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Entry version 114 (13 Nov 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Cysteine synthase A

Gene

cysK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

(Microbial infection) In addition to its role in cysteine synthesis, stimulates the tRNase activity of CdiA-CT from E.coli strain 536 / UPEC; stimulation does not require O-acetylserine sulfhydrylase activity. CdiA is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (experiments done in strains BW25113 and X90, both K12 derivatives). This protein is not required for CDI of strain EC93, whose toxin may function by forming inner cell membrane pores (PubMed:22333533). CysK stabilizes CdiA-CT, allowing it to bind tRNA substrate; neither CdiA-CT nor CysK bind tRNA alone in vitro (PubMed:27531961).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pyridoxal 5'-phosphate2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=40 mM for 3-chloro-L-alanine1 Publication
  2. KM=15.4 mM for thioglycolate1 Publication

    pH dependencei

    Optimum pH is 9-10.5.1 Publication

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-cysteine biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes L-cysteine from L-serine.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Serine acetyltransferase (cysE)
    2. Cysteine synthase A (cysK), Cysteine synthase B (cysM)
    This subpathway is part of the pathway L-cysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-cysteine from L-serine, the pathway L-cysteine biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei8Allosteric inhibitorBy similarity1
    Binding sitei72Pyridoxal phosphateBy similarity1
    Binding sitei269Allosteric inhibitor; via amide nitrogenBy similarity1
    Binding sitei273Pyridoxal phosphateBy similarity1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAllosteric enzyme, Lyase, Transferase
    Biological processAmino-acid biosynthesis, Cysteine biosynthesis
    LigandPyridoxal phosphate

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:ACSERLYA-MONOMER
    ECOL316407:JW2407-MONOMER
    MetaCyc:ACSERLYA-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P0ABK5

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00136;UER00200

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Cysteine synthase A (EC:2.5.1.47)
    Short name:
    CSase A
    Alternative name(s):
    O-acetylserine (thiol)-lyase A
    Short name:
    OAS-TL A
    O-acetylserine sulfhydrylase A
    S-carboxymethylcysteine synthase (EC:4.5.1.51 Publication)
    Sulfate starvation-induced protein 5
    Short name:
    SSI5
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:cysK
    Synonyms:cysZ
    Ordered Locus Names:b2414, JW2407
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Significant decrease in tRNA nuclease activity of contact-dependent growth inhibitor CdiA-CT from strain 536 / UPEC (deletion in strain BW25113).2 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi42K → A: Still stimulates tRNase activity of CdiA-CT in vitro and in vivo. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved5 Publications
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001670862 – 323Cysteine synthase AAdd BLAST322

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei42N6-(pyridoxal phosphate)lysine1 Publication1

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P0ABK5

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0ABK5

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P0ABK5

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0ABK5

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...
    SWISS-2DPAGEi
    P0ABK5

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Repressed by sulfate or cysteine.

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer (Ref. 6, PubMed:27531961).

    Forms a cysteine synthase complex with 1 copy of CysE (By similarity).

    By similarity3 Publications

    (Microbial infection) Interacts with CdiA-CT from strain 536 / UPEC, this is blocked upon preincubation with O-acetyl-L-serine. CysK forms a complex with CdiA-CT/CdiI (PubMed:22333533). One CdiA toxin subunit binds to each subunit of the CysK homodimer, and one CdiI immunity protein binds to each toxin subunit; the immune complex is thus a dimer of trimers. The 4 C-terminal residues of CdiA fit into the active site of CysK (PubMed:27531961).

    2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4259701, 23 interactors
    851217, 1 interactor

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-3742 cysEK cysteine synthase complex

    Database of interacting proteins

    More...
    DIPi
    DIP-36170N

    Protein interaction database and analysis system

    More...
    IntActi
    P0ABK5, 14 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b2414

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P0ABK5

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni177 – 181Pyridoxal phosphate bindingBy similarity5

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105C6T Bacteria
    COG0031 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000217394

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0ABK5

    KEGG Orthology (KO)

    More...
    KOi
    K01738

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0ABK5

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.1100, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR005856 Cys_synth
    IPR005859 CysK
    IPR001216 P-phosphate_BS
    IPR001926 PLP-dep
    IPR036052 Trypto_synt_PLP_dependent

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00291 PALP, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53686 SSF53686, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01139 cysK, 1 hit
    TIGR01136 cysKM, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00901 CYS_SYNTHASE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P0ABK5-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSKIFEDNSL TIGHTPLVRL NRIGNGRILA KVESRNPSFS VKCRIGANMI
    60 70 80 90 100
    WDAEKRGVLK PGVELVEPTS GNTGIALAYV AAARGYKLTL TMPETMSIER
    110 120 130 140 150
    RKLLKALGAN LVLTEGAKGM KGAIQKAEEI VASNPEKYLL LQQFSNPANP
    160 170 180 190 200
    EIHEKTTGPE IWEDTDGQVD VFIAGVGTGG TLTGVSRYIK GTKGKTDLIS
    210 220 230 240 250
    VAVEPTDSPV IAQALAGEEI KPGPHKIQGI GAGFIPANLD LKLVDKVIGI
    260 270 280 290 300
    TNEEAISTAR RLMEEEGILA GISSGAAVAA ALKLQEDESF TNKNIVVILP
    310 320
    SSGERYLSTA LFADLFTEKE LQQ
    Length:323
    Mass (Da):34,490
    Last modified:January 23, 2007 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i20ADDE911845AE72
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti182L → W in AAA23654 (PubMed:3290198).Curated1
    Sequence conflicti186 – 187SR → TP in AAA23654 (PubMed:3290198).Curated2

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    X12615 Genomic DNA Translation: CAA31137.1
    M21451 Genomic DNA Translation: AAA23654.1
    U00096 Genomic DNA Translation: AAC75467.1
    AP009048 Genomic DNA Translation: BAA16288.1
    M21994 Genomic DNA Translation: AAA24383.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    E65015 SYECAC

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_416909.1, NC_000913.3
    WP_000034402.1, NZ_STEB01000039.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75467; AAC75467; b2414
    BAA16288; BAA16288; BAA16288

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    946877

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW2407
    eco:b2414

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.4317

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X12615 Genomic DNA Translation: CAA31137.1
    M21451 Genomic DNA Translation: AAA23654.1
    U00096 Genomic DNA Translation: AAC75467.1
    AP009048 Genomic DNA Translation: BAA16288.1
    M21994 Genomic DNA Translation: AAA24383.1
    PIRiE65015 SYECAC
    RefSeqiNP_416909.1, NC_000913.3
    WP_000034402.1, NZ_STEB01000039.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5J43X-ray2.70A/E1-323[»]
    5J5VX-ray2.75A/D1-323[»]
    SMRiP0ABK5
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4259701, 23 interactors
    851217, 1 interactor
    ComplexPortaliCPX-3742 cysEK cysteine synthase complex
    DIPiDIP-36170N
    IntActiP0ABK5, 14 interactors
    STRINGi511145.b2414

    2D gel databases

    SWISS-2DPAGEiP0ABK5

    Proteomic databases

    EPDiP0ABK5
    jPOSTiP0ABK5
    PaxDbiP0ABK5
    PRIDEiP0ABK5

    Genome annotation databases

    EnsemblBacteriaiAAC75467; AAC75467; b2414
    BAA16288; BAA16288; BAA16288
    GeneIDi946877
    KEGGiecj:JW2407
    eco:b2414
    PATRICifig|1411691.4.peg.4317

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB0189

    Phylogenomic databases

    eggNOGiENOG4105C6T Bacteria
    COG0031 LUCA
    HOGENOMiHOG000217394
    InParanoidiP0ABK5
    KOiK01738
    PhylomeDBiP0ABK5

    Enzyme and pathway databases

    UniPathwayiUPA00136;UER00200
    BioCyciEcoCyc:ACSERLYA-MONOMER
    ECOL316407:JW2407-MONOMER
    MetaCyc:ACSERLYA-MONOMER
    SABIO-RKiP0ABK5

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P0ABK5

    Family and domain databases

    Gene3Di3.40.50.1100, 2 hits
    InterProiView protein in InterPro
    IPR005856 Cys_synth
    IPR005859 CysK
    IPR001216 P-phosphate_BS
    IPR001926 PLP-dep
    IPR036052 Trypto_synt_PLP_dependent
    PfamiView protein in Pfam
    PF00291 PALP, 1 hit
    SUPFAMiSSF53686 SSF53686, 1 hit
    TIGRFAMsiTIGR01139 cysK, 1 hit
    TIGR01136 cysKM, 1 hit
    PROSITEiView protein in PROSITE
    PS00901 CYS_SYNTHASE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

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    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCYSK_ECOLI
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0ABK5
    Secondary accession number(s): P11096, P21546
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: January 23, 2007
    Last modified: November 13, 2019
    This is version 114 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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    Main funding by: National Institutes of Health

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