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Protein

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase

Gene

ispD

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).UniRule annotation

Catalytic activityi

CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol.UniRule annotation

Pathwayi: isopentenyl diphosphate biosynthesis via DXP pathway

This protein is involved in step 2 of the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr)
  2. 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD)
  3. 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE)
  4. 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF)
  5. 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG)
  6. 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH)
This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via DXP pathway, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate, the pathway isopentenyl diphosphate biosynthesis via DXP pathway and in Isoprenoid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei15 – 151Transition state stabilizerUniRule annotation
Sitei21 – 211Transition state stabilizerUniRule annotation
Sitei138 – 1381Positions MEP for the nucleophilic attackUniRule annotation
Sitei194 – 1941Positions MEP for the nucleophilic attackUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Isoprene biosynthesis

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-180-MONOMER.
UniPathwayiUPA00056; UER00093.

Names & Taxonomyi

Protein namesi
Recommended name:
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferaseUniRule annotation (EC:2.7.7.60UniRule annotation)
Alternative name(s):
4-diphosphocytidyl-2C-methyl-D-erythritol synthaseUniRule annotation
MEP cytidylyltransferaseUniRule annotation
Short name:
MCTUniRule annotation
Gene namesi
Name:ispDUniRule annotation
Ordered Locus Names:TTHA0171
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2132132-C-methyl-D-erythritol 4-phosphate cytidylyltransferasePRO_0000075640Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA0171.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi21 – 233Combined sources
Beta strandi27 – 304Combined sources
Helixi31 – 388Combined sources
Turni39 – 413Combined sources
Beta strandi43 – 497Combined sources
Beta strandi62 – 654Combined sources
Helixi70 – 8011Combined sources
Beta strandi83 – 886Combined sources
Helixi98 – 11114Combined sources
Beta strandi112 – 1198Combined sources
Beta strandi122 – 1276Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi133 – 1364Combined sources
Helixi138 – 1403Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi148 – 1514Combined sources
Helixi152 – 16514Combined sources
Helixi172 – 1787Combined sources
Beta strandi184 – 1874Combined sources
Helixi198 – 20811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PX7X-ray2.20A/B1-213[»]
ProteinModelPortaliQ5SLX2.
SMRiQ5SLX2. Positions 1-210.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SLX2.

Family & Domainsi

Sequence similaritiesi

Belongs to the IspD family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CE5. Bacteria.
COG1211. LUCA.
HOGENOMiHOG000218563.
KOiK00991.
OMAiGYGMPKA.
OrthoDBiEOG6B3662.
PhylomeDBiQ5SLX2.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_00108. IspD.
InterProiIPR001228. IspD.
IPR018294. ISPD_synthase_CS.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01128. IspD. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR00453. ispD. 1 hit.
PROSITEiPS01295. ISPD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SLX2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVSVLIPAA GNGLRLGRGP KAFLQVGGRT LLEWTLAAFR DAAEVLVALP
60 70 80 90 100
PGAEPPKGLG AVFLEGGATR QASVARLLEA ASLPLVLVHD VARPFVSRGL
110 120 130 140 150
VARVLEAAQR SGAAVPVLPV PDTLMAPEGE AYGRVVPREA FRLVQTPQGF
160 170 180 190 200
FTALLREAHA YARRKGLEAS DDAQLVQALG YPVALVEGEA TAFKITHPQD
210
LVLAEALARV WSA
Length:213
Mass (Da):22,423
Last modified:December 21, 2004 - v1
Checksum:i1CA594359920EF7A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD69994.1.
RefSeqiWP_011174170.1. NC_006461.1.
YP_143437.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD69994; BAD69994; BAD69994.
GeneIDi3169663.
KEGGittj:TTHA0171.
PATRICi23955283. VBITheThe93045_0169.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD69994.1.
RefSeqiWP_011174170.1. NC_006461.1.
YP_143437.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PX7X-ray2.20A/B1-213[»]
ProteinModelPortaliQ5SLX2.
SMRiQ5SLX2. Positions 1-210.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0171.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD69994; BAD69994; BAD69994.
GeneIDi3169663.
KEGGittj:TTHA0171.
PATRICi23955283. VBITheThe93045_0169.

Phylogenomic databases

eggNOGiENOG4105CE5. Bacteria.
COG1211. LUCA.
HOGENOMiHOG000218563.
KOiK00991.
OMAiGYGMPKA.
OrthoDBiEOG6B3662.
PhylomeDBiQ5SLX2.

Enzyme and pathway databases

UniPathwayiUPA00056; UER00093.
BioCyciTTHE300852:GH8R-180-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SLX2.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_00108. IspD.
InterProiIPR001228. IspD.
IPR018294. ISPD_synthase_CS.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01128. IspD. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR00453. ispD. 1 hit.
PROSITEiPS01295. ISPD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "Crystal structure of 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase from Thermus thermophilus HB8."
    Southeast collaboratory for structural genomics (SECSG)
    Submitted (JUN-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiISPD_THET8
AccessioniPrimary (citable) accession number: Q5SLX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: December 21, 2004
Last modified: November 11, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.