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P9WP28

- DAGK_MYCTO

UniProt

P9WP28 - DAGK_MYCTO

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Protein

Diacylglycerol kinase

Gene

dagK

Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of diacylglycerol (DAG) into phosphatidic acid. Is involved in the biosynthesis of phosphatidylinositol mannosides (PIMs), probably via a role in the biosynthesis of phosphatidylinositol (PI), a PIM precursor, which is derived from phosphatidic acid. Is also able to phosphorylate other various amphipathic lipids of host and bacterial origin in vitro, such as ceramide.1 Publication

Catalytic activityi

ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate.1 Publication

Cofactori

Mg2+By similarityNote: Binds 1 Mg(2+) ion per subunit. This ion appears to have a structural role and is required for catalytic activity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei101 – 1011ATPPROSITE-ProRule annotation
Metal bindingi226 – 2261Magnesium; via carbonyl oxygenBy similarity
Metal bindingi229 – 2291MagnesiumBy similarity
Metal bindingi231 – 2311Magnesium; via carbonyl oxygenBy similarity
Active sitei285 – 2851Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 235ATPPROSITE-ProRule annotation
Nucleotide bindingi76 – 827ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. diacylglycerol kinase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
  4. NAD+ kinase activity Source: InterPro

GO - Biological processi

  1. phospholipid biosynthetic process Source: UniProtKB-KW
  2. protein kinase C-activating G-protein coupled receptor signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Diacylglycerol kinase (EC:2.7.1.107)
Short name:
DAG kinase
Short name:
DAGK
Gene namesi
Name:dagK
Ordered Locus Names:MT2312
OrganismiMycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Taxonomic identifieri83331 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001020: Chromosome

Subcellular locationi

Secretedcell wall Curated

GO - Cellular componenti

  1. cell wall Source: UniProtKB-KW
  2. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene exhibit a disruption of the production of certain higher-order phosphatidylinositol mannosides (PIMs) species.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Diacylglycerol kinasePRO_0000427024Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP9WP28.
SMRiP9WP28. Positions 34-306.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 140132DAGKcPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the diacylglycerol/lipid kinase family.Curated
Contains 1 DAGKc domain.PROSITE-ProRule annotation

Family and domain databases

InterProiIPR016064. ATP-NAD_kinase_PpnK-typ.
IPR005218. Diacylglycerol/lipid_kinase.
IPR001206. Diacylglycerol_kinase_cat_dom.
[Graphical view]
PfamiPF00781. DAGK_cat. 1 hit.
[Graphical view]
SMARTiSM00046. DAGKc. 1 hit.
[Graphical view]
SUPFAMiSSF111331. SSF111331. 1 hit.
TIGRFAMsiTIGR00147. TIGR00147. 1 hit.
PROSITEiPS50146. DAGK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P9WP28-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAGQLRRHE IGKVTALTNP LSGHGAAVKA AHGAIARLKH RGVDVVEIVG
60 70 80 90 100
GDAHDARHLL AAAVAKGTDA VMVTGGDGVV SNALQVLAGT DIPLGIIPAG
110 120 130 140 150
TGNDHAREFG LPTKNPKAAA DIVVDGWTET IDLGRIQDDN GIEKWFGTVA
160 170 180 190 200
ATGFDSLVND RANRMRWPHG RMRYYIAMLA ELSRLRPLPF RLVLDGTEEI
210 220 230 240 250
VADLTLADFG NTRSYGGGLL ICPNADHSDG LLDITMAQSD SRTKLLRLFP
260 270 280 290 300
TIFKGAHVEL DEVSTTRAKT VHVECPGINV YADGDFACPL PAEISAVPAA

LQVLRPRHG
Length:309
Mass (Da):32,805
Last modified:April 16, 2014 - v1
Checksum:i34F5E363D62BB284
GO

Sequence cautioni

The sequence AE000516 differs from that shown. Reason: Frameshift at position 95. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000516 Genomic DNA. No translation available.
PIRiH70861.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000516 Genomic DNA. No translation available.
PIRi H70861.

3D structure databases

ProteinModelPortali P9WP28.
SMRi P9WP28. Positions 34-306.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR016064. ATP-NAD_kinase_PpnK-typ.
IPR005218. Diacylglycerol/lipid_kinase.
IPR001206. Diacylglycerol_kinase_cat_dom.
[Graphical view ]
Pfami PF00781. DAGK_cat. 1 hit.
[Graphical view ]
SMARTi SM00046. DAGKc. 1 hit.
[Graphical view ]
SUPFAMi SSF111331. SSF111331. 1 hit.
TIGRFAMsi TIGR00147. TIGR00147. 1 hit.
PROSITEi PS50146. DAGK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CDC 1551 / Oshkosh.
  2. "M. tuberculosis Rv2252 encodes a diacylglycerol kinase involved in the biosynthesis of phosphatidylinositol mannosides (PIMs)."
    Owens R.M., Hsu F.F., VanderVen B.C., Purdy G.E., Hesteande E., Giannakas P., Sacchettini J.C., McKinney J.D., Hill P.J., Belisle J.T., Butcher B.A., Pethe K., Russell D.G.
    Mol. Microbiol. 60:1152-1163(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    Strain: CDC 1551 / Oshkosh.

Entry informationi

Entry nameiDAGK_MYCTO
AccessioniPrimary (citable) accession number: P9WP28
Secondary accession number(s): L0TAM7, O53526
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 26, 2014
This is version 7 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3