027.1; -; Genomic_DNA.
DR PIR; A70379; A70379.
DR RefSeq; NP_213622.1; NC_000918.1.
DR RefSeq; WP_010880560.1; NC_000918.1.
DR PDB; 2V2Q; X-ray; 2.30 A; A/B=1-268.
DR PDB; 2V2V; X-ray; 2.40 A; A/B=1-268.
DR PDB; 2V2Z; X-ray; 2.25 A; A/B=1-268.
DR PDB; 2V34; X-ray; 2.30 A; A/B=1-268.
DR PDB; 2V8P; X-ray; 2.10 A; A/B=1-268.
DR PDB; 2VF3; X-ray; 2.20 A; A/B=1-268.
DR PDBsum; 2V2Q; -.
DR PDBsum; 2V2V; -.
DR PDBsum; 2V2Z; -.
DR PDBsum; 2V34; -.
DR PDBsum; 2V8P; -.
DR PDBsum; 2VF3; -.
DR AlphaFoldDB; O67060; -.
DR SMR; O67060; -.
DR STRING; 224324.aq_915; -.
DR EnsemblBacteria; AAC07027; AAC07027; aq_915.
DR KEGG; aae:aq_915; -.
DR PATRIC; fig|224324.8.peg.714; -.
DR eggNOG; COG1947; Bacteria.
DR HOGENOM; CLU_053057_2_0_0; -.
DR InParanoid; O67060; -.
DR OMA; RWPSPAK; -.
DR OrthoDB; 1938933at2; -.
DR BRENDA; 2.7.1.148; 396.
DR UniPathway; UPA00056; UER00094.
DR EvolutionaryTrace; O67060; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IBA:GO_Central.
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; 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; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Isoprene biosynthesis; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..268
FT /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT /id="PRO_0000189183"
FT ACT_SITE 9
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT ACT_SITE 130
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT BINDING 88..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT STRAND 2..19
FT /evidence="ECO:0007829|PDB:2V8P"
FT STRAND 25..46
FT /evidence="ECO:0007829|PDB:2V8P"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2V8P"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2V8P"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:2V8P"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:2V8P"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:2V8P"
FT HELIX 95..110
FT /evidence="ECO:0007829|PDB:2V8P"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:2V8P"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:2V8P"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:2V8P"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:2V8P"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:2V8P"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:2V8P"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:2V8P"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:2V8P"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:2VF3"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:2V8P"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2V8P"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:2V8P"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:2V8P"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:2V8P"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:2V8P"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:2V8P"
SQ SEQUENCE 268 AA; 29788 MW; C905F9B988E0B45D CRC64;
MIKVLSPAKI NLGLWVLGRL PSGYHEILTL YQEIPFYDEI YIREGVLRVE TNIGIPQEEN
LVYKGLREFE RITGIEINYS IFIQKNIPPG AGLGGGSSNL AVVLKKVNEL LGSPLSEEEL
RELVGSISAD APFFLLGKSA IGRGKGEVLE PVETEISGKI TLVIPQVSSS TGRVYSSLRE
EHFVTPEYAE EKIQRIISGE VEEIENVLGD IARELYPEIN EVYRFVEYLG FKPFVSGSGS
TVYFFGGASE ELKKAAKMRG WKVVELEL
