ISPE_SALTY
ID ISPE_SALTY Reviewed; 283 AA.
AC P30753;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase;
DE Short=CMK;
DE EC=2.7.1.148;
DE AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase;
GN Name=ispE; Synonyms=ipk; OrderedLocusNames=STM1779;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7679718; DOI=10.1099/00221287-139-2-259;
RA Post D.A., Hove-Jensen B., Switzer R.L.;
RT "Characterization of the hemA-prs region of the Escherichia coli and
RT Salmonella typhimurium chromosomes: identification of two open reading
RT frames and implications for prs expression.";
RL J. Gen. Microbiol. 139:259-266(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 187-283.
RX PubMed=2838463; DOI=10.1128/jb.170.7.3243-3248.1988;
RA Bower S.G., Hove-Jensen B., Switzer R.L.;
RT "Structure of the gene encoding phosphoribosylpyrophosphate synthetase
RT (prsA) in Salmonella typhimurium.";
RL J. Bacteriol. 170:3243-3248(1988).
CC -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group
CC of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000250}.
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 -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 3/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=M19488; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M77236; AAA27195.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20694.1; -; Genomic_DNA.
DR EMBL; M19488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S27732; S27732.
DR RefSeq; NP_460735.1; NC_003197.2.
DR RefSeq; WP_000988246.1; NC_003197.2.
DR AlphaFoldDB; P30753; -.
DR SMR; P30753; -.
DR STRING; 99287.STM1779; -.
DR PaxDb; P30753; -.
DR EnsemblBacteria; AAL20694; AAL20694; STM1779.
DR GeneID; 1253298; -.
DR KEGG; stm:STM1779; -.
DR PATRIC; fig|99287.12.peg.1875; -.
DR HOGENOM; CLU_053057_3_0_6; -.
DR OMA; RWPSPAK; -.
DR PhylomeDB; P30753; -.
DR BioCyc; SENT99287:STM1779-MON; -.
DR UniPathway; UPA00056; UER00094.
DR Proteomes; UP000001014; 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; 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..283
FT /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT /id="PRO_0000189258"
FT ACT_SITE 10
FT /evidence="ECO:0000250"
FT ACT_SITE 141
FT /evidence="ECO:0000250"
FT BINDING 99..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 252
FT /note="S -> L (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 283 AA; 30883 MW; E33EAF956D12A5BD CRC64;
MMTHWPSPAK LNLFLYITGQ RADGYHTLQT LFQFLDYGDT LHIEPRHDGE IHLLTPVNGV
ENEDNLIVRA ARLLMKVASE SGRLPAGSGA DISIEKRLPM GGGLGGGSSN AATVLVALNH
LWQCGLSIDE LATLGLTLGA DVPVFVRGHA AFAEGVGEIL TPVNPPEKWY LVAHPGVSIP
TPVIFKDPQL PRNTPKRSID TLLKCEFSND CEVIARKRFR EVDAALSWLL EYAPSRLTGT
GACVFAEFDT ESCARQVLEQ APEWLNAFVA KGVNLSPLHR ELL
