ISPE_SHIF8
ID ISPE_SHIF8 Reviewed; 283 AA.
AC Q0T5I7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=SFV_1222;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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 -!- SUBUNIT: Homodimer. {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; CP000266; ABF03428.1; -; Genomic_DNA.
DR RefSeq; WP_001260333.1; NC_008258.1.
DR AlphaFoldDB; Q0T5I7; -.
DR SMR; Q0T5I7; -.
DR EnsemblBacteria; ABF03428; ABF03428; SFV_1222.
DR GeneID; 66674972; -.
DR KEGG; sfv:SFV_1222; -.
DR HOGENOM; CLU_053057_3_0_6; -.
DR OMA; RWPSPAK; -.
DR BioCyc; SFLE373384:SFV_RS06805-MON; -.
DR UniPathway; UPA00056; UER00094.
DR Proteomes; UP000000659; 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 Transferase.
FT CHAIN 1..283
FT /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT /id="PRO_1000007895"
FT ACT_SITE 10
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT ACT_SITE 141
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT BINDING 99..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
SQ SEQUENCE 283 AA; 30953 MW; 59A28094A05D13E1 CRC64;
MRTQWPSPAK LNLFLYITGQ RADGYHTLQT LFQFLDYGDT ISIELRDDGD IRLLTPVEGV
EHEDNLIVRA ARLLMKTAAD SGRLPTGSGA NISIDKRLPM GGGLGGGSSN AATVLVALNH
LWQCGLSMDE LAEMGLTLGA DVPVFVRGHA AFAEGVGEIL TPVDPPEKWY LVAHPGVSIP
TPVIFKDPEL PRNTPKRSIE TLLKCEFSND CEVIARKRFR EVDAVLSWLL EYAPSRLTGT
GACVFAEFDT ESEARQVLEQ APEWLNGFVA KGVNLSPLHR AML
