Cystathionine beta-synthase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32582 (CBS_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 111. History...

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

Documents (4) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Cystathionine beta-synthase
EC=4.2.1.22

Alternative name(s):
Beta-thionase
Serine sulfhydrase
Sulfur transfer protein 4

Gene names

Name:	CYS4
Synonyms:	STR4
Ordered Locus Names:	YGR155W
ORF Names:	G6667

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	507 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-serine + L-homocysteine = L-cystathionine + H₂O.
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-homocysteine and L-serine: step 1/2.
Miscellaneous	Present with 41900 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the cysteine synthase/cystathionine beta-synthase family. Contains 1 CBS domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis
Domain	CBS domain
Ligand	Pyridoxal phosphate
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process from serine Inferred from direct assay. Source: SGD cysteine biosynthetic process via cystathionine Inferred from mutant phenotype Ref.1. Source: SGD hydrogen sulfide biosynthetic process Inferred from direct assay. Source: SGD transsulfuration Inferred from mutant phenotype Ref.1. Source: SGD
Cellular component	mitochondrion Inferred from direct assay. Source: SGD
Molecular function	cystathionine beta-synthase activity Inferred from direct assay. Source: SGD pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 507

507

Cystathionine beta-synthase

PRO_0000167135

Regions

Domain

373 – 432

CBS

Region

196 – 200

Pyridoxal phosphate binding By similarity

Sites

Binding site

Pyridoxal phosphate By similarity

Binding site

289

Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue

N6-(pyridoxal phosphate)lysine By similarity

Modified residue

128

Phosphothreonine Ref.10

Modified residue

134

Phosphoserine Ref.10

Modified residue

350

Phosphoserine Ref.9 Ref.10

Modified residue

424

Phosphoserine Ref.10

Natural variations

Natural variant

504

S → N in strain: UCD932.

Experimental info

Sequence conflict

T → A in AAC37401. Ref.3

Sequence conflict

A → T in AAC37401. Ref.3

Sequence conflict

Missing in AAC37401. Ref.3

Sequence conflict

104

L → W in AAC37401. Ref.3

Sequence conflict

129

A → V in AAC37401. Ref.3

Sequence conflict

163

N → T in AAC37401. Ref.3

Sequence conflict

407

D → Y in AAC37401. Ref.3

Sequence conflict

436 – 437

GK → VE in AAC37401. Ref.3

Sequence conflict

441

F → V in AAC37401. Ref.3

Sequence conflict

481

K → E in AAC37401. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P32582 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: D0C7059B20FD0746
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FASTA

507

56,022

        10         20         30         40         50         60 
MTKSEQQADS RHNVIDLVGN TPLIALKKLP KALGIKPQIY AKLELYNPGG SIKDRIAKSM 

        70         80         90        100        110        120 
VEEAEASGRI HPSRSTLIEP TSGNTGIGLA LIGAIKGYRT IITLPEKMSN EKVSVLKALG 

       130        140        150        160        170        180 
AEIIRTPTAA AWDSPESHIG VAKKLEKEIP GAVILDQYNN MMNPEAHYFG TGREIQRQLE 

       190        200        210        220        230        240 
DLNLFDNLRA VVAGAGTGGT ISGISKYLKE QNDKIQIVGA DPFGSILAQP ENLNKTDITD 

       250        260        270        280        290        300 
YKVEGIGYDF VPQVLDRKLI DVWYKTDDKP SFKYARQLIS NEGVLVGGSS GSAFTAVVKY 

       310        320        330        340        350        360 
CEDHPELTED DVIVAIFPDS IRSYLTKFVD DEWLKKNNLW DDDVLARFDS SKLEASTTKY 

       370        380        390        400        410        420 
ADVFGNATVK DLHLKPVVSV KETAKVTDVI KILKDNGFDQ LPVLTEDGKL SGLVTLSELL 

       430        440        450        460        470        480 
RKLSINNSNN DNTIKGKYLD FKKLNNFNDV SSYNENKSGK KKFIKFDENS KLSDLNRFFE 

       490        500 
KNSSAVITDG LKPIHIVTKM DLLSYLA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8366024] [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: 8022826] [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: 8585325] [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. Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[7]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-128; SER-134; SER-350 AND SER-424, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	A48661.
RefSeq	NP_011671.1. NM_001181284.1.
3D structure databases
ProteinModelPortal	P32582.
SMR	P32582. Positions 5-507.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1282N.
IntAct	P32582. 77 interactions.
MINT	MINT-391362.
STRING	P32582.
Proteomic databases
PeptideAtlas	P32582.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR155W; YGR155W; YGR155W.
GeneID	853059.
KEGG	sce:YGR155W.
NMPDR	fig\|4932.3.peg.2791.
Organism-specific databases
CYGD	YGR155w.
SGD	S000003387. CYS4.
Phylogenomic databases
GeneTree	EFGT00050000001990.
HOGENOM	HBG748215.
OMA	KVDLLTW.
OrthoDB	EOG4CNV1D.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-388.
Gene expression databases
ArrayExpress	P32582.
Genevestigator	P32582.
GermOnline	YGR155W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001216. Cys_synth_BS. IPR005857. Cysta_beta_synth. IPR000644. Cysta_beta_synth_core. IPR001926. PyrdxlP-dep_enz_bsu. [Graphical view]
KO	K01697.
Pfam	PF00571. CBS. 1 hit. PF00291. PALP. 1 hit. [Graphical view]
SMART	SM00116. CBS. 2 hits. [Graphical view]
SUPFAM	SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMs	TIGR01137. Cysta_beta. 1 hit.
PROSITE	PS51371. CBS. 1 hit. PS00901. CYS_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	972992.

Entry information

Entry name

CBS_YEAST

Accession

Primary (citable) accession number: P32582
Secondary accession number(s): D6VUT5

Q27JK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	December 14, 2011
This is version 111 of the entry and version 1 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 VII

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

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