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P31373

- CYS3_YEAST

UniProt

P31373 - CYS3_YEAST

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Protein

Cystathionine gamma-lyase

Gene

CYS3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphate1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521SubstrateBy similarity
Binding sitei104 – 1041SubstrateBy similarity
Binding sitei109 – 1091SubstrateBy similarity
Binding sitei334 – 3341SubstrateBy similarity

GO - Molecular functioni

  1. cystathionine gamma-lyase activity Source: SGD
  2. identical protein binding Source: IntAct
  3. L-cysteine desulfhydrase activity Source: UniProtKB-EC
  4. L-cystine L-cysteine-lyase (deaminating) Source: UniProtKB-EC
  5. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. cysteine biosynthetic process Source: SGD
  2. cysteine biosynthetic process via cystathionine Source: SGD
  3. transsulfuration Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-389.
YEAST:YAL012W-MONOMER.
ReactomeiREACT_188977. Cysteine formation from homocysteine.
REACT_188980. Degradation of cysteine and homocysteine.
UniPathwayiUPA00136; UER00202.

Names & Taxonomyi

Protein namesi
Recommended name:
Cystathionine gamma-lyase (EC:4.4.1.1)
Alternative name(s):
Gamma-cystathionase
Sulfur transfer protein 1
Gene namesi
Name:CYS3
Synonyms:CYI1, STR1
Ordered Locus Names:YAL012W
ORF Names:FUN35
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome I

Organism-specific databases

SGDiS000000010. CYS3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 394393Cystathionine gamma-lyasePRO_0000114754Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei204 – 2041N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei362 – 3621Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP31373.
PaxDbiP31373.
PeptideAtlasiP31373.

Expressioni

Gene expression databases

GenevestigatoriP31373.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-5473,EBI-5473

Protein-protein interaction databases

BioGridi31754. 156 interactions.
DIPiDIP-4440N.
IntActiP31373. 5 interactions.
MINTiMINT-483065.
STRINGi4932.YAL012W.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 157Combined sources
Beta strandi38 – 4710Combined sources
Turni51 – 533Combined sources
Helixi56 – 6813Combined sources
Beta strandi72 – 787Combined sources
Helixi80 – 8910Combined sources
Beta strandi96 – 1027Combined sources
Helixi105 – 1139Combined sources
Turni116 – 1183Combined sources
Beta strandi123 – 1275Combined sources
Helixi128 – 1358Combined sources
Beta strandi138 – 1458Combined sources
Turni150 – 1523Combined sources
Helixi158 – 16811Combined sources
Turni169 – 1735Combined sources
Beta strandi175 – 1795Combined sources
Turni181 – 1833Combined sources
Helixi184 – 1874Combined sources
Helixi190 – 1934Combined sources
Beta strandi196 – 2016Combined sources
Turni202 – 2076Combined sources
Beta strandi215 – 2206Combined sources
Helixi222 – 23514Combined sources
Helixi241 – 25111Combined sources
Helixi254 – 27219Combined sources
Turni276 – 2783Combined sources
Beta strandi279 – 2835Combined sources
Helixi293 – 2997Combined sources
Helixi301 – 3033Combined sources
Beta strandi307 – 3159Combined sources
Helixi317 – 32610Combined sources
Beta strandi328 – 3325Combined sources
Beta strandi342 – 3443Combined sources
Turni346 – 3505Combined sources
Turni356 – 3605Combined sources
Beta strandi361 – 3633Combined sources
Beta strandi368 – 3725Combined sources
Helixi378 – 39316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N8PX-ray2.60A/B/C/D2-394[»]
ProteinModelPortaliP31373.
SMRiP31373. Positions 2-394.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31373.

Family & Domainsi

Sequence similaritiesi

Belongs to the trans-sulfuration enzymes family.Curated

Phylogenomic databases

eggNOGiCOG0626.
GeneTreeiENSGT00390000000312.
HOGENOMiHOG000246415.
InParanoidiP31373.
KOiK01758.
OMAiHERNANE.
OrthoDBiEOG71VT31.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11808. PTHR11808. 1 hit.
PfamiPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFiPIRSF001434. CGS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31373-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTLQESDKFA TKAIHAGEHV DVHGSVIEPI SLSTTFKQSS PANPIGTYEY
60 70 80 90 100
SRSQNPNREN LERAVAALEN AQYGLAFSSG SATTATILQS LPQGSHAVSI
110 120 130 140 150
GDVYGGTHRY FTKVANAHGV ETSFTNDLLN DLPQLIKENT KLVWIETPTN
160 170 180 190 200
PTLKVTDIQK VADLIKKHAA GQDVILVVDN TFLSPYISNP LNFGADIVVH
210 220 230 240 250
SATKYINGHS DVVLGVLATN NKPLYERLQF LQNAIGAIPS PFDAWLTHRG
260 270 280 290 300
LKTLHLRVRQ AALSANKIAE FLAADKENVV AVNYPGLKTH PNYDVVLKQH
310 320 330 340 350
RDALGGGMIS FRIKGGAEAA SKFASSTRLF TLAESLGGIE SLLEVPAVMT
360 370 380 390
HGGIPKEARE ASGVFDDLVR ISVGIEDTDD LLEDIKQALK QATN
Length:394
Mass (Da):42,542
Last modified:January 23, 2007 - v2
Checksum:i861A5AA7557687FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05146 Genomic DNA. Translation: AAC04945.1.
D14135 Genomic DNA. Translation: BAA03190.1.
BK006935 Genomic DNA. Translation: DAA06976.1.
PIRiS31228.
RefSeqiNP_009390.1. NM_001178157.1.

Genome annotation databases

EnsemblFungiiYAL012W; YAL012W; YAL012W.
GeneIDi851221.
KEGGisce:YAL012W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05146 Genomic DNA. Translation: AAC04945.1 .
D14135 Genomic DNA. Translation: BAA03190.1 .
BK006935 Genomic DNA. Translation: DAA06976.1 .
PIRi S31228.
RefSeqi NP_009390.1. NM_001178157.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1N8P X-ray 2.60 A/B/C/D 2-394 [» ]
ProteinModelPortali P31373.
SMRi P31373. Positions 2-394.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31754. 156 interactions.
DIPi DIP-4440N.
IntActi P31373. 5 interactions.
MINTi MINT-483065.
STRINGi 4932.YAL012W.

Proteomic databases

MaxQBi P31373.
PaxDbi P31373.
PeptideAtlasi P31373.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YAL012W ; YAL012W ; YAL012W .
GeneIDi 851221.
KEGGi sce:YAL012W.

Organism-specific databases

SGDi S000000010. CYS3.

Phylogenomic databases

eggNOGi COG0626.
GeneTreei ENSGT00390000000312.
HOGENOMi HOG000246415.
InParanoidi P31373.
KOi K01758.
OMAi HERNANE.
OrthoDBi EOG71VT31.

Enzyme and pathway databases

UniPathwayi UPA00136 ; UER00202 .
BioCyci MetaCyc:MONOMER-389.
YEAST:YAL012W-MONOMER.
Reactomei REACT_188977. Cysteine formation from homocysteine.
REACT_188980. Degradation of cysteine and homocysteine.

Miscellaneous databases

EvolutionaryTracei P31373.
NextBioi 968118.
PROi P31373.

Gene expression databases

Genevestigatori P31373.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR11808. PTHR11808. 1 hit.
Pfami PF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view ]
PIRSFi PIRSF001434. CGS. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. 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. 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.

Entry informationi

Entry nameiCYS3_YEAST
AccessioniPrimary (citable) accession number: P31373
Secondary accession number(s): D6VPK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 38300 molecules/cell in log phase SD medium.1 Publication

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
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome I
    Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

External Data

Dasty 3