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Protein

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

Gene

ispD

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Unreviewed-Annotation score: Annotation score: 3 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 annotationSAAS annotation

Catalytic activityi

CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol.UniRule annotationSAAS 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 annotationSAAS 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), 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 (ispH1), 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
Binding sitei22 – 221CTPCombined sources
Sitei22 – 221Transition state stabilizerUniRule annotation
Binding sitei82 – 821CTPCombined sources
Sitei150 – 1501Positions MEP for the nucleophilic attackUniRule annotation
Binding sitei204 – 2041CTPCombined sources
Sitei204 – 2041Positions MEP for the nucleophilic attackUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 158CTPCombined sources
Nucleotide bindingi76 – 783CTPCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

NucleotidyltransferaseUniRule annotationSAAS annotationImported, Transferase

Keywords - Biological processi

Isoprene biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciMSME246196:GJ4Y-6075-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
Gene namesi
Name:ispDUniRule annotationImported
Ordered Locus Names:MSMEG_6076Imported, MSMEI_5916Imported
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)Imported
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000006158 Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi246196.MSMEG_6076.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XWLX-ray1.49A/B1-219[»]
2XWMX-ray1.80A/B1-219[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the IspD family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiENOG4105CE5. Bacteria.
COG1211. LUCA.
HOGENOMiHOG000218563.
KOiK00991.
OMAiQAYTPQM.
OrthoDBiEOG6B3662.

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.

A0R560-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVAVVPAA GSGERLRAGR PKAFVTLGGT PLLEHALSGL RASGVIDRIV
60 70 80 90 100
IAVPPALTDE SKLVFGGEDS VIVSGGVDRT ESVALALEAA GDAEFVLVHD
110 120 130 140 150
AARALTPPAL IARVVAALKE GHSAVVPGLA PADTIKAVDA NGAVLGTPER
160 170 180 190 200
AGLRAVQTPQ GFHADVLRRA YARATAGGVT DDASLVEQLG TPVQIVDGDP
210 220
LAFKITTPLD LVLAEAVLAR GA
Length:222
Mass (Da):22,378
Last modified:January 9, 2007 - v1
Checksum:i0A22A8EE2B8670AC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK71879.1.
CP001663 Genomic DNA. Translation: AFP42349.1.
RefSeqiWP_011731019.1. NZ_CP009494.1.
YP_890298.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK71879; ABK71879; MSMEG_6076.
AFP42349; AFP42349; MSMEI_5916.
GeneIDi4536829.
KEGGimsb:LJ00_30045.
msg:MSMEI_5916.
msm:MSMEG_6076.
PATRICi18084389. VBIMycSme59918_5914.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK71879.1.
CP001663 Genomic DNA. Translation: AFP42349.1.
RefSeqiWP_011731019.1. NZ_CP009494.1.
YP_890298.1. NC_008596.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XWLX-ray1.49A/B1-219[»]
2XWMX-ray1.80A/B1-219[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_6076.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK71879; ABK71879; MSMEG_6076.
AFP42349; AFP42349; MSMEI_5916.
GeneIDi4536829.
KEGGimsb:LJ00_30045.
msg:MSMEI_5916.
msm:MSMEG_6076.
PATRICi18084389. VBIMycSme59918_5914.

Phylogenomic databases

eggNOGiENOG4105CE5. Bacteria.
COG1211. LUCA.
HOGENOMiHOG000218563.
KOiK00991.
OMAiQAYTPQM.
OrthoDBiEOG6B3662.

Enzyme and pathway databases

UniPathwayiUPA00056; UER00093.
BioCyciMSME246196:GJ4Y-6075-MONOMER.

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. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MC2 155Imported.
  2. Hayward D., Fahey B.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155Imported and MC2 155Imported.
  3. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
    Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.M.
    Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155Imported and MC2 155Imported.
  4. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
    Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
    Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155Imported and MC2 155Imported.

Entry informationi

Entry nameiA0R560_MYCS2
AccessioniPrimary (citable) accession number: A0R560
Entry historyi
Integrated into UniProtKB/TrEMBL: January 9, 2007
Last sequence update: January 9, 2007
Last modified: June 8, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.