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Protein

PTS-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL

Gene

dhaL

Organism
Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone binds to DhaK.1 Publication

Miscellaneous

Unlike the carbohydrate-specific transporters of the PTS, the complex DhaKML has no transport activity.1 Publication

Catalytic activityi

Phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate.By similarity

Cofactori

Mg2+1 Publication

Pathwayi: glycerol degradation

This protein is involved in the pathway glycerol degradation, which is part of Polyol metabolism.Curated
View all proteins of this organism that are known to be involved in the pathway glycerol degradation and in Polyol metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi29MagnesiumCombined sources1 Publication1
Metal bindingi34MagnesiumCombined sources1 Publication1
Metal bindingi36MagnesiumCombined sources1 Publication1
Binding sitei115ADP; via carbonyl oxygenCombined sources1 Publication1
Binding sitei124ADP; via amide nitrogenCombined sources1 Publication1
Binding sitei161ADP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi37 – 40ADPCombined sources1 Publication4
Nucleotide bindingi78 – 79ADPCombined sources1 Publication2
Nucleotide bindingi174 – 176ADPCombined sources1 Publication3

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • glycerone kinase activity Source: InterPro
  • magnesium ion binding Source: UniProtKB
  • phosphoenolpyruvate-glycerone phosphotransferase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionKinase, Transferase
Biological processGlycerol metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00616.

Names & Taxonomyi

Protein namesi
Recommended name:
PTS-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL1 Publication (EC:2.7.1.121By similarity)
Gene namesi
Name:dhaL1 Publication
Ordered Locus Names:LL0249
ORF Names:L46694
OrganismiLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Taxonomic identifieri272623 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
Proteomesi
  • UP000002196 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi114R → A: Reduces activity 3-fold. 1 Publication1
Mutagenesisi114R → E: Reduces activity 100-fold. 1 Publication1
Mutagenesisi161R → A: Loss of activity. 1 Publication1
Mutagenesisi164Y → A: Reduces activity about 20-fold. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002705351 – 192PTS-dependent dihydroxyacetone kinase, ADP-binding subunit DhaLAdd BLAST192

Proteomic databases

PaxDbiQ9CIV7.

Expressioni

Inductioni

Induced by dihydroxyacetone via the DhaQ-DhaS complex.1 Publication

Interactioni

Subunit structurei

Homodimer. The dihydroxyacetone kinase complex is composed of a homodimer of DhaM, a homodimer of DhaK and the subunit DhaL.1 Publication

Protein-protein interaction databases

STRINGi272623.L46694.

Structurei

Secondary structure

1192
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 20Combined sources17
Helixi22 – 28Combined sources7
Turni29 – 32Combined sources4
Helixi37 – 54Combined sources18
Helixi60 – 74Combined sources15
Helixi79 – 94Combined sources16
Helixi100 – 115Combined sources16
Beta strandi121 – 123Combined sources3
Helixi125 – 136Combined sources12
Helixi142 – 151Combined sources10
Helixi152 – 154Combined sources3
Helixi161 – 169Combined sources9
Helixi175 – 191Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CR3X-ray2.10A/B2-192[»]
ProteinModelPortaliQ9CIV7.
SMRiQ9CIV7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CIV7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 189DhaLPROSITE-ProRule annotationAdd BLAST185

Phylogenomic databases

eggNOGiENOG4108UTZ. Bacteria.
COG2376. LUCA.
HOGENOMiHOG000226525.
KOiK05879.
OMAiGENVDRG.

Family and domain databases

InterProiView protein in InterPro
IPR012737. DhaK_L_YcgS.
IPR004007. DhaL_dom.
PfamiView protein in Pfam
PF02734. Dak2. 1 hit.
SMARTiView protein in SMART
SM01120. Dak2. 1 hit.
SUPFAMiSSF101473. SSF101473. 1 hit.
TIGRFAMsiTIGR02365. dha_L_ycgS. 1 hit.
PROSITEiView protein in PROSITE
PS51480. DHAL. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CIV7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTIDTTIEW LGKFNEKIQE NKAYLSELDG PIGDGDHGAN MARGMSETMK
60 70 80 90 100
ALEVSNFGNV SEIFKKVAMT LMSKVGGASG PLYGSAFLAM SKTAIETLDT
110 120 130 140 150
SELIYAGLEA IQKRGKAQVG EKTMVDIWSA FLNDLQTDSA SKDNLEKVVK
160 170 180 190
ASAGLLATKG RASYLGERSI GHIDPGTQSS AYLFETLLEV VA
Length:192
Mass (Da):20,578
Last modified:June 1, 2001 - v1
Checksum:i7609CBD5D97D1751
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005176 Genomic DNA. Translation: AAK04347.1.
PIRiA86656.
RefSeqiNP_266405.1. NC_002662.1.
WP_010905236.1. NC_002662.1.

Genome annotation databases

EnsemblBacteriaiAAK04347; AAK04347; L46694.
GeneIDi1113859.
KEGGilla:L46694.
PATRICifig|272623.7.peg.274.

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.

Entry informationi

Entry nameiDHAL_LACLA
AccessioniPrimary (citable) accession number: Q9CIV7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: June 1, 2001
Last modified: June 7, 2017
This is version 80 of the entry and version 1 of the sequence. See 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