Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9YBL2 (CYSO_AERPE)

Last modified January 19, 2010. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Protein cysO
Alternative name(s):
    Cysteine synthase
    EC=2.5.1.47
    O-acetylserine sulfhydrylase
    O-phosphoserine sulfhydrylase
    EC=2.5.1.65
    Cystathionine beta-synthase
    EC=4.2.1.22
    Serine sulfhydrase
Gene names
Name: cysO
Ordered Locus Names: APE_1586
OrganismAeropyrum pernix [Complete proteome] [HAMAP]
Taxonomic identifier56636 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum

Hide | Top

Protein attributes

Sequence length389 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

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. Ref.2

Catalytic activity

O(3)-acetyl-L-serine + H2S = L-cysteine + acetate. Ref.2 Ref.3

O-phospho-L-serine + H2S = L-cysteine + phosphate. Ref.2 Ref.3

L-serine + L-homocysteine = L-cystathionine + H2O. Ref.2 Ref.3

Cofactor

Pyridoxal phosphate. Ref.2

Pathway

Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.

Subunit structure

Homodimer. Ref.2

Sequence similarities

Belongs to the cysteine synthase/cystathionine beta-synthase family.

Biophysicochemical properties

Kinetic parameters:

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)

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)

KM=8 mM for L-serine (in the presence of 0.7 mM L-homocysteine at pH 8.3 and 85 degrees Celsius)

KM=0.5 mM for L-homocysteine (in the presence of 30 mM L-serine at pH 8.3 and 85 degrees Celsius)

KM=0.2 mM for sulfide (in the presence of 20 mM L-serine at pH 8.5 and 70 degrees Celsius)

KM=31 mM for L-serine (in the presence of 1 mM sodium sulfide at pH 8.5 and 70 degrees Celsius)

KM=13 mM for O(3)-acetyl-L-serine (in the presence of 20 mM thiosulfate at pH 6.1 and 85 degrees Celsius)

KM=21 mM for thiosulfate (in the presence of 20 mM O(3)-acetyl-L-serine at pH 6.1 and 85 degrees Celsius)

pH dependence:

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

Temperature dependence:

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.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 389388Protein cysO
PRO_0000167131

Regions

Region261 – 2655Pyridoxal phosphate binding

Sites

Binding site1551Pyridoxal phosphate
Binding site3411Pyridoxal phosphate

Amino acid modifications

Modified residue1271N6-(pyridoxal phosphate)lysine

Secondary structure

1 ........................................................................... 389
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q9YBL2-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C103727AC1B9C72B

FASTA38941,981
        10         20         30         40         50         60 
MALADISGYL DVLDSVRGFS YLENAREVLR SGEARCLGNP RSEPEYVKAL YVIGASRIPV 

        70         80         90        100        110        120 
GDGCSHTLEE LGVFDISVPG EMVFPSPLDF FERGKPTPLV RSRLQLPNGV RVWLKLEWYN 

       130        140        150        160        170        180 
PFSLSVKDRP AVEIISRLSR RVEKGSLVAD ATSSNFGVAL SAVARLYGYR ARVYLPGAAE 

       190        200        210        220        230        240 
EFGKLLPRLL GAQVIVDPEA PSTVHLLPRV MKDSKNEGFV HVNQFYNDAN FEAHMRGTAR 

       250        260        270        280        290        300 
EIFVQSRRGG LALRGVAGSL GTSGHMSAAA FYLQSVDPSI RAVLVQPAQG DSIPGIRRVE 

       310        320        330        340        350        360 
TGMLWINMLD ISYTLAEVTL EEAMEAVVEV ARSDGLVIGP SGGAAVKALA KKAAEGDLEP 

       370        380 
GDYVVVVPDT GFKYLSLVQN ALEGAGDSV

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1."
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. expand/collapse author list , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.
DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 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: 12644499] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-8, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[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: 16005886] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000002 Genomic DNA. Translation: BAA80586.1.
PIRE72537.
RefSeqNP_148041.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WKVX-ray2.00A/B1-389[»]
ModBaseSearch...

Genome annotation databases

GeneID1446114.
GenomeReviewsGene locus APE_1586 in contig BA000002_GR.
KEGGape:APE_1586.
NMPDRfig|272557.1.peg.1149.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG748215.
OMALNQFEND.

Enzyme and pathway databases

BioCycAPER272557:APE1586-MONOMER.
BRENDA2.5.1.47. 256344.
2.5.1.65. 256344.
4.2.1.22. 256344.

Family and domain databases

InterProIPR001216. Cys_synth_BS.
IPR001926. PyrdxlP-dep_enz_bsu.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
PROSITEPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameCYSO_AERPE
AccessionPrimary (citable) accession number: Q9YBL2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 23, 2007
Last modified: January 19, 2010
This is version 59 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents