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P31373 (CYS3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cystathionine gamma-lyase

EC=4.4.1.1
Alternative name(s):
Gamma-cystathionase
Sulfur transfer protein 1
Gene names
Name:CYS3
Synonyms:CYI1, STR1
Ordered Locus Names:YAL012W
ORF Names:FUN35
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-cystathionine + H2O = L-cysteine + NH3 + 2-oxobutanoate.

Cofactor

Pyridoxal phosphate. Ref.11

Pathway

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

Subunit structure

Homotetramer. Ref.11

Subcellular location

Cytoplasm.

Miscellaneous

Present with 38300 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the trans-sulfuration enzymes family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-5473,EBI-5473

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 394393Cystathionine gamma-lyase
PRO_0000114754

Sites

Binding site521Substrate By similarity
Binding site1041Substrate By similarity
Binding site1091Substrate By similarity
Binding site3341Substrate By similarity

Amino acid modifications

Modified residue2041N6-(pyridoxal phosphate)lysine By similarity
Modified residue3621Phosphoserine Ref.9 Ref.10

Secondary structure

....................................................................... 394
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31373 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 861A5AA7557687FC

FASTA39442,542
        10         20         30         40         50         60 
MTLQESDKFA TKAIHAGEHV DVHGSVIEPI SLSTTFKQSS PANPIGTYEY SRSQNPNREN 

        70         80         90        100        110        120 
LERAVAALEN AQYGLAFSSG SATTATILQS LPQGSHAVSI GDVYGGTHRY FTKVANAHGV 

       130        140        150        160        170        180 
ETSFTNDLLN DLPQLIKENT KLVWIETPTN PTLKVTDIQK VADLIKKHAA GQDVILVVDN 

       190        200        210        220        230        240 
TFLSPYISNP LNFGADIVVH SATKYINGHS DVVLGVLATN NKPLYERLQF LQNAIGAIPS 

       250        260        270        280        290        300 
PFDAWLTHRG LKTLHLRVRQ AALSANKIAE FLAADKENVV AVNYPGLKTH PNYDVVLKQH 

       310        320        330        340        350        360 
RDALGGGMIS FRIKGGAEAA SKFASSTRLF TLAESLGGIE SLLEVPAVMT HGGIPKEARE 

       370        380        390 
ASGVFDDLVR ISVGIEDTDD LLEDIKQALK QATN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the CYS3 (CYI1) gene of Saccharomyces cerevisiae."
Ono B., Tanaka K., Naito K., Heike C., Shinoda S., Yamamoto S., Ohmori S., Oshima T., Toh-e A.
J. Bacteriol. 174:3339-3347(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"Cloning and bacterial expression of the CYS3 gene encoding cystathionine gamma-lyase of Saccharomyces cerevisiae and the physicochemical and enzymatic properties of the protein."
Yamagata S., D'Andrea R.J., Fujisaki S., Isaji M., Nakamura K.
J. Bacteriol. 175:4800-4808(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: DBY939.
[3]"Physical localization of yeast CYS3, a gene whose product resembles the rat gamma-cystathionase and Escherichia coli cystathionine gamma-synthase enzymes."
Barton A.B., Kaback D.B., Clark M.W., Keng T., Ouellette B.F.F., Storms R.K., Zeng B., Zhong W.W., Fortin N., Delaney S., Bussey H.
Yeast 9:363-369(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32 kb region between the LTE1 and SPO7 genes."
Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B., Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.
Genome 36:32-42(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[5]"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K.
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]"Cystathionine gamma-lyase of Saccharomyces cerevisiae: structural gene and cystathionine gamma-synthase activity."
Ono B., Ishii N., Naito K., Miyoshi S., Shinoda S., Yamamoto S., Ohmori S.
Yeast 9:389-397(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-19, CHARACTERIZATION.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzymes family: crystal structure of cystathionine gamma-lyase from yeast and intrafamiliar structure comparison."
Messerschmidt A., Worbs M., Steegborn C., Wahl M.C., Huber R., Laber B., Clausen T.
Biol. Chem. 384:373-386(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-393 IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L05146 Genomic DNA. Translation: AAC04945.1.
D14135 Genomic DNA. Translation: BAA03190.1.
BK006935 Genomic DNA. Translation: DAA06976.1.
PIRS31228.
RefSeqNP_009390.1. NM_001178157.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N8PX-ray2.60A/B/C/D2-393[»]
ProteinModelPortalP31373.
SMRP31373. Positions 2-394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31754. 155 interactions.
DIPDIP-4440N.
IntActP31373. 5 interactions.
MINTMINT-483065.
STRING4932.YAL012W.

Proteomic databases

PaxDbP31373.
PeptideAtlasP31373.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAL012W; YAL012W; YAL012W.
GeneID851221.
KEGGsce:YAL012W.

Organism-specific databases

SGDS000000010. CYS3.

Phylogenomic databases

eggNOGCOG0626.
GeneTreeENSGT00390000000312.
HOGENOMHOG000246415.
KOK01758.
OMAEECEDAR.
OrthoDBEOG71VT31.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-389.
YEAST:YAL012W-MONOMER.
UniPathwayUPA00136; UER00202.

Gene expression databases

GenevestigatorP31373.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11808. PTHR11808. 1 hit.
PfamPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFPIRSF001434. CGS. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP31373.
NextBio968118.
PROP31373.

Entry information

Entry nameCYS3_YEAST
AccessionPrimary (citable) accession number: P31373
Secondary accession number(s): D6VPK6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome I

Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways