CBS_YEAST
ID CBS_YEAST Reviewed; 507 AA.
AC P32582; D6VUT5; Q05177; Q27JK1; Q27JK4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Cystathionine beta-synthase;
DE EC=4.2.1.22;
DE AltName: Full=Beta-thionase;
DE AltName: Full=Serine sulfhydrase;
DE AltName: Full=Sulfur transfer protein 4;
GN Name=CYS4; Synonyms=STR4; OrderedLocusNames=YGR155W; ORFNames=G6667;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26786 / X2180-1A;
RX PubMed=8366024; DOI=10.1128/jb.175.17.5366-5374.1993;
RA Cherest H., Thomas D., Surdin-Kerjan Y.;
RT "Cysteine biosynthesis in Saccharomyces cerevisiae occurs through the
RT transsulfuration pathway which has been built up by enzyme recruitment.";
RL J. Bacteriol. 175:5366-5374(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A5-8-1A;
RA Ono B., Inoue T., Kijima K., Matsuda A., Negishi K., Shinoda S.;
RT "Identification of the structural gene of cystathionine beta-synthase in
RT saccharomyces cerevisiae.";
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8022826; DOI=10.1073/pnas.91.14.6614;
RA Kruger W.D., Cox D.R.;
RT "A yeast system for expression of human cystathionine beta-synthase:
RT structural and functional conservation of the human and yeast genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6614-6618(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UCD932, UCD939, UCD940, and UCD957;
RA Linderholm A.L., Bisson L.F.;
RT "Allele diversity among genes of the sulfate reduction pathway in wine
RT strains of Saccharomyces cerevisiae.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8585325; DOI=10.1002/yea.320111410;
RA Skala J., Nawrocki A., Goffeau A.;
RT "The sequence of a 27 kb segment on the right arm of chromosome VII from
RT Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2,
RT NSR1 genes and ten new open reading frames.";
RL Yeast 11:1421-1427(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [7]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND SER-424, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND SER-424, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homocysteine + L-serine = H2O + L,L-cystathionine;
CC Xref=Rhea:RHEA:10112, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:58161, ChEBI:CHEBI:58199; EC=4.2.1.22;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-homocysteine and L-serine: step 1/2.
CC -!- MISCELLANEOUS: Present with 41900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; X72922; CAA51426.1; -; Genomic_DNA.
DR EMBL; D16502; BAA03952.1; -; Genomic_DNA.
DR EMBL; L14578; AAC37401.1; -; Unassigned_DNA.
DR EMBL; DQ393806; ABD57960.1; -; Genomic_DNA.
DR EMBL; DQ393807; ABD57961.1; -; Genomic_DNA.
DR EMBL; DQ393808; ABD57962.1; -; Genomic_DNA.
DR EMBL; DQ393809; ABD57963.1; -; Genomic_DNA.
DR EMBL; X85807; CAA59812.1; -; Genomic_DNA.
DR EMBL; Z72940; CAA97169.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08246.1; -; Genomic_DNA.
DR PIR; A48661; A48661.
DR RefSeq; NP_011671.3; NM_001181284.3.
DR PDB; 6C2H; X-ray; 1.49 A; A=1-353.
DR PDB; 6C2Q; X-ray; 2.17 A; A=1-353.
DR PDB; 6C2Z; X-ray; 1.37 A; A=1-353.
DR PDB; 6C4P; X-ray; 2.30 A; A=1-353.
DR PDBsum; 6C2H; -.
DR PDBsum; 6C2Q; -.
DR PDBsum; 6C2Z; -.
DR PDBsum; 6C4P; -.
DR AlphaFoldDB; P32582; -.
DR SMR; P32582; -.
DR BioGRID; 33403; 211.
DR DIP; DIP-1282N; -.
DR IntAct; P32582; 31.
DR MINT; P32582; -.
DR STRING; 4932.YGR155W; -.
DR iPTMnet; P32582; -.
DR MaxQB; P32582; -.
DR PaxDb; P32582; -.
DR PRIDE; P32582; -.
DR EnsemblFungi; YGR155W_mRNA; YGR155W; YGR155W.
DR GeneID; 853059; -.
DR KEGG; sce:YGR155W; -.
DR SGD; S000003387; CYS4.
DR VEuPathDB; FungiDB:YGR155W; -.
DR eggNOG; KOG1252; Eukaryota.
DR GeneTree; ENSGT00510000047027; -.
DR HOGENOM; CLU_021018_0_0_1; -.
DR InParanoid; P32582; -.
DR OMA; KFADDEW; -.
DR BioCyc; MetaCyc:YGR155W-MON; -.
DR BioCyc; YEAST:YGR155W-MON; -.
DR BRENDA; 4.2.1.22; 984.
DR Reactome; R-SCE-1614603; Cysteine formation from homocysteine.
DR SABIO-RK; P32582; -.
DR UniPathway; UPA00136; UER00201.
DR PRO; PR:P32582; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32582; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004122; F:cystathionine beta-synthase activity; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IDA:SGD.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IMP:SGD.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IDA:SGD.
DR GO; GO:0019346; P:transsulfuration; IMP:SGD.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IMP:SGD.
DR CDD; cd04608; CBS_pair_CBS; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR046353; CBS_C.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR005857; Cysta_beta_synth.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00291; PALP; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF53686; SSF53686; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR TIGRFAMs; TIGR01137; cysta_beta; 1.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; CBS domain; Cysteine biosynthesis;
KW Lyase; Phosphoprotein; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..507
FT /note="Cystathionine beta-synthase"
FT /id="PRO_0000167135"
FT DOMAIN 373..432
FT /note="CBS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 84
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 196..200
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 53
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT VARIANT 504
FT /note="S -> N (in strain: UCD932)"
FT CONFLICT 2
FT /note="T -> A (in Ref. 3; AAC37401)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="A -> T (in Ref. 3; AAC37401)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="Missing (in Ref. 3; AAC37401)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="L -> W (in Ref. 3; AAC37401)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="A -> V (in Ref. 3; AAC37401)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="N -> T (in Ref. 3; AAC37401)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="D -> Y (in Ref. 3; AAC37401)"
FT /evidence="ECO:0000305"
FT CONFLICT 436..437
FT /note="GK -> VE (in Ref. 3; AAC37401)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="F -> V (in Ref. 3; AAC37401)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="K -> E (in Ref. 3; AAC37401)"
FT /evidence="ECO:0000305"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:6C2Z"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:6C2Z"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:6C2Z"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6C2Z"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:6C2Z"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:6C2Z"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:6C2Z"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:6C2Z"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:6C2Z"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:6C2Z"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:6C2Z"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:6C2Z"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 268..282
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 288..303
FT /evidence="ECO:0007829|PDB:6C2Z"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:6C2Z"
FT TURN 325..329
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:6C2Z"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:6C2Z"
SQ SEQUENCE 507 AA; 56022 MW; D0C7059B20FD0746 CRC64;
MTKSEQQADS RHNVIDLVGN TPLIALKKLP KALGIKPQIY AKLELYNPGG SIKDRIAKSM
VEEAEASGRI HPSRSTLIEP TSGNTGIGLA LIGAIKGYRT IITLPEKMSN EKVSVLKALG
AEIIRTPTAA AWDSPESHIG VAKKLEKEIP GAVILDQYNN MMNPEAHYFG TGREIQRQLE
DLNLFDNLRA VVAGAGTGGT ISGISKYLKE QNDKIQIVGA DPFGSILAQP ENLNKTDITD
YKVEGIGYDF VPQVLDRKLI DVWYKTDDKP SFKYARQLIS NEGVLVGGSS GSAFTAVVKY
CEDHPELTED DVIVAIFPDS IRSYLTKFVD DEWLKKNNLW DDDVLARFDS SKLEASTTKY
ADVFGNATVK DLHLKPVVSV KETAKVTDVI KILKDNGFDQ LPVLTEDGKL SGLVTLSELL
RKLSINNSNN DNTIKGKYLD FKKLNNFNDV SSYNENKSGK KKFIKFDENS KLSDLNRFFE
KNSSAVITDG LKPIHIVTKM DLLSYLA
