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Q5SH23 (LYSX_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-aminoadipate--LysW ligase LysX

Short name=AAA--LysW ligase LysX
EC=6.3.2.n4
Gene names
Name:lysX
Ordered Locus Names:TTHA1907
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length280 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the ATP-dependent formation of a covalent bond between the amino group of alpha-aminoadipate (AAA) and the gamma-carboxyl group of the C-terminal glutamate residue in LysW. Ref.3

Catalytic activity

ATP + [LysW] + L-2-aminoadipate = ADP + phosphate + [LysW]-L-2-aminoadipate. Ref.3

Cofactor

Binds 2 magnesium ions per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 1/5.

Subunit structure

Homodimer. Ref.1

Sequence similarities

Belongs to the RimK family. LysX subfamily.

Contains 1 ATP-grasp domain.

Biophysicochemical properties

Kinetic parameters:

KM=2.1 mM for alpha-aminoadipate Ref.3

KM=2.6 mM for ATP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 280280Alpha-aminoadipate--LysW ligase LysX
PRO_0000391001

Regions

Domain93 – 276184ATP-grasp
Nucleotide binding133 – 1397ATP
Nucleotide binding169 – 18012ATP
Motif258 – 2592N-[TS] motif that is essential for LysX substrate specificity

Sites

Metal binding2371Magnesium 1 By similarity
Metal binding2491Magnesium 1 By similarity
Metal binding2491Magnesium 2 By similarity
Metal binding2511Magnesium 2 By similarity
Binding site891ATP By similarity
Binding site1291ATP
Binding site1941ATP
Binding site2021ATP By similarity

Secondary structure

.................................................... 280
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5SH23 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: B168629146AF1344

FASTA28030,718
        10         20         30         40         50         60 
MLAILYDRIR PDERMLFERA EALGLPYKKV YVPALPMVLG ERPKELEGVT VALERCVSQS 

        70         80         90        100        110        120 
RGLAAARYLT ALGIPVVNRP EVIEACGDKW ATSVALAKAG LPQPKTALAT DREEALRLME 

       130        140        150        160        170        180 
AFGYPVVLKP VIGSWGRLLA KVTDRAAAEA LLEHKEVLGG FQHQLFYIQE YVEKPGRDIR 

       190        200        210        220        230        240 
VFVVGERAIA AIYRRSAHWI TNTARGGQAE NCPLTEEVAR LSVKAAEAVG GGVVAVDLFE 

       250        260        270        280 
SERGLLVNEV NHTMEFKNSV HTTGVDIPGE ILKYAWSLAS 

« Hide

References

« Hide 'large scale' references
[1]"Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus thermophilus HB8."
Sakai H., Vassylyeva M.N., Matsuura T., Sekine S., Gotoh K., Nishiyama M., Terada T., Shirouzu M., Kuramitsu S., Vassylyev D.G., Yokoyama S.
J. Mol. Biol. 332:729-740(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP, SUBUNIT.
Strain: HB8 / ATCC 27634 / DSM 579.
[2]"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.
[3]"Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus."
Horie A., Tomita T., Saiki A., Kono H., Taka H., Mineki R., Fujimura T., Nishiyama C., Kuzuyama T., Nishiyama M.
Nat. Chem. Biol. 5:673-679(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[4]"Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus."
Ouchi T., Tomita T., Horie A., Yoshida A., Takahashi K., Nishida H., Lassak K., Taka H., Mineki R., Fujimura T., Kosono S., Nishiyama C., Masui R., Kuramitsu S., Albers S.V., Kuzuyama T., Nishiyama M.
Nat. Chem. Biol. 9:277-283(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ATP ANALOG.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB103032 Genomic DNA. Translation: BAC67243.1.
AP008226 Genomic DNA. Translation: BAD71730.1.
RefSeqYP_145173.1. NC_006461.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UC8X-ray2.00A/B1-280[»]
1UC9X-ray2.38A/B1-280[»]
3VPDX-ray1.95A/B1-279[»]
ProteinModelPortalQ5SH23.
SMRQ5SH23. Positions 1-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA1907.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71730; BAD71730; BAD71730.
GeneID3167971.
KEGGttj:TTHA1907.
PATRIC23958779. VBITheThe93045_1875.

Phylogenomic databases

eggNOGCOG0189.
HOGENOMHOG000228553.
KOK05827.
OMAACMERIA.
OrthoDBEOG6DZDX8.
PhylomeDBQ5SH23.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-6728.
TTHE300852:GH8R-1953-MONOMER.
UniPathwayUPA00033; UER00035.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProIPR011761. ATP-grasp.
IPR013651. ATP-grasp_RimK-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR011870. LysX_arch.
IPR016185. PreATP-grasp_dom.
IPR004666. RpS6_RimK/Lys_biosynth_LsyX.
[Graphical view]
PfamPF08443. RimK. 1 hit.
[Graphical view]
SUPFAMSSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR02144. LysX_arch. 1 hit.
TIGR00768. rimK_fam. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5SH23.

Entry information

Entry nameLYSX_THET8
AccessionPrimary (citable) accession number: Q5SH23
Secondary accession number(s): Q84BR0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways