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Q9YBL2 (CYSO_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:cysO
Ordered Locus Names:APE_1586
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum ›

Protein attributes

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

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) Ref.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)

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.

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...

Sequences

Sequence LengthMass (Da)Tools
Q9YBL2 [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

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] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000002 Genomic DNA. Translation: BAA80586.1.
PIRE72537.
RefSeqNP_148041.1. NC_000854.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WKVX-ray2.00A/B1-389[»]
3VSAX-ray2.07A/B1-389[»]
3VSCX-ray2.07A/B1-389[»]
3VSDX-ray2.09A/B1-389[»]
ProteinModelPortalQ9YBL2.
SMRQ9YBL2. Positions 2-384.
ModBaseSearch...

Protein-protein interaction databases

STRING272557.APE_1586.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA80586; BAA80586; APE_1586.
GeneID1446114.
KEGGape:APE_1586.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0031.
HOGENOMHOG000217394.
KOK10150.
OMALEWYNPF.

Enzyme and pathway databases

BioCycAPER272557:GJD6-1077-MONOMER.
SABIO-RKQ9YBL2.
UniPathwayUPA00136; UER00200.

Family and domain databases

InterProIPR001216. Cys_synth_BS.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMSSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
PROSITEPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9YBL2.

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: May 1, 2013
This is version 79 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents