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Protein

Protein CysO

Gene

cysO

Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cysteine synthase that can also catalyze the synthesis of S-sulfo-L-cysteine from thiosulfate and O(3)-acetyl-L-serine, as well as the sulfhydrylation of L-serine by sulfide.1 Publication

Catalytic activityi

O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate.
O-phospho-L-serine + H2S = L-cysteine + phosphate.
L-serine + L-homocysteine = L-cystathionine + H2O.

Cofactori

pyridoxal 5'-phosphate1 Publication

Kineticsi

  1. KM=28 mM for O(3)-acetyl-L-serine (in the presence of 1 mM sodium sulfide at pH 6.7 and 60 degrees Celsius)1 Publication
  2. KM=0.2 mM for sulfide (in the presence of 20 mM O(3)-acetyl-L-serine at pH 6.7 and 60 degrees Celsius)1 Publication
  3. KM=8 mM for L-serine (in the presence of 0.7 mM L-homocysteine at pH 8.3 and 85 degrees Celsius)1 Publication
  4. KM=0.5 mM for L-homocysteine (in the presence of 30 mM L-serine at pH 8.3 and 85 degrees Celsius)1 Publication
  5. KM=0.2 mM for sulfide (in the presence of 20 mM L-serine at pH 8.5 and 70 degrees Celsius)1 Publication
  6. KM=31 mM for L-serine (in the presence of 1 mM sodium sulfide at pH 8.5 and 70 degrees Celsius)1 Publication
  7. KM=13 mM for O(3)-acetyl-L-serine (in the presence of 20 mM thiosulfate at pH 6.1 and 85 degrees Celsius)1 Publication
  8. KM=21 mM for thiosulfate (in the presence of 20 mM O(3)-acetyl-L-serine at pH 6.1 and 85 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 6.7 for O-acetylserine sulfhydrylase A activity and 8.1-8.8 for cystathionine beta-synthase activity.1 Publication

    Temperature dependencei

    Optimum temperature is above 90 degrees Celsius for S-sulfo-L-cysteine synthase activity, 70-80 degrees Celsius for O-acetylserine sulfhydrylase A activity, and 80 degrees Celsius for both cystathionine beta-synthase and L-serine sulfhdrylase activities.1 Publication

    Pathway: 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. no protein annotated in this organism
    2. Protein CysO (cysO)
    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 sitei155 – 1551Pyridoxal phosphate1 Publication
    Binding sitei341 – 3411Pyridoxal phosphate1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Cysteine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciAPER272557:GJD6-1077-MONOMER.
    BRENDAi2.5.1.47. 171.
    2.5.1.65. 171.
    SABIO-RKQ9YBL2.
    UniPathwayiUPA00136; UER00200.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein CysO
    Alternative name(s):
    Cystathionine beta-synthase (EC:4.2.1.22)
    Cysteine synthase (EC:2.5.1.47)
    O-acetylserine sulfhydrylase
    O-phosphoserine sulfhydrylase (EC:2.5.1.65)
    Serine sulfhydrase
    Gene namesi
    Name:cysO
    Ordered Locus Names:APE_1586
    OrganismiAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
    Taxonomic identifieri272557 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum
    ProteomesiUP000002518 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 389388Protein CysOPRO_0000167131Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei127 – 1271N6-(pyridoxal phosphate)lysine

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    STRINGi272557.APE_1586.

    Structurei

    Secondary structure

    1
    389
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53Combined sources
    Helixi6 – 116Combined sources
    Helixi12 – 154Combined sources
    Helixi22 – 3110Combined sources
    Beta strandi33 – 353Combined sources
    Beta strandi37 – 393Combined sources
    Helixi40 – 423Combined sources
    Helixi44 – 5310Combined sources
    Beta strandi56 – 638Combined sources
    Beta strandi65 – 673Combined sources
    Turni68 – 747Combined sources
    Beta strandi83 – 864Combined sources
    Helixi87 – 937Combined sources
    Beta strandi99 – 1013Combined sources
    Helixi107 – 1093Combined sources
    Beta strandi110 – 1167Combined sources
    Helixi117 – 1193Combined sources
    Turni121 – 1233Combined sources
    Helixi128 – 13811Combined sources
    Turni139 – 1413Combined sources
    Beta strandi147 – 1515Combined sources
    Helixi154 – 16613Combined sources
    Beta strandi170 – 1767Combined sources
    Helixi181 – 1899Combined sources
    Beta strandi193 – 1975Combined sources
    Beta strandi201 – 2033Combined sources
    Helixi204 – 2063Combined sources
    Helixi207 – 21711Combined sources
    Turni224 – 2263Combined sources
    Helixi228 – 2369Combined sources
    Helixi238 – 24811Combined sources
    Beta strandi253 – 2586Combined sources
    Beta strandi261 – 2633Combined sources
    Helixi264 – 27613Combined sources
    Beta strandi281 – 2877Combined sources
    Helixi299 – 3013Combined sources
    Helixi305 – 3084Combined sources
    Beta strandi314 – 3185Combined sources
    Helixi320 – 33415Combined sources
    Helixi340 – 35415Combined sources
    Beta strandi360 – 3678Combined sources
    Helixi371 – 3733Combined sources
    Helixi375 – 3828Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WKVX-ray2.00A/B1-389[»]
    3VSAX-ray2.07A/B1-389[»]
    3VSCX-ray2.07A/B1-389[»]
    3VSDX-ray2.09A/B1-389[»]
    ProteinModelPortaliQ9YBL2.
    SMRiQ9YBL2. Positions 2-384.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9YBL2.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni261 – 2655Pyridoxal phosphate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0031.
    HOGENOMiHOG000217394.
    KOiK10150.
    OMAiKLEWYHP.

    Family and domain databases

    InterProiIPR001216. P-phosphate_BS.
    IPR001926. TrpB-like_PLP-dep.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    [Graphical view]
    SUPFAMiSSF53686. SSF53686. 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.

    Q9YBL2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MALADISGYL DVLDSVRGFS YLENAREVLR SGEARCLGNP RSEPEYVKAL
    60 70 80 90 100
    YVIGASRIPV GDGCSHTLEE LGVFDISVPG EMVFPSPLDF FERGKPTPLV
    110 120 130 140 150
    RSRLQLPNGV RVWLKLEWYN PFSLSVKDRP AVEIISRLSR RVEKGSLVAD
    160 170 180 190 200
    ATSSNFGVAL SAVARLYGYR ARVYLPGAAE EFGKLLPRLL GAQVIVDPEA
    210 220 230 240 250
    PSTVHLLPRV MKDSKNEGFV HVNQFYNDAN FEAHMRGTAR EIFVQSRRGG
    260 270 280 290 300
    LALRGVAGSL GTSGHMSAAA FYLQSVDPSI RAVLVQPAQG DSIPGIRRVE
    310 320 330 340 350
    TGMLWINMLD ISYTLAEVTL EEAMEAVVEV ARSDGLVIGP SGGAAVKALA
    360 370 380
    KKAAEGDLEP GDYVVVVPDT GFKYLSLVQN ALEGAGDSV
    Length:389
    Mass (Da):41,981
    Last modified:January 23, 2007 - v3
    Checksum:iC103727AC1B9C72B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000002 Genomic DNA. Translation: BAA80586.1.
    PIRiE72537.
    RefSeqiNP_148041.1. NC_000854.2.
    WP_010866467.1. NC_000854.2.

    Genome annotation databases

    EnsemblBacteriaiBAA80586; BAA80586; APE_1586.
    GeneIDi1446114.
    KEGGiape:APE_1586.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000002 Genomic DNA. Translation: BAA80586.1.
    PIRiE72537.
    RefSeqiNP_148041.1. NC_000854.2.
    WP_010866467.1. NC_000854.2.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WKVX-ray2.00A/B1-389[»]
    3VSAX-ray2.07A/B1-389[»]
    3VSCX-ray2.07A/B1-389[»]
    3VSDX-ray2.09A/B1-389[»]
    ProteinModelPortaliQ9YBL2.
    SMRiQ9YBL2. Positions 2-384.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi272557.APE_1586.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAA80586; BAA80586; APE_1586.
    GeneIDi1446114.
    KEGGiape:APE_1586.

    Phylogenomic databases

    eggNOGiCOG0031.
    HOGENOMiHOG000217394.
    KOiK10150.
    OMAiKLEWYHP.

    Enzyme and pathway databases

    UniPathwayiUPA00136; UER00200.
    BioCyciAPER272557:GJD6-1077-MONOMER.
    BRENDAi2.5.1.47. 171.
    2.5.1.65. 171.
    SABIO-RKQ9YBL2.

    Miscellaneous databases

    EvolutionaryTraceiQ9YBL2.

    Family and domain databases

    InterProiIPR001216. P-phosphate_BS.
    IPR001926. TrpB-like_PLP-dep.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    [Graphical view]
    SUPFAMiSSF53686. SSF53686. 1 hit.
    PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.
    2. "Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1."
      Mino K., Ishikawa K.
      J. Bacteriol. 185:2277-2284(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-8, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.
    3. "Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in L-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0 A resolution."
      Oda Y., Mino K., Ishikawa K., Ataka M.
      J. Mol. Biol. 351:334-344(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY.
      Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.

    Entry informationi

    Entry nameiCYSO_AERPE
    AccessioniPrimary (citable) accession number: Q9YBL2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: January 23, 2007
    Last modified: April 29, 2015
    This is version 91 of the entry and version 3 of the sequence. [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

    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

    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 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.