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Homocysteine/cysteine synthase (EC 2.5.1.47) (EC 2.5.1.49) (O-acetylserine/O-acetylhomoserine sulfhydrylase) (OAS-OAH SHLase) (OAS-OAH sulfhydrylase)

 CYSD_YEAST              Reviewed;         444 AA.
P06106; D6VYU6;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
18-JUL-2018, entry version 184.
RecName: Full=Homocysteine/cysteine synthase {ECO:0000305};
EC=2.5.1.47 {ECO:0000269|PubMed:4609980};
EC=2.5.1.49 {ECO:0000269|PubMed:4609980, ECO:0000269|PubMed:4947307};
AltName: Full=O-acetylserine/O-acetylhomoserine sulfhydrylase {ECO:0000303|PubMed:8511969};
Short=OAS-OAH SHLase {ECO:0000303|PubMed:8511969};
Short=OAS-OAH sulfhydrylase {ECO:0000303|PubMed:4609980};
Name=MET17 {ECO:0000303|PubMed:8511969};
Synonyms=MET15 {ECO:0000303|PubMed:1781681},
MET25 {ECO:0000303|PubMed:3022238};
OrderedLocusNames=YLR303W {ECO:0000312|SGD:S000004294};
ORFNames=L8003.1;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 28383 / FL100 / VTT C-80102;
PubMed=3022238; DOI=10.1093/nar/14.20.7861;
Kerjan P., Cherest H., Surdin-Kerjan Y.;
"Nucleotide sequence of the Saccharomyces cerevisiae MET25 gene.";
Nucleic Acids Res. 14:7861-7871(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
PubMed=7765825; DOI=10.1007/s002530050222;
Yamagata S., Isaji M., Nakamura K., Fujisaki S., Doi K., Bawden S.,
D'Andrea R.;
"Overexpression of the Saccharomyces cerevisiae MET17/MET25 gene in
Escherichia coli and comparative characterization of the product with
O-acetylserine.O-acetylhomoserine sulfhydrylase of the yeast.";
Appl. Microbiol. Biotechnol. 42:92-99(1994).
[6]
PROTEIN SEQUENCE OF 2-10.
PubMed=8511969; DOI=10.1002/yea.320090409;
Ono B., Ishii N., Naito K., Miyoshi S., Shinoda S., Yamamoto S.,
Ohmori S.;
"Cystathionine gamma-lyase of Saccharomyces cerevisiae: structural
gene and cystathionine gamma-synthase activity.";
Yeast 9:389-397(1993).
[7]
PROTEIN SEQUENCE OF 131-140 AND 351-362.
STRAIN=ATCC 38531 / Y41;
PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x;
Norbeck J., Blomberg A.;
"Protein expression during exponential growth in 0.7 M NaCl medium of
Saccharomyces cerevisiae.";
FEMS Microbiol. Lett. 137:1-8(1996).
[8]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
PubMed=4947307;
Yamagata S.;
"Homocysteine synthesis in yeast. Partial purification and properties
of O-acetylhomoserine sulfhydrylase.";
J. Biochem. 70:1035-1045(1971).
[9]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
COFACTOR.
PubMed=4609980;
Yamagata S., Takeshima K., Naiki N.;
"Evidence for the identity of O-acetylserine sulfhydrylase with O-
acetylhomoserine sulfhydrylase in yeast.";
J. Biochem. 75:1221-1229(1974).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=795806; DOI=10.1093/oxfordjournals.jbchem.a131338;
Yamagata S., Takeshima K.;
"O-acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Further
purification and characterization as a pyridoxal enzyme.";
J. Biochem. 80:777-785(1976).
[11]
SUBUNIT.
PubMed=795807;
Yamagata S.;
"O-acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Subunit
structure.";
J. Biochem. 80:787-797(1976).
[12]
FUNCTION.
PubMed=3299001; DOI=10.1007/BF00331505;
D'Andrea R., Surdin-Kerjan Y., Pure G., Cherest H.;
"Molecular genetics of met17 and met25 mutants of Saccharomyces
cerevisiae: intragenic complementation between mutations of a single
structural gene.";
Mol. Gen. Genet. 207:165-170(1987).
[13]
GENE NAME.
PubMed=1781681;
Ono B., Ishii N., Fujino S., Aoyama I.;
"Role of hydrosulfide ions (HS-) in methylmercury resistance in
Saccharomyces cerevisiae.";
Appl. Environ. Microbiol. 57:3183-3186(1991).
[14]
PATHWAY.
PubMed=1732168;
Cherest H., Surdin-Kerjan Y.;
"Genetic analysis of a new mutation conferring cysteine auxotrophy in
Saccharomyces cerevisiae: updating of the sulfur metabolism pathway.";
Genetics 130:51-58(1992).
[15]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=11914276; DOI=10.1101/gad.970902;
Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M.,
Piccirillo S., Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H.,
Miller P., Gerstein M., Roeder G.S., Snyder M.;
"Subcellular localization of the yeast proteome.";
Genes Dev. 16:707-719(2002).
[16]
PATHWAY.
PubMed=12586406; DOI=10.1111/j.1574-6968.2003.tb11531.x;
Takagi H., Yoshioka K., Awano N., Nakamori S., Ono B.;
"Role of Saccharomyces cerevisiae serine O-acetyltransferase in
cysteine biosynthesis.";
FEMS Microbiol. Lett. 218:291-297(2003).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[19]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-160, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- FUNCTION: Catalyzes the conversion of O-acetyl-L-homoserine (OAH)
into homocysteine in the methionine biosynthesis pathway. Also
catalyzes the conversion of O-acetylserine (OAS) into cysteine,
the last step in the cysteine biosynthesis pathway
(PubMed:7765825, PubMed:4609980, PubMed:795806). However, it seems
that in S.cerevisiae cysteine biosynthesis occurs exclusively
through the cystathionine pathway and not via direct incorporation
of sulfur into OAS (PubMed:1732168). It therefore has no metabolic
role in cysteine biosynthesis and may only have a regulatory role
controlling OAS levels (PubMed:12586406).
{ECO:0000269|PubMed:4609980, ECO:0000269|PubMed:7765825,
ECO:0000269|PubMed:795806, ECO:0000305|PubMed:12586406,
ECO:0000305|PubMed:1732168}.
-!- CATALYTIC ACTIVITY: O-acetyl-L-homoserine + methanethiol = L-
methionine + acetate. {ECO:0000269|PubMed:4609980,
ECO:0000269|PubMed:4947307, ECO:0000269|PubMed:7765825,
ECO:0000269|PubMed:795806}.
-!- CATALYTIC ACTIVITY: O-acetyl-L-serine + hydrogen sulfide = L-
cysteine + acetate. {ECO:0000269|PubMed:4609980,
ECO:0000269|PubMed:7765825, ECO:0000269|PubMed:795806}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:4609980,
ECO:0000269|PubMed:4947307, ECO:0000269|PubMed:7765825,
ECO:0000269|PubMed:795806};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=8.7 mM for O-acetyl-L-homoserine
{ECO:0000269|PubMed:7765825};
KM=6.67 mM for O-acetyl-L-homoserine (at pH 7.8 in Tris-HCl
buffer) {ECO:0000269|PubMed:4609980};
KM=5.12 mM for O-acetyl-L-serine (at pH 7.8 in potassium
phosphate buffer) {ECO:0000269|PubMed:4609980};
pH dependence:
Optimum pH is 7.8 (for O-acetylhomoserine sulfhydrylase activity
in Tris-HCl buffer) and 8.4 (for both O-acetylhomoserine
sulfhydrylase and O-acetylserine sulfhydrylase activities in
barbital-HCl buffer). {ECO:0000269|PubMed:4609980,
ECO:0000269|PubMed:4947307};
-!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
novo pathway; L-homocysteine from O-acetyl-L-homoserine.
{ECO:0000305|PubMed:12586406, ECO:0000305|PubMed:1732168}.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:795807}.
-!- INTERACTION:
Q01329:PTA1; NbExp=2; IntAct=EBI-11487, EBI-14145;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11914276}.
-!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; X04493; CAA28181.1; -; Genomic_DNA.
EMBL; U17243; AAB67347.1; -; Genomic_DNA.
EMBL; AY723848; AAU09765.1; -; Genomic_DNA.
EMBL; BK006945; DAA09612.1; -; Genomic_DNA.
PIR; A25539; A25539.
RefSeq; NP_013406.1; NM_001182191.1.
ProteinModelPortal; P06106; -.
SMR; P06106; -.
BioGrid; 31567; 84.
DIP; DIP-1664N; -.
IntAct; P06106; 7.
MINT; P06106; -.
STRING; 4932.YLR303W; -.
CarbonylDB; P06106; -.
iPTMnet; P06106; -.
PaxDb; P06106; -.
PRIDE; P06106; -.
EnsemblFungi; YLR303W; YLR303W; YLR303W.
GeneID; 851010; -.
KEGG; sce:YLR303W; -.
EuPathDB; FungiDB:YLR303W; -.
SGD; S000004294; MET17.
GeneTree; ENSGT00550000075611; -.
HOGENOM; HOG000246417; -.
InParanoid; P06106; -.
KO; K17069; -.
OMA; NPRFNIP; -.
OrthoDB; EOG092C2OYU; -.
BioCyc; MetaCyc:YLR303W-MONOMER; -.
BioCyc; YEAST:YLR303W-MONOMER; -.
PRO; PR:P06106; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004124; F:cysteine synthase activity; IDA:SGD.
GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IDA:SGD.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0019344; P:cysteine biosynthetic process; TAS:SGD.
GO; GO:0006555; P:methionine metabolic process; IMP:SGD.
CDD; cd00614; CGS_like; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
InterPro; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
Pfam; PF01053; Cys_Met_Meta_PP; 1.
PIRSF; PIRSF001434; CGS; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR01326; OAH_OAS_sulfhy; 1.
PROSITE; PS00868; CYS_MET_METAB_PP; 1.
1: Evidence at protein level;
Amino-acid biosynthesis; Complete proteome; Cysteine biosynthesis;
Cytoplasm; Direct protein sequencing; Isopeptide bond;
Methionine biosynthesis; Multifunctional enzyme; Phosphoprotein;
Pyridoxal phosphate; Reference proteome; Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7765825,
ECO:0000269|PubMed:8511969}.
CHAIN 2 444 Homocysteine/cysteine synthase.
/FTId=PRO_0000114776.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956}.
MOD_RES 209 209 N6-(pyridoxal phosphate)lysine.
{ECO:0000250|UniProtKB:P06721}.
CROSSLNK 160 160 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
SEQUENCE 444 AA; 48672 MW; F84224625C921B35 CRC64;
MPSHFDTVQL HAGQENPGDN AHRSRAVPIY ATTSYVFENS KHGSQLFGLE VPGYVYSRFQ
NPTSNVLEER IAALEGGAAA LAVSSGQAAQ TLAIQGLAHT GDNIVSTSYL YGGTYNQFKI
SFKRFGIEAR FVEGDNPEEF EKVFDERTKA VYLETIGNPK YNVPDFEKIV AIAHKHGIPV
VVDNTFGAGG YFCQPIKYGA DIVTHSATKW IGGHGTTIGG IIVDSGKFPW KDYPEKFPQF
SQPAEGYHGT IYNEAYGNLA YIVHVRTELL RDLGPLMNPF ASFLLLQGVE TLSLRAERHG
ENALKLAKWL EQSPYVSWVS YPGLASHSHH ENAKKYLSNG FGGVLSFGVK DLPNADKETD
PFKLSGAQVV DNLKLASNLA NVGDAKTLVI APYFTTHKQL NDKEKLASGV TKDLIRVSVG
IEFIDDIIAD FQQSFETVFA GQKP


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