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Q9YBL2

- CYSO_AERPE

UniProt

Q9YBL2 - CYSO_AERPE

Protein

Protein CysO

Gene

cysO

Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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 phosphate.1 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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei155 – 1551Pyridoxal phosphate1 Publication
    Binding sitei341 – 3411Pyridoxal phosphate1 Publication

    GO - Molecular functioni

    1. cystathionine beta-synthase activity Source: UniProtKB-EC
    2. cysteine synthase activity Source: UniProtKB-EC
    3. O-phosphoserine sulfhydrylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cysteine biosynthetic process from serine Source: InterPro

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiHLEKDIR.

    Family and domain databases

    InterProiIPR001216. P-phosphate_BS.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [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

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    MALADISGYL DVLDSVRGFS YLENAREVLR SGEARCLGNP RSEPEYVKAL    50
    YVIGASRIPV GDGCSHTLEE LGVFDISVPG EMVFPSPLDF FERGKPTPLV 100
    RSRLQLPNGV RVWLKLEWYN PFSLSVKDRP AVEIISRLSR RVEKGSLVAD 150
    ATSSNFGVAL SAVARLYGYR ARVYLPGAAE EFGKLLPRLL GAQVIVDPEA 200
    PSTVHLLPRV MKDSKNEGFV HVNQFYNDAN FEAHMRGTAR EIFVQSRRGG 250
    LALRGVAGSL GTSGHMSAAA FYLQSVDPSI RAVLVQPAQG DSIPGIRRVE 300
    TGMLWINMLD ISYTLAEVTL EEAMEAVVEV ARSDGLVIGP SGGAAVKALA 350
    KKAAEGDLEP GDYVVVVPDT GFKYLSLVQN ALEGAGDSV 389
    Length:389
    Mass (Da):41,981
    Last modified:January 23, 2007 - v3
    Checksum:iC103727AC1B9C72B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000002 Genomic DNA. Translation: BAA80586.1 .
    PIRi E72537.
    RefSeqi NP_148041.1. NC_000854.2.
    WP_010866467.1. NC_000854.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WKV X-ray 2.00 A/B 1-389 [» ]
    3VSA X-ray 2.07 A/B 1-389 [» ]
    3VSC X-ray 2.07 A/B 1-389 [» ]
    3VSD X-ray 2.09 A/B 1-389 [» ]
    ProteinModelPortali Q9YBL2.
    SMRi Q9YBL2. Positions 2-384.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272557.APE_1586.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAA80586 ; BAA80586 ; APE_1586 .
    GeneIDi 1446114.
    KEGGi ape:APE_1586.

    Phylogenomic databases

    eggNOGi COG0031.
    HOGENOMi HOG000217394.
    KOi K10150.
    OMAi HLEKDIR.

    Enzyme and pathway databases

    UniPathwayi UPA00136 ; UER00200 .
    BioCyci APER272557:GJD6-1077-MONOMER.
    SABIO-RK Q9YBL2.

    Miscellaneous databases

    EvolutionaryTracei Q9YBL2.

    Family and domain databases

    InterProi IPR001216. P-phosphate_BS.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view ]
    Pfami PF00291. PALP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53686. SSF53686. 1 hit.
    PROSITEi PS00901. CYS_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 84 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