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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.1 Publication
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate.1 Publication
L-serine + L-homocysteine = L-cystathionine + H2O.2 Publications

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

    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. 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)DescriptionActionsGraphical viewLength
    Binding sitei155Pyridoxal phosphate1 Publication1
    Binding sitei341Pyridoxal phosphate1 Publication1

    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

    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:4.2.1.222 Publications)
    Cysteine synthase (EC:2.5.1.471 Publication)
    O-acetylserine sulfhydrylase1 Publication
    O-phosphoserine sulfhydrylase1 Publication (EC:2.5.1.651 Publication)
    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
    Proteomesi
    • UP000002518 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001671312 – 389Protein CysOAdd BLAST388

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei127N6-(pyridoxal phosphate)lysine1

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    STRINGi272557.APE_1586.

    Structurei

    Secondary structure

    1389
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 5Combined sources3
    Helixi6 – 11Combined sources6
    Helixi12 – 15Combined sources4
    Helixi22 – 31Combined sources10
    Beta strandi33 – 35Combined sources3
    Beta strandi37 – 39Combined sources3
    Helixi40 – 42Combined sources3
    Helixi44 – 53Combined sources10
    Beta strandi56 – 63Combined sources8
    Beta strandi65 – 67Combined sources3
    Turni68 – 74Combined sources7
    Beta strandi83 – 86Combined sources4
    Helixi87 – 93Combined sources7
    Beta strandi99 – 101Combined sources3
    Helixi107 – 109Combined sources3
    Beta strandi110 – 116Combined sources7
    Helixi117 – 119Combined sources3
    Turni121 – 123Combined sources3
    Helixi128 – 138Combined sources11
    Turni139 – 141Combined sources3
    Beta strandi147 – 151Combined sources5
    Helixi154 – 166Combined sources13
    Beta strandi170 – 176Combined sources7
    Helixi181 – 189Combined sources9
    Beta strandi193 – 197Combined sources5
    Beta strandi201 – 203Combined sources3
    Helixi204 – 206Combined sources3
    Helixi207 – 217Combined sources11
    Turni224 – 226Combined sources3
    Helixi228 – 236Combined sources9
    Helixi238 – 248Combined sources11
    Beta strandi253 – 258Combined sources6
    Beta strandi261 – 263Combined sources3
    Helixi264 – 276Combined sources13
    Beta strandi281 – 287Combined sources7
    Helixi299 – 301Combined sources3
    Helixi305 – 308Combined sources4
    Beta strandi314 – 318Combined sources5
    Helixi320 – 334Combined sources15
    Helixi340 – 354Combined sources15
    Beta strandi360 – 367Combined sources8
    Helixi371 – 373Combined sources3
    Helixi375 – 382Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1WKVX-ray2.00A/B1-389[»]
    3VSAX-ray2.07A/B1-389[»]
    3VSCX-ray2.07A/B1-389[»]
    3VSDX-ray2.09A/B1-389[»]
    5B36X-ray2.15A/B1-389[»]
    5B3AX-ray2.14A/B1-389[»]
    ProteinModelPortaliQ9YBL2.
    SMRiQ9YBL2.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9YBL2.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni261 – 265Pyridoxal phosphate binding5

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiarCOG01430. Archaea.
    COG0031. LUCA.
    HOGENOMiHOG000217394.
    KOiK10150.
    OMAiYAKLEWY.

    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.

    Genome annotation databases

    EnsemblBacteriaiBAA80586; BAA80586; APE_1586.
    KEGGiape:APE_1586.

    Cross-referencesi

    Sequence databases

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

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1WKVX-ray2.00A/B1-389[»]
    3VSAX-ray2.07A/B1-389[»]
    3VSCX-ray2.07A/B1-389[»]
    3VSDX-ray2.09A/B1-389[»]
    5B36X-ray2.15A/B1-389[»]
    5B3AX-ray2.14A/B1-389[»]
    ProteinModelPortaliQ9YBL2.
    SMRiQ9YBL2.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi272557.APE_1586.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAA80586; BAA80586; APE_1586.
    KEGGiape:APE_1586.

    Phylogenomic databases

    eggNOGiarCOG01430. Archaea.
    COG0031. LUCA.
    HOGENOMiHOG000217394.
    KOiK10150.
    OMAiYAKLEWY.

    Enzyme and pathway databases

    UniPathwayiUPA00136; UER00200.
    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...

    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: November 2, 2016
    This is version 100 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

    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.