Cystathionine gamma-lyase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P31373 (CYS3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 129. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cysteine biosynthetic process via cystathionine Inferred from mutant phenotype PubMed 10509018. Source: SGD transsulfuration Inferred from mutant phenotype PubMed 8366024. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 14562095 PubMed 22842922. Source: SGD nucleus Inferred from direct assay PubMed 22842922. Source: SGD
Molecular_function	L-cysteine desulfhydrase activity Inferred from electronic annotation. Source: EC L-cystine L-cysteine-lyase (deaminating) Inferred from electronic annotation. Source: EC cystathionine gamma-lyase activity Inferred from direct assay Ref.1. Source: SGD pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-5473,EBI-5473

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.7

Chain

2 – 394

393

Cystathionine gamma-lyase

PRO_0000114754

Sites

Binding site

Substrate By similarity

Binding site

104

Substrate By similarity

Binding site

109

Substrate By similarity

Binding site

334

Substrate By similarity

Amino acid modifications

Modified residue

Phosphothreonine Ref.10

Modified residue

Phosphoserine Ref.10

Modified residue

Phosphoserine Ref.9 Ref.10

Modified residue

204

N6-(pyridoxal phosphate)lysine By similarity

Modified residue

362

Phosphoserine Ref.10

Secondary structure

394

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P31373 [UniParc].

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

FASTA

394

42,542

        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' referencesShow '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 204511 / S288c / AB972.
[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]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, MASS SPECTROMETRY. Strain: YAL6B.
[10]	"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 THR-2; SER-39; SER-40 AND SER-362, MASS SPECTROMETRY.
[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.

PIR

S31228.

RefSeq

NP_009390.1. NM_001178157.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N8P	X-ray	2.60	A/B/C/D	2-393	[»]

ProteinModelPortal

P31373.

SMR

P31373. Positions 2-394.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4440N.

IntAct

P31373. 6 interactions.

MINT

MINT-483065.

STRING

4932.YAL012W.

Proteomic databases

PaxDb

P31373.

PeptideAtlas

P31373.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YAL012W; YAL012W; YAL012W.

GeneID

851221.

KEGG

sce:YAL012W.

Organism-specific databases

SGD

S000000010. CYS3.

Phylogenomic databases

eggNOG

COG0626.

GeneTree

ENSGT00390000000312.

HOGENOM

HOG000246415.

K01758.

OMA

PIHANST.

OrthoDB

EOG447K2R.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-389.

UniPathway

UPA00136; UER00202.

Gene expression databases

Genevestigator

P31373.

GermOnline

YAL012W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

InterPro

IPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

PANTHER

PTHR11808. PTHR11808. 1 hit.

Pfam

PF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]

PIRSF

PIRSF001434. CGS. 1 hit.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P31373.

NextBio

968118.

Entry information

Entry name

CYS3_YEAST

Accession

Primary (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 3, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome I

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

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·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents