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Protein

Cysteine synthase A

Gene

cysK

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
    Binding sitei8Allosteric inhibitor1 Publication1
    Binding sitei72Pyridoxal phosphate3 Publications1
    Binding sitei269Allosteric inhibitor; via amide nitrogen1 Publication1
    Binding sitei273Pyridoxal phosphate3 Publications1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

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

    Enzyme and pathway databases

    BioCyciSENT99287:G1FZD-2453-MONOMER
    BRENDAi2.5.1.47 2169
    SABIO-RKiP0A1E3
    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
    Proteomesi
    • UP000001014 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001670892 – 323Cysteine synthase AAdd BLAST322

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei42N6-(pyridoxal phosphate)lysine1

    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

    1323
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 7Combined sources4
    Helixi8 – 11Combined sources4
    Beta strandi17 – 19Combined sources3
    Beta strandi21 – 26Combined sources6
    Beta strandi28 – 32Combined sources5
    Helixi37 – 39Combined sources3
    Helixi42 – 55Combined sources14
    Beta strandi64 – 68Combined sources5
    Helixi72 – 84Combined sources13
    Beta strandi88 – 93Combined sources6
    Helixi98 – 106Combined sources9
    Beta strandi110 – 114Combined sources5
    Helixi116 – 118Combined sources3
    Helixi119 – 132Combined sources14
    Turni135 – 137Combined sources3
    Beta strandi138 – 140Combined sources3
    Turni143 – 145Combined sources3
    Helixi148 – 155Combined sources8
    Helixi157 – 164Combined sources8
    Turni165 – 167Combined sources3
    Beta strandi171 – 175Combined sources5
    Beta strandi177 – 179Combined sources3
    Helixi180 – 190Combined sources11
    Turni191 – 193Combined sources3
    Beta strandi199 – 205Combined sources7
    Helixi210 – 215Combined sources6
    Helixi241 – 243Combined sources3
    Beta strandi245 – 250Combined sources6
    Helixi252 – 266Combined sources15
    Helixi272 – 284Combined sources13
    Helixi288 – 290Combined sources3
    Beta strandi295 – 299Combined sources5
    Helixi303 – 306Combined sources4
    Helixi310 – 312Combined sources3
    Helixi318 – 321Combined sources4

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP0A1E3

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni177 – 181Pyridoxal phosphate binding5

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105C6T Bacteria
    COG0031 LUCA
    HOGENOMiHOG000217394
    KOiK01738
    OMAiWDSGERY
    PhylomeDBiP0A1E3

    Family and domain databases

    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

    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)DescriptionActionsGraphical viewLength
    Sequence conflicti70S → N in AAA27051 (PubMed:3290198).Curated1
    Sequence conflicti267 – 268GI → VF in AAA27051 (PubMed:3290198).Curated2

    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_003197.2
    WP_000036904.1, NC_003197.2

    Genome annotation databases

    EnsemblBacteriaiAAL21324; AAL21324; STM2430
    GeneIDi1253952
    KEGGistm:STM2430
    PATRICifig|99287.12.peg.2567

    Similar proteinsi

    Entry informationi

    Entry nameiCYSK_SALTY
    AccessioniPrimary (citable) accession number: P0A1E3
    Secondary accession number(s): P12674
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: January 23, 2007
    Last modified: March 28, 2018
    This is version 96 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health