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Protein

Cystathionine beta-synthase

Gene

CYS4

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

Functioni

Catalytic activityi

L-serine + L-homocysteine = L-cystathionine + H2O.

Cofactori

Pathwayi: L-cysteine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-cysteine from L-homocysteine and L-serine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Cystathionine beta-synthase (CYS4)
  2. Cystathionine gamma-lyase (CYS3)
This subpathway is part of the pathway L-cysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-cysteine from L-homocysteine and L-serine, the pathway L-cysteine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841Pyridoxal phosphateBy similarity
Binding sitei289 – 2891Pyridoxal phosphateBy similarity

GO - Molecular functioni

  • cystathionine beta-synthase activity Source: SGD

GO - Biological processi

  • cysteine biosynthetic process from serine Source: SGD
  • cysteine biosynthetic process via cystathionine Source: SGD
  • hydrogen sulfide biosynthetic process Source: SGD
  • transsulfuration Source: SGD
  • traversing start control point of mitotic cell cycle 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-388.
YEAST:YGR155W-MONOMER.
BRENDAi4.2.1.22. 984.
ReactomeiR-SCE-1614603. Cysteine formation from homocysteine.
SABIO-RKP32582.
UniPathwayiUPA00136; UER00201.

Names & Taxonomyi

Protein namesi
Recommended name:
Cystathionine beta-synthase (EC:4.2.1.22)
Alternative name(s):
Beta-thionase
Serine sulfhydrase
Sulfur transfer protein 4
Gene namesi
Name:CYS4
Synonyms:STR4
Ordered Locus Names:YGR155W
ORF Names:G6667
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR155W.
SGDiS000003387. CYS4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 507507Cystathionine beta-synthasePRO_0000167135Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei134 – 1341PhosphoserineCombined sources
Modified residuei350 – 3501PhosphoserineCombined sources
Modified residuei424 – 4241PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32582.
PeptideAtlasiP32582.

PTM databases

iPTMnetiP32582.

Interactioni

Protein-protein interaction databases

BioGridi33403. 141 interactions.
DIPiDIP-1282N.
IntActiP32582. 8 interactions.
MINTiMINT-391362.

Structurei

3D structure databases

ProteinModelPortaliP32582.
SMRiP32582. Positions 13-507.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini373 – 43260CBSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni196 – 2005Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Contains 1 CBS domain.PROSITE-ProRule annotation

Keywords - Domaini

CBS domain

Phylogenomic databases

GeneTreeiENSGT00510000047027.
HOGENOMiHOG000217392.
InParanoidiP32582.
KOiK01697.
OMAiWIKTDDA.
OrthoDBiEOG7G4QR4.

Family and domain databases

InterProiIPR000644. CBS_dom.
IPR005857. Cysta_beta_synth.
IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00571. CBS. 2 hits.
PF00291. PALP. 1 hit.
[Graphical view]
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01137. cysta_beta. 1 hit.
PROSITEiPS51371. CBS. 1 hit.
PS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32582-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKSEQQADS RHNVIDLVGN TPLIALKKLP KALGIKPQIY AKLELYNPGG
60 70 80 90 100
SIKDRIAKSM VEEAEASGRI HPSRSTLIEP TSGNTGIGLA LIGAIKGYRT
110 120 130 140 150
IITLPEKMSN EKVSVLKALG AEIIRTPTAA AWDSPESHIG VAKKLEKEIP
160 170 180 190 200
GAVILDQYNN MMNPEAHYFG TGREIQRQLE DLNLFDNLRA VVAGAGTGGT
210 220 230 240 250
ISGISKYLKE QNDKIQIVGA DPFGSILAQP ENLNKTDITD YKVEGIGYDF
260 270 280 290 300
VPQVLDRKLI DVWYKTDDKP SFKYARQLIS NEGVLVGGSS GSAFTAVVKY
310 320 330 340 350
CEDHPELTED DVIVAIFPDS IRSYLTKFVD DEWLKKNNLW DDDVLARFDS
360 370 380 390 400
SKLEASTTKY ADVFGNATVK DLHLKPVVSV KETAKVTDVI KILKDNGFDQ
410 420 430 440 450
LPVLTEDGKL SGLVTLSELL RKLSINNSNN DNTIKGKYLD FKKLNNFNDV
460 470 480 490 500
SSYNENKSGK KKFIKFDENS KLSDLNRFFE KNSSAVITDG LKPIHIVTKM

DLLSYLA
Length:507
Mass (Da):56,022
Last modified:October 1, 1993 - v1
Checksum:iD0C7059B20FD0746
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21T → A in AAC37401 (PubMed:8022826).Curated
Sequence conflicti8 – 81A → T in AAC37401 (PubMed:8022826).Curated
Sequence conflicti63 – 631Missing in AAC37401 (PubMed:8022826).Curated
Sequence conflicti104 – 1041L → W in AAC37401 (PubMed:8022826).Curated
Sequence conflicti129 – 1291A → V in AAC37401 (PubMed:8022826).Curated
Sequence conflicti163 – 1631N → T in AAC37401 (PubMed:8022826).Curated
Sequence conflicti407 – 4071D → Y in AAC37401 (PubMed:8022826).Curated
Sequence conflicti436 – 4372GK → VE in AAC37401 (PubMed:8022826).Curated
Sequence conflicti441 – 4411F → V in AAC37401 (PubMed:8022826).Curated
Sequence conflicti481 – 4811K → E in AAC37401 (PubMed:8022826).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti504 – 5041S → N in strain: UCD932.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72922 Genomic DNA. Translation: CAA51426.1.
D16502 Genomic DNA. Translation: BAA03952.1.
L14578 Unassigned DNA. Translation: AAC37401.1.
DQ393806 Genomic DNA. Translation: ABD57960.1.
DQ393807 Genomic DNA. Translation: ABD57961.1.
DQ393808 Genomic DNA. Translation: ABD57962.1.
DQ393809 Genomic DNA. Translation: ABD57963.1.
X85807 Genomic DNA. Translation: CAA59812.1.
Z72940 Genomic DNA. Translation: CAA97169.1.
BK006941 Genomic DNA. Translation: DAA08246.1.
PIRiA48661.
RefSeqiNP_011671.3. NM_001181284.3.

Genome annotation databases

EnsemblFungiiYGR155W; YGR155W; YGR155W.
GeneIDi853059.
KEGGisce:YGR155W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72922 Genomic DNA. Translation: CAA51426.1.
D16502 Genomic DNA. Translation: BAA03952.1.
L14578 Unassigned DNA. Translation: AAC37401.1.
DQ393806 Genomic DNA. Translation: ABD57960.1.
DQ393807 Genomic DNA. Translation: ABD57961.1.
DQ393808 Genomic DNA. Translation: ABD57962.1.
DQ393809 Genomic DNA. Translation: ABD57963.1.
X85807 Genomic DNA. Translation: CAA59812.1.
Z72940 Genomic DNA. Translation: CAA97169.1.
BK006941 Genomic DNA. Translation: DAA08246.1.
PIRiA48661.
RefSeqiNP_011671.3. NM_001181284.3.

3D structure databases

ProteinModelPortaliP32582.
SMRiP32582. Positions 13-507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33403. 141 interactions.
DIPiDIP-1282N.
IntActiP32582. 8 interactions.
MINTiMINT-391362.

PTM databases

iPTMnetiP32582.

Proteomic databases

MaxQBiP32582.
PeptideAtlasiP32582.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR155W; YGR155W; YGR155W.
GeneIDi853059.
KEGGisce:YGR155W.

Organism-specific databases

EuPathDBiFungiDB:YGR155W.
SGDiS000003387. CYS4.

Phylogenomic databases

GeneTreeiENSGT00510000047027.
HOGENOMiHOG000217392.
InParanoidiP32582.
KOiK01697.
OMAiWIKTDDA.
OrthoDBiEOG7G4QR4.

Enzyme and pathway databases

UniPathwayiUPA00136; UER00201.
BioCyciMetaCyc:MONOMER-388.
YEAST:YGR155W-MONOMER.
BRENDAi4.2.1.22. 984.
ReactomeiR-SCE-1614603. Cysteine formation from homocysteine.
SABIO-RKP32582.

Miscellaneous databases

PROiP32582.

Family and domain databases

InterProiIPR000644. CBS_dom.
IPR005857. Cysta_beta_synth.
IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00571. CBS. 2 hits.
PF00291. PALP. 1 hit.
[Graphical view]
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01137. cysta_beta. 1 hit.
PROSITEiPS51371. CBS. 1 hit.
PS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cysteine biosynthesis in Saccharomyces cerevisiae occurs through the transsulfuration pathway which has been built up by enzyme recruitment."
    Cherest H., Thomas D., Surdin-Kerjan Y.
    J. Bacteriol. 175:5366-5374(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26786 / X2180-1A.
  2. "Identification of the structural gene of cystathionine beta-synthase in saccharomyces cerevisiae."
    Ono B., Inoue T., Kijima K., Matsuda A., Negishi K., Shinoda S.
    Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: A5-8-1A.
  3. "A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes."
    Kruger W.D., Cox D.R.
    Proc. Natl. Acad. Sci. U.S.A. 91:6614-6618(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Allele diversity among genes of the sulfate reduction pathway in wine strains of Saccharomyces cerevisiae."
    Linderholm A.L., Bisson L.F.
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: UCD932, UCD939, UCD940 and UCD957.
  5. "The sequence of a 27 kb segment on the right arm of chromosome VII from Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2, NSR1 genes and ten new open reading frames."
    Skala J., Nawrocki A., Goffeau A.
    Yeast 11:1421-1427(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  7. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  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 SER-134 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-350 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCBS_YEAST
AccessioniPrimary (citable) accession number: P32582
Secondary accession number(s): D6VUT5
, Q05177, Q27JK1, Q27JK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 8, 2016
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 41900 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.