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Q976J8 (LYSW_SULTO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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/glutamate carrier protein LysW
Alternative name(s):
AAA carrier protein LysW
Gene names
Name:lysW
Ordered Locus Names:STK_01925
ORF Names:STS023
OrganismSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) [Complete proteome] [HAMAP]
Taxonomic identifier273063 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length56 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Carrier protein that bears the covalently bound substrates for arginine and lysine biosynthesis; bound L-glutamate is sequentially converted to L-ornithine, while bound alpha-aminoadipate (AAA) is sequentially converted to L-lysine. Ref.2

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway.

Amino-acid biosynthesis; L-arginine biosynthesis.

Subunit structure

Monomer. Ref.2

Post-translational modification

Formation of an isopeptide bond between the gamma-carboxyl group of the C-terminal glutamate and the amino group of alpha-aminoadipate (AAA) is catalyzed by LysX. The bound AAA is then converted to L-lysine in a series of reactions catalyzed by LysZ, LysY and LysJ. Release of the product L-lysine is catalyzed by LysK. Formation of an isopeptide bond between the gamma-carboxyl group of the C-terminal glutamate and the amino group of L-glutamate is catalyzed by ArgX. The bound substrate is then sequentially converted to ornithine which is eventually converted to L-arginine (Ref.2).

Miscellaneous

Binds zinc ions via its zinc finger domain, as shown by X-ray crystallography (Ref.2). In contrast, the absorption spectrum of the ortholog from Thermophilus suggests that it may bind iron ions, possibly via the predicted zinc finger domain.

Sequence similarities

Contains 1 TFIIB-type zinc finger.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5656Alpha-aminoadipate/glutamate carrier protein LysW
PRO_0000084538

Regions

Zinc finger1 – 3434TFIIB-type
Motif501EDWGE

Sites

Metal binding61Zinc
Metal binding91Zinc
Metal binding271Zinc
Metal binding291Zinc

Amino acid modifications

Modified residue5615-glutamyl 2-aminoadipic acid; alternate
Modified residue5615-glutamyl glutamate; alternate
Modified residue5615-glutamyl N2-lysine; alternate Probable
Modified residue5615-glutamyl N2-ornithine; alternate Probable

Secondary structure

............. 56
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q976J8 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: C72792074AD8585A

FASTA566,104
        10         20         30         40         50 
MVVLKCPVCN GDVNVPDDAL PGEIVEHECG AQLEVYNDHG RLALRLAEQV GEDWGE 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7."
Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.
DNA Res. 8:123-140(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 16993 / JCM 10545 / NBRC 100140 / 7.
[2]"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 (1.8 ANGSTROMS) IN COMPLEXES WITH ZINC AND ARGX, FUNCTION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000023 Genomic DNA. Translation: BAB65149.1.
RefSeqNP_376040.1. NC_003106.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3VPBX-ray1.80E/F1-56[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273063.STS023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB65149; BAB65149; STK_01925.
GeneID1458077.
KEGGsto:STS023.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG252918.
HOGENOMHOG000105320.
KOK05826.
OMAEIVEHEC.
ProtClustDBCLSK802585.

Enzyme and pathway databases

BioCycSTOK273063:GJC7-212-MONOMER.
UniPathwayUPA00033.
UPA00068.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameLYSW_SULTO
AccessionPrimary (citable) accession number: Q976J8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 58 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