Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cysteine synthase A

Gene

cysK

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Two cysteine synthase enzymes are found, this enzyme and CysM; both catalyze the same reaction. Cysteine synthase B (CysM) can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product.1 Publication

Catalytic activityi

O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate.1 Publication

Cofactori

pyridoxal 5'-phosphate2 Publications

Enzyme regulationi

O-acetyl-L-serine causes the CysE-CysK complex to dissociate in the absence of hydrogen sulfide.1 Publication

Kineticsi

  1. KM=5 mM for O-acetyl-L-serine as isolated subunit and in complex with CysK1 Publication

    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei8 – 81Allosteric inhibitor1 Publication
    Binding sitei72 – 721Pyridoxal phosphate3 Publications
    Binding sitei269 – 2691Allosteric inhibitor; via amide nitrogen1 Publication
    Binding sitei273 – 2731Pyridoxal phosphate3 Publications

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Cysteine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-2446-MONOMER.
    BRENDAi2.5.1.47. 2169.
    SABIO-RKP0A1E3.
    UniPathwayiUPA00136; UER00200.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cysteine synthase A (EC:2.5.1.471 Publication)
    Short name:
    CSase A
    Alternative name(s):
    O-acetylserine (thiol)-lyase A1 Publication
    Short name:
    OAS-TL A
    O-acetylserine sulfhydrylase A1 Publication
    Gene namesi
    Name:cysK
    Ordered Locus Names:STM2430
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    Proteomesi
    • UP000001014 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 323322Cysteine synthase APRO_0000167089Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei42 – 421N6-(pyridoxal phosphate)lysine

    Proteomic databases

    PaxDbiP0A1E3.
    PRIDEiP0A1E3.

    Interactioni

    Subunit structurei

    Part of the cysteine synthase complex formed at a ratio of 2 copies of this protein and 1 copy of serine acetyltransferase (cysE). The complex reversibly dissociates in the presence of O-acetyl-L-serine but in the absence of hydrogen sulfide (PubMed:4977445). Homodimer (PubMed:10452898, PubMed:11023792, PubMed:9761678).4 Publications

    Protein-protein interaction databases

    STRINGi99287.STM2430.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 74Combined sources
    Helixi8 – 114Combined sources
    Beta strandi17 – 193Combined sources
    Beta strandi21 – 266Combined sources
    Beta strandi28 – 325Combined sources
    Helixi37 – 393Combined sources
    Helixi42 – 5514Combined sources
    Beta strandi64 – 685Combined sources
    Helixi72 – 8413Combined sources
    Beta strandi88 – 936Combined sources
    Helixi98 – 1069Combined sources
    Beta strandi110 – 1145Combined sources
    Helixi116 – 1183Combined sources
    Helixi119 – 13214Combined sources
    Turni135 – 1373Combined sources
    Beta strandi138 – 1403Combined sources
    Turni143 – 1453Combined sources
    Helixi148 – 1558Combined sources
    Helixi157 – 1648Combined sources
    Turni165 – 1673Combined sources
    Beta strandi171 – 1755Combined sources
    Beta strandi177 – 1793Combined sources
    Helixi180 – 19011Combined sources
    Turni191 – 1933Combined sources
    Beta strandi199 – 2057Combined sources
    Helixi210 – 2156Combined sources
    Helixi241 – 2433Combined sources
    Beta strandi245 – 2506Combined sources
    Helixi252 – 26615Combined sources
    Helixi272 – 28413Combined sources
    Helixi288 – 2903Combined sources
    Beta strandi295 – 2995Combined sources
    Helixi303 – 3064Combined sources
    Helixi310 – 3123Combined sources
    Helixi318 – 3214Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D6SX-ray2.30A/B2-323[»]
    1FCJX-ray2.00A/B/C/D2-323[»]
    1OASX-ray2.20A/B2-323[»]
    ProteinModelPortaliP0A1E3.
    SMRiP0A1E3. Positions 2-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A1E3.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni177 – 1815Pyridoxal phosphate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105C6T. Bacteria.
    COG0031. LUCA.
    HOGENOMiHOG000217394.
    KOiK01738.
    OMAiVKCRIGS.
    OrthoDBiEOG6Q2SP8.
    PhylomeDBiP0A1E3.

    Family and domain databases

    InterProiIPR005856. Cys_synth.
    IPR005859. CysK.
    IPR001216. P-phosphate_BS.
    IPR001926. TrpB-like_PLP-dep.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    [Graphical view]
    SUPFAMiSSF53686. SSF53686. 1 hit.
    TIGRFAMsiTIGR01139. cysK. 1 hit.
    TIGR01136. cysKM. 1 hit.
    PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A1E3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSKIYEDNSL TIGHTPLVRL NRIGNGRILA KVESRNPSFS VKCRIGANMI
    60 70 80 90 100
    WDAEKRGVLK PGVELVEPTS GNTGIALAYV AAARGYKLTL TMPETMSIER
    110 120 130 140 150
    RKLLKALGAN LVLTEGAKGM KGAIQKAEEI VASDPQKYLL LQQFSNPANP
    160 170 180 190 200
    EIHEKTTGPE IWEDTDGQVD VFISGVGTGG TLTGVTRYIK GTKGKTDLIT
    210 220 230 240 250
    VAVEPTDSPV IAQALAGEEI KPGPHKIQGI GAGFIPGNLD LKLIDKVVGI
    260 270 280 290 300
    TNEEAISTAR RLMEEEGILA GISSGAAVAA ALKLQEDESF TNKNIVVILP
    310 320
    SSGERYLSTA LFADLFTEKE LQQ
    Length:323
    Mass (Da):34,536
    Last modified:January 23, 2007 - v2
    Checksum:iCE74168FAAE99B9E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti70 – 701S → N in AAA27051 (PubMed:3290198).Curated
    Sequence conflicti267 – 2682GI → VF in AAA27051 (PubMed:3290198).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M21450 Genomic DNA. Translation: AAA27051.1.
    AE006468 Genomic DNA. Translation: AAL21324.1.
    PIRiB28181. SYEBAC.
    RefSeqiNP_461365.1. NC_003197.1.
    WP_000036904.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL21324; AAL21324; STM2430.
    GeneIDi1253952.
    KEGGistm:STM2430.
    PATRICi32383489. VBISalEnt20916_2567.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M21450 Genomic DNA. Translation: AAA27051.1.
    AE006468 Genomic DNA. Translation: AAL21324.1.
    PIRiB28181. SYEBAC.
    RefSeqiNP_461365.1. NC_003197.1.
    WP_000036904.1. NC_003197.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D6SX-ray2.30A/B2-323[»]
    1FCJX-ray2.00A/B/C/D2-323[»]
    1OASX-ray2.20A/B2-323[»]
    ProteinModelPortaliP0A1E3.
    SMRiP0A1E3. Positions 2-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi99287.STM2430.

    Proteomic databases

    PaxDbiP0A1E3.
    PRIDEiP0A1E3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL21324; AAL21324; STM2430.
    GeneIDi1253952.
    KEGGistm:STM2430.
    PATRICi32383489. VBISalEnt20916_2567.

    Phylogenomic databases

    eggNOGiENOG4105C6T. Bacteria.
    COG0031. LUCA.
    HOGENOMiHOG000217394.
    KOiK01738.
    OMAiVKCRIGS.
    OrthoDBiEOG6Q2SP8.
    PhylomeDBiP0A1E3.

    Enzyme and pathway databases

    UniPathwayiUPA00136; UER00200.
    BioCyciSENT99287:GCTI-2446-MONOMER.
    BRENDAi2.5.1.47. 2169.
    SABIO-RKP0A1E3.

    Miscellaneous databases

    EvolutionaryTraceiP0A1E3.

    Family and domain databases

    InterProiIPR005856. Cys_synth.
    IPR005859. CysK.
    IPR001216. P-phosphate_BS.
    IPR001926. TrpB-like_PLP-dep.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    [Graphical view]
    SUPFAMiSSF53686. SSF53686. 1 hit.
    TIGRFAMsiTIGR01139. cysK. 1 hit.
    TIGR01136. cysKM. 1 hit.
    PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH."
      Byrne C.R., Monroe R.S., Ward K.A., Kredich N.M.
      J. Bacteriol. 170:3150-3157(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16 AND 321-323.
      Strain: LT2.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    3. "Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium."
      Kredich N.M., Becker M.A., Tomkins G.M.
      J. Biol. Chem. 244:2428-2439(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: LT2.
    4. "Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium."
      Burkhard P., Rao G.S.J., Hohenester E., Schnackerz K.D., Cook P.F., Jansonius J.N.
      J. Mol. Biol. 283:121-133(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR, SUBUNIT, SEQUENCE REVISION TO 267-268.
    5. "Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium."
      Burkhard P., Tai C.-H., Ristroph C.M., Cook P.F., Jansonius J.N.
      J. Mol. Biol. 291:941-953(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) MUTANT ALA-42 IN COMPLEX WITH PYRIDOXAL PHOSPHATE.
    6. "Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound."
      Burkhard P., Tai C.-H., Jansonius J.N., Cook P.F.
      J. Mol. Biol. 303:279-286(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR, ALLOSTERIC REGULATION.

    Entry informationi

    Entry nameiCYSK_SALTY
    AccessioniPrimary (citable) accession number: P0A1E3
    Secondary accession number(s): P12674
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: January 23, 2007
    Last modified: February 17, 2016
    This is version 86 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, 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.