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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: 4 out of 5-Experimental evidence at protein leveli

Functioni

ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone.1 Publication

Pathwayi: glycerol degradation

This protein is involved in the pathway glycerol degradation, which is part of Polyol metabolism.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei115 – 1151ADP; via carbonyl oxygen1 Publication
Binding sitei161 – 1611ADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 407ADP1 Publication
Nucleotide bindingi78 – 792ADP1 Publication
Nucleotide bindingi174 – 1763ADP1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycerol metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciLLAC272623:GHSH-272-MONOMER.
UniPathwayiUPA00616.

Names & Taxonomyi

Protein namesi
Recommended name:
PTS-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL (EC:2.7.-.-)
Gene namesi
Name:dhaL
Ordered Locus Names:LL0249
ORF Names:L46694
OrganismiLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Taxonomic identifieri272623 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
Proteomesi
  • UP000002196 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141R → A: Reduces activity 3-fold. 1 Publication
Mutagenesisi114 – 1141R → E: Reduces activity 100-fold. 1 Publication
Mutagenesisi161 – 1611R → A: Loss of activity. 1 Publication
Mutagenesisi164 – 1641Y → A: Reduces activity about 20-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 192192PTS-dependent dihydroxyacetone kinase, ADP-binding subunit DhaLPRO_0000270535Add
BLAST

Proteomic databases

PaxDbiQ9CIV7.

Expressioni

Inductioni

Induced by dihydroxyacetone via the DhaQ-DhaS complex.

Interactioni

Subunit structurei

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

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2017Combined sources
Helixi22 – 287Combined sources
Turni29 – 324Combined sources
Helixi37 – 5418Combined sources
Helixi60 – 7415Combined sources
Helixi79 – 9416Combined sources
Helixi100 – 11516Combined sources
Beta strandi121 – 1233Combined sources
Helixi125 – 13612Combined sources
Helixi142 – 15110Combined sources
Helixi152 – 1543Combined sources
Helixi161 – 1699Combined sources
Helixi175 – 19117Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9CIV7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 189185DhaLPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 DhaL domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108UTZ. Bacteria.
COG2376. LUCA.
HOGENOMiHOG000226525.
KOiK05879.
OMAiMAKGFGM.
OrthoDBiEOG65J57G.

Family and domain databases

InterProiIPR012737. DhaK_L_YcgS.
IPR004007. DhaL_dom.
[Graphical view]
PfamiPF02734. Dak2. 1 hit.
[Graphical view]
SMARTiSM01120. Dak2. 1 hit.
[Graphical view]
SUPFAMiSSF101473. SSF101473. 1 hit.
TIGRFAMsiTIGR02365. dha_L_ycgS. 1 hit.
PROSITEiPS51480. DHAL. 1 hit.
[Graphical view]

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.
PATRICi22292678. VBILacLac136773_0274.

Cross-referencesi

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.

3D structure databases

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

Protein-protein interaction databases

STRINGi272623.L46694.

Proteomic databases

PaxDbiQ9CIV7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK04347; AAK04347; L46694.
GeneIDi1113859.
KEGGilla:L46694.
PATRICi22292678. VBILacLac136773_0274.

Phylogenomic databases

eggNOGiENOG4108UTZ. Bacteria.
COG2376. LUCA.
HOGENOMiHOG000226525.
KOiK05879.
OMAiMAKGFGM.
OrthoDBiEOG65J57G.

Enzyme and pathway databases

UniPathwayiUPA00616.
BioCyciLLAC272623:GHSH-272-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9CIV7.

Family and domain databases

InterProiIPR012737. DhaK_L_YcgS.
IPR004007. DhaL_dom.
[Graphical view]
PfamiPF02734. Dak2. 1 hit.
[Graphical view]
SMARTiSM01120. Dak2. 1 hit.
[Graphical view]
SUPFAMiSSF101473. SSF101473. 1 hit.
TIGRFAMsiTIGR02365. dha_L_ycgS. 1 hit.
PROSITEiPS51480. DHAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403."
    Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A.
    Genome Res. 11:731-753(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: IL1403.
  2. "X-ray structures of the three Lactococcus lactis dihydroxyacetone kinase subunits and of a transient intersubunit complex."
    Zurbriggen A., Jeckelmann J.M., Christen S., Bieniossek C., Baumann U., Erni B.
    J. Biol. Chem. 283:35789-35796(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-192 IN COMPLEX WITH ADP AND MAGNESIUM IONS, FUNCTION, MUTAGENESIS OF ARG-114; ARG-161 AND TYR-164.

Entry informationi

Entry nameiDHAL_LACLA
AccessioniPrimary (citable) accession number: Q9CIV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 74 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.