MCY1_YEAST
ID MCY1_YEAST Reviewed; 393 AA.
AC P53206; D6VUE8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Putative mitochondrial cysteine synthase {ECO:0000305|PubMed:9409150};
DE Short=CS;
DE EC=2.5.1.47;
DE AltName: Full=Cysteine synthase-like protein {ECO:0000303|PubMed:17482430};
DE Short=CSl;
DE AltName: Full=O-acetylserine (thiol)-lyase;
DE Short=OAS-TL;
DE AltName: Full=O-acetylserine sulfhydrylase;
GN Name=MCY1 {ECO:0000303|PubMed:27097106}; OrderedLocusNames=YGR012W;
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 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [2]
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 [3]
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 [4]
RP FUNCTION.
RX PubMed=9409150; DOI=10.1128/mmbr.61.4.503-532.1997;
RA Thomas D., Surdin-Kerjan Y.;
RT "Metabolism of sulfur amino acids in Saccharomyces cerevisiae.";
RL Microbiol. Mol. Biol. Rev. 61:503-532(1997).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT accumulation of a subclass of preproteins.";
RL Mol. Biol. Cell 17:1436-1450(2006).
RN [8]
RP GENE FAMILY.
RX PubMed=17482430; DOI=10.1016/j.resmic.2007.03.002;
RA Brzywczy J., Natorff R., Sienko M., Paszewski A.;
RT "Multiple fungal enzymes possess cysteine synthase activity in vitro.";
RL Res. Microbiol. 158:428-436(2007).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=27097106; DOI=10.7554/elife.13943;
RA Hughes A.L., Hughes C.E., Henderson K.A., Yazvenko N., Gottschling D.E.;
RT "Selective sorting and destruction of mitochondrial membrane proteins in
RT aged yeast.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Putative cysteine synthase that catalyzes the conversion of
CC O-acetyl-L-serine (OAS) into cysteine, the last step in the cysteine
CC biosynthesis pathway. However, this CS-like protein is unlikely to
CC function in cysteine biosynthesis. It seems that in S.cerevisiae
CC cysteine biosynthesis occurs exclusively through the cystathionine
CC pathway and not via direct incorporation of sulfur into OAS.
CC {ECO:0000305|PubMed:9409150}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC Evidence={ECO:0000250|UniProtKB:P0ABK5};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P0ABK5};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC Mitochondrion outer membrane {ECO:0000269|PubMed:16407407}; Single-pass
CC membrane protein {ECO:0000255}. Note=Selective removal from
CC mitochondrial outer membrane is achieved by sorting into a
CC mitochondrial-derived compartment, or MDC, followed by release through
CC mitochondrial fission and elimination by autophagy.
CC {ECO:0000269|PubMed:27097106}.
CC -!- MISCELLANEOUS: Present with 4650 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; Z72797; CAA96995.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08109.1; -; Genomic_DNA.
DR PIR; S64303; S64303.
DR RefSeq; NP_011526.1; NM_001181141.1.
DR AlphaFoldDB; P53206; -.
DR SMR; P53206; -.
DR BioGRID; 33255; 135.
DR IntAct; P53206; 1.
DR MINT; P53206; -.
DR STRING; 4932.YGR012W; -.
DR iPTMnet; P53206; -.
DR MaxQB; P53206; -.
DR PaxDb; P53206; -.
DR PRIDE; P53206; -.
DR EnsemblFungi; YGR012W_mRNA; YGR012W; YGR012W.
DR GeneID; 852895; -.
DR KEGG; sce:YGR012W; -.
DR SGD; S000003244; MCY1.
DR VEuPathDB; FungiDB:YGR012W; -.
DR eggNOG; KOG1481; Eukaryota.
DR HOGENOM; CLU_021018_1_0_1; -.
DR InParanoid; P53206; -.
DR OMA; FWDSGER; -.
DR PRO; PR:P53206; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53206; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..393
FT /note="Putative mitochondrial cysteine synthase"
FT /id="PRO_0000167130"
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 230..234
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P16703"
FT BINDING 338
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P16703"
FT MOD_RES 86
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P16703"
SQ SEQUENCE 393 AA; 42801 MW; 76C73396D77B69AC CRC64;
MSCSQNKTSV SLAWRECISI ASVLIGAYAS YKYYKLFKTR DIPRPKEGVE ELIGNTPLVK
IRSLTKATGV NIYAKLELCN PAGSAKDRVA LNIIKTAEEL GELVRGEPGW VFEGTSGSTG
ISIAVVCNAL GYRAHISLPD DTSLEKLALL ESLGATVNKV KPASIVDPNQ YVNAAKKACN
ELKKSGNGIR AVFADQFENE ANWKVHYQTT GPEIAHQTKG NIDAFIAGCG TGGTITGVAK
FLKERAKIPC HVVLADPQGS GFYNRVNYGV MYDYVEKEGT RRRHQVDTIV EGIGLNRITH
NFHMGEKFID ESIRVNDNQA IRMAKYLSVN DGLFVGSSTA INAVAAIQVA KTLPHGSNIV
IIACDSGSRH LSKFWKEAKE IDHDVSLEEV INI
