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P62615

- ISPE_ECOLI

UniProt

P62615 - ISPE_ECOLI

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Protein

4-diphosphocytidyl-2-C-methyl-D-erythritol kinase

Gene

ispE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. Phosphorylates isopentenyl phosphate at low rates. Also acts on isopentenol, and, much less efficiently, dimethylallyl alcohol. Dimethylallyl monophosphate does not serve as a substrate.

Catalytic activityi

ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101By similarity
Active sitei141 – 1411By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi99 – 10911ATPSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity Source: EcoCyc
  2. ATP binding Source: EcoCyc

GO - Biological processi

  1. isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway Source: UniProtKB-UniPathway
  2. terpenoid biosynthetic process Source: UniProtKB-HAMAP
  3. ubiquinone biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Isoprene biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11294-MONOMER.
ECOL316407:JW1199-MONOMER.
MetaCyc:EG11294-MONOMER.
UniPathwayiUPA00056; UER00094.

Names & Taxonomyi

Protein namesi
Recommended name:
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (EC:2.7.1.148)
Short name:
CMK
Alternative name(s):
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
Gene namesi
Name:ispE
Synonyms:ipk, ychB
Ordered Locus Names:b1208, JW1199
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11294. ispE.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi239 – 2391G → R: Loss of activity. 1 Publication
Mutagenesisi240 – 2401T → I: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2832834-diphosphocytidyl-2-C-methyl-D-erythritol kinasePRO_0000189215Add
BLAST

Proteomic databases

PaxDbiP62615.

Expressioni

Gene expression databases

GenevestigatoriP62615.

Interactioni

Subunit structurei

Homodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
glmSP171691EBI-562202,EBI-551022

Protein-protein interaction databases

DIPiDIP-48028N.
IntActiP62615. 1 interaction.
STRINGi511145.b1208.

Structurei

Secondary structure

1
283
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 2019Combined sources
Beta strandi26 – 4924Combined sources
Beta strandi51 – 533Combined sources
Helixi62 – 643Combined sources
Helixi66 – 8015Combined sources
Beta strandi89 – 957Combined sources
Helixi106 – 12116Combined sources
Helixi128 – 1369Combined sources
Helixi142 – 1476Combined sources
Beta strandi151 – 1544Combined sources
Turni155 – 1584Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi169 – 1735Combined sources
Helixi181 – 1855Combined sources
Helixi199 – 2035Combined sources
Helixi212 – 2187Combined sources
Helixi220 – 23011Combined sources
Beta strandi235 – 2373Combined sources
Beta strandi244 – 2507Combined sources
Helixi251 – 26010Combined sources
Beta strandi267 – 2759Combined sources
Helixi277 – 2815Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WW4X-ray2.00A/B1-283[»]
ProteinModelPortaliP62615.
SMRiP62615. Positions 1-282.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GHMP kinase family. IspE subfamily.Curated

Phylogenomic databases

eggNOGiCOG1947.
HOGENOMiHOG000019601.
InParanoidiP62615.
KOiK00919.
OMAiVSTAEIF.
OrthoDBiEOG62VNQ2.
PhylomeDBiP62615.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.890. 1 hit.
HAMAPiMF_00061. IspE.
InterProiIPR013750. GHMP_kinase_C_dom.
IPR006204. GHMP_kinase_N_dom.
IPR004424. IspE.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR20861:SF2. PTHR20861:SF2. 1 hit.
PfamiPF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PIRSFiPIRSF010376. IspE. 1 hit.
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55060. SSF55060. 1 hit.
TIGRFAMsiTIGR00154. ispE. 1 hit.

Sequencei

Sequence statusi: Complete.

P62615 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRTQWPSPAK LNLFLYITGQ RADGYHTLQT LFQFLDYGDT ISIELRDDGD
60 70 80 90 100
IRLLTPVEGV EHEDNLIVRA ARLLMKTAAD SGRLPTGSGA NISIDKRLPM
110 120 130 140 150
GGGLGGGSSN AATVLVALNH LWQCGLSMDE LAEMGLTLGA DVPVFVRGHA
160 170 180 190 200
AFAEGVGEIL TPVDPPEKWY LVAHPGVSIP TPVIFKDPEL PRNTPKRSIE
210 220 230 240 250
TLLKCEFSND CEVIARKRFR EVDAVLSWLL EYAPSRLTGT GACVFAEFDT
260 270 280
ESEARQVLEQ APEWLNGFVA KGANLSPLHR AML
Length:283
Mass (Da):30,925
Last modified:July 19, 2004 - v1
Checksum:i59A2921FA05D13E1
GO

Sequence cautioni

The sequence BAA01106.1 differs from that shown. Reason: Frameshift at position 50.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 27669SNDCE…GANLS → TQAYGRANTKGAPFRRTAVK CRSLGKLLLECAGKCLLRVE AVLQRDVQNRTRSQA in BAA01106. (PubMed:1427085)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10264 Genomic DNA. Translation: BAA01106.1. Frameshift.
M77237 Genomic DNA. Translation: AAA24434.1.
U18555 Genomic DNA. Translation: AAC43434.1.
AJ249325 Genomic DNA. Translation: CAB64963.1.
AF179284 Genomic DNA. Translation: AAF13867.1.
AF216300 Genomic DNA. Translation: AAF29530.1.
AB037116 Genomic DNA. Translation: BAA94247.1.
U00096 Genomic DNA. Translation: AAC74292.1.
AP009048 Genomic DNA. Translation: BAA36066.1.
PIRiB47706.
RefSeqiNP_415726.1. NC_000913.3.
YP_489475.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74292; AAC74292; b1208.
BAA36066; BAA36066; BAA36066.
GeneIDi12931821.
945774.
KEGGiecj:Y75_p1180.
eco:b1208.
PATRICi32117668. VBIEscCol129921_1256.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10264 Genomic DNA. Translation: BAA01106.1 . Frameshift.
M77237 Genomic DNA. Translation: AAA24434.1 .
U18555 Genomic DNA. Translation: AAC43434.1 .
AJ249325 Genomic DNA. Translation: CAB64963.1 .
AF179284 Genomic DNA. Translation: AAF13867.1 .
AF216300 Genomic DNA. Translation: AAF29530.1 .
AB037116 Genomic DNA. Translation: BAA94247.1 .
U00096 Genomic DNA. Translation: AAC74292.1 .
AP009048 Genomic DNA. Translation: BAA36066.1 .
PIRi B47706.
RefSeqi NP_415726.1. NC_000913.3.
YP_489475.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WW4 X-ray 2.00 A/B 1-283 [» ]
ProteinModelPortali P62615.
SMRi P62615. Positions 1-282.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48028N.
IntActi P62615. 1 interaction.
STRINGi 511145.b1208.

Chemistry

ChEMBLi CHEMBL2366480.

Proteomic databases

PaxDbi P62615.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74292 ; AAC74292 ; b1208 .
BAA36066 ; BAA36066 ; BAA36066 .
GeneIDi 12931821.
945774.
KEGGi ecj:Y75_p1180.
eco:b1208.
PATRICi 32117668. VBIEscCol129921_1256.

Organism-specific databases

EchoBASEi EB1271.
EcoGenei EG11294. ispE.

Phylogenomic databases

eggNOGi COG1947.
HOGENOMi HOG000019601.
InParanoidi P62615.
KOi K00919.
OMAi VSTAEIF.
OrthoDBi EOG62VNQ2.
PhylomeDBi P62615.

Enzyme and pathway databases

UniPathwayi UPA00056 ; UER00094 .
BioCyci EcoCyc:EG11294-MONOMER.
ECOL316407:JW1199-MONOMER.
MetaCyc:EG11294-MONOMER.

Miscellaneous databases

PROi P62615.

Gene expression databases

Genevestigatori P62615.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
3.30.70.890. 1 hit.
HAMAPi MF_00061. IspE.
InterProi IPR013750. GHMP_kinase_C_dom.
IPR006204. GHMP_kinase_N_dom.
IPR004424. IspE.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view ]
PANTHERi PTHR20861:SF2. PTHR20861:SF2. 1 hit.
Pfami PF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF010376. IspE. 1 hit.
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55060. SSF55060. 1 hit.
TIGRFAMsi TIGR00154. ispE. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of genes involved in the biosynthesis of delta-aminolevulinic acid in Escherichia coli."
    Ikemi M., Murakami K., Hashimoto M., Murooka Y.
    Gene 121:127-132(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Characterization of the hemA-prs region of the Escherichia coli and Salmonella typhimurium chromosomes: identification of two open reading frames and implications for prs expression."
    Post D.A., Hove-Jensen B., Switzer R.L.
    J. Gen. Microbiol. 139:259-266(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12."
    Strohmaier H., Remler P., Renner W., Hoegenauer G.
    J. Bacteriol. 177:4488-4500(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  4. "Isopentenyl diphosphate biosynthesis via a mevalonate-independent pathway: isopentenyl monophosphate kinase catalyzes the terminal enzymatic step."
    Lange B.M., Croteau R.
    Proc. Natl. Acad. Sci. U.S.A. 96:13714-13719(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Biosynthesis of terpenoids: YchB protein of Escherichia coli phosphorylates the 2-hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol."
    Luettgen H., Rohdich F., Herz S., Wungsintaweekul J., Hecht S., Schuhr C.A., Fellermeier M., Sagner S., Zenk M.H., Bacher A., Eisenreich W.
    Proc. Natl. Acad. Sci. U.S.A. 97:1062-1067(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  6. "Studies on the nonmevalonate pathway: conversion of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol to its 2-phospho derivative by 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase."
    Kuzuyama T., Takagi M., Kaneda K., Watanabe H., Dairi T., Seto H.
    Tetrahedron Lett. 41:2925-2928(2000)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  9. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. "Identification of lethal mutations in Escherichia coli genes encoding enzymes of the methylerythritol phosphate pathway."
    Sauret-Gueeto S., Ramos-Valdivia A., Ibanez E., Boronat A., Rodriguez-Concepcion M.
    Biochem. Biophys. Res. Commun. 307:408-415(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-239 AND THR-240.

Entry informationi

Entry nameiISPE_ECOLI
AccessioniPrimary (citable) accession number: P62615
Secondary accession number(s): P24209
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: October 29, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be an isopentenyl monophosphate kinase.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3