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Database: UniProt/TrEMBL
Entry: F6EQR2_AMYSD
LinkDB: F6EQR2_AMYSD
Original site: F6EQR2_AMYSD 
ID   F6EQR2_AMYSD            Unreviewed;       322 AA.
AC   F6EQR2;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   29-OCT-2014, entry version 21.
DE   RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase {ECO:0000256|HAMAP-Rule:MF_00061};
DE            Short=CMK {ECO:0000256|HAMAP-Rule:MF_00061};
DE            EC=2.7.1.148 {ECO:0000256|HAMAP-Rule:MF_00061};
DE   AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase {ECO:0000256|HAMAP-Rule:MF_00061};
GN   Name=ispE {ECO:0000256|HAMAP-Rule:MF_00061,
GN   ECO:0000313|EMBL:AEF41939.1};
GN   OrderedLocusNames=AS9A_3499 {ECO:0000313|EMBL:AEF41939.1};
OS   Amycolicicoccus subflavus (strain DSM 45089 / DQS3-9A1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Amycolicicoccus.
OX   NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF41939.1, ECO:0000313|Proteomes:UP000009235};
RN   [1] {ECO:0000313|EMBL:AEF41939.1, ECO:0000313|Proteomes:UP000009235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX   PubMed=21725023; DOI=10.1128/JB.05388-11;
RA   Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA   Wu X.L.;
RT   "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT   actinomycete isolated from crude oil-polluted soil.";
RL   J. Bacteriol. 193:4538-4539(2011).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy
CC       group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
CC       {ECO:0000256|HAMAP-Rule:MF_00061, ECO:0000256|SAAS:SAAS00090320}.
CC   -!- CATALYTIC ACTIVITY: ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-
CC       erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-
CC       D-erythritol. {ECO:0000256|HAMAP-Rule:MF_00061,
CC       ECO:0000256|SAAS:SAAS00090328}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 3/6. {ECO:0000256|HAMAP-
CC       Rule:MF_00061, ECO:0000256|SAAS:SAAS00090332}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00061}.
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DR   EMBL; CP002786; AEF41939.1; -; Genomic_DNA.
DR   RefSeq; YP_004494739.1; NC_015564.1.
DR   ProteinModelPortal; F6EQR2; -.
DR   EnsemblBacteria; AEF41939; AEF41939; AS9A_3499.
DR   GeneID; 10635667; -.
DR   KEGG; asd:AS9A_3499; -.
DR   KO; K00919; -.
DR   OMA; AREDGYH; -.
DR   BioCyc; ASUB443218:GH9R-3535-MONOMER; -.
DR   UniPathway; UPA00056; UER00094.
DR   GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP.
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; 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; PTHR20861:SF2; PTHR20861: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 {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|RuleBase:RU003563};
KW   Complete proteome {ECO:0000313|Proteomes:UP000009235};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00090370};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|RuleBase:RU003563};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|RuleBase:RU003563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009235};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|RuleBase:RU003563}.
FT   NP_BIND     101    111       ATP. {ECO:0000256|HAMAP-Rule:MF_00061}.
FT   ACT_SITE     16     16       {ECO:0000256|HAMAP-Rule:MF_00061}.
FT   ACT_SITE    143    143       {ECO:0000256|HAMAP-Rule:MF_00061}.
SQ   SEQUENCE   322 AA;  33465 MW;  191821039B31520E CRC64;
     MLHVVDEPVK VRAPAKVNLH LAVGDLRDDG YHELTTVFQA LSLYDEVAVT RGDALTVSVK
     GEGAREVPLD ENNLVWRAAQ LMAEKAGRSP RIHIAIRKGI PVAGGLAGGS ADAAATLVAL
     NTLWHLELSR GELSDLAAEL GSDVPFSLRG GTAMGIGRGE QLLPVLSRST YHWVLAFANG
     GLSTPAVYKE LDRLRESGTR PRLGSADDLM HALTVGDPDA LAPLLGNDLQ AAAISLKPQL
     RRTLRAGKDA GALAAIVSGS GPTCAFLCRD AEDAVSVGVE VSATGVCRTV RTATGPVPGA
     RVIDTDSGPD DPAQERAVDG GA
//
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