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Q976J8

- LYSW_SULTO

UniProt

Q976J8 - LYSW_SULTO

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Protein

Alpha-aminoadipate/glutamate carrier protein LysW

Gene

lysW

Organism
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi6 – 61Zinc
Metal bindingi9 – 91Zinc
Metal bindingi27 – 271Zinc
Metal bindingi29 – 291Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1 – 3434TFIIB-typeAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine biosynthetic process Source: UniProtKB-UniPathway
  2. lysine biosynthetic process via aminoadipic acid Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Lysine biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciSTOK273063:GJC7-212-MONOMER.
UniPathwayiUPA00033.
UPA00068.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-aminoadipate/glutamate carrier protein LysW
Alternative name(s):
AAA carrier protein LysW
Gene namesi
Name:lysW
Ordered Locus Names:STK_01925
ORF Names:STS023
OrganismiSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Taxonomic identifieri273063 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001015: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5656Alpha-aminoadipate/glutamate carrier protein LysWPRO_0000084538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 5615-glutamyl 2-aminoadipic acid; alternate
Modified residuei56 – 5615-glutamyl glutamate; alternate
Modified residuei56 – 5615-glutamyl N2-lysine; alternateCurated
Modified residuei56 – 5615-glutamyl N2-ornithine; alternateCurated

Post-translational modificationi

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 (PubMed:23434852).1 Publication

Keywords - PTMi

Isopeptide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi273063.STS023.

Structurei

Secondary structure

1
56
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54
Turni7 – 93
Beta strandi12 – 154
Beta strandi24 – 263
Beta strandi32 – 387
Beta strandi41 – 466

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VPBX-ray1.80E/F1-56[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi50 – 501EDWGE

Sequence similaritiesi

Contains 1 TFIIB-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1 – 3434TFIIB-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG252918.
HOGENOMiHOG000105320.
KOiK05826.
OMAiEIVEHEC.

Sequencei

Sequence statusi: Complete.

Q976J8 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVVLKCPVCN GDVNVPDDAL PGEIVEHECG AQLEVYNDHG RLALRLAEQV

GEDWGE
Length:56
Mass (Da):6,104
Last modified:December 1, 2001 - v1
Checksum:iC72792074AD8585A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000023 Genomic DNA. Translation: BAB65149.1.
RefSeqiNP_376040.1. NC_003106.2.

Genome annotation databases

EnsemblBacteriaiBAB65149; BAB65149; STK_01925.
GeneIDi1458077.
KEGGisto:STS023.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000023 Genomic DNA. Translation: BAB65149.1 .
RefSeqi NP_376040.1. NC_003106.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3VPB X-ray 1.80 E/F 1-56 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273063.STS023.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB65149 ; BAB65149 ; STK_01925 .
GeneIDi 1458077.
KEGGi sto:STS023.

Phylogenomic databases

eggNOGi NOG252918.
HOGENOMi HOG000105320.
KOi K05826.
OMAi EIVEHEC.

Enzyme and pathway databases

UniPathwayi UPA00033 .
UPA00068 .
BioCyci STOK273063:GJC7-212-MONOMER.

Family and domain databases

ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 16993 / JCM 10545 / NBRC 100140 / 7.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ZINC AND ARGX, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiLYSW_SULTO
AccessioniPrimary (citable) accession number: Q976J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: December 1, 2001
Last modified: October 1, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds zinc ions via its zinc finger domain, as shown by X-ray crystallography (PubMed:23434852). In contrast, the absorption spectrum of the ortholog from Thermophilus suggests that it may bind iron ions, possibly via the predicted zinc finger domain.1 Publication

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

External Data

Dasty 3