METC_YEAST
ID METC_YEAST Reviewed; 340 AA.
AC P43623; D6VTT7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Putative cystathionine beta-lyase;
DE Short=CBL;
DE EC=4.4.1.13;
DE AltName: Full=Beta-cystathionase;
DE AltName: Full=Cysteine lyase;
DE AltName: Full=Cysteine-S-conjugate beta-lyase;
DE AltName: Full=Increased recombination centers protein 7;
GN Name=IRC7; OrderedLocusNames=YFR055W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8686379;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<149::aid-yea893>3.0.co;2-g;
RA Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M.,
RA Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.;
RT "Analysis of a 36.2 kb DNA sequence including the right telomere of
RT chromosome VI from Saccharomyces cerevisiae.";
RL Yeast 12:149-167(1996).
RN [4]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) +
CC pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homocysteine from L-cystathionine: step 1/1.
CC -!- MISCELLANEOUS: Present with 2610 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D50617; BAA09295.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12497.1; -; Genomic_DNA.
DR PIR; S56311; S56311.
DR RefSeq; NP_116714.1; NM_001180021.1.
DR AlphaFoldDB; P43623; -.
DR SMR; P43623; -.
DR BioGRID; 31212; 85.
DR DIP; DIP-5187N; -.
DR IntAct; P43623; 1.
DR MINT; P43623; -.
DR STRING; 4932.YFR055W; -.
DR PaxDb; P43623; -.
DR PRIDE; P43623; -.
DR EnsemblFungi; YFR055W_mRNA; YFR055W; YFR055W.
DR GeneID; 850616; -.
DR KEGG; sce:YFR055W; -.
DR SGD; S000001952; IRC7.
DR VEuPathDB; FungiDB:YFR055W; -.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_5_1_1; -.
DR InParanoid; P43623; -.
DR OMA; GPYTYGR; -.
DR BioCyc; MetaCyc:YFR055W-MON; -.
DR BioCyc; YEAST:YFR055W-MON; -.
DR BRENDA; 4.4.1.13; 984.
DR UniPathway; UPA00051; UER00078.
DR PRO; PR:P43623; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43623; protein.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IBA:GO_Central.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IDA:SGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019450; P:L-cysteine catabolic process to pyruvate; IDA:SGD.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:SGD.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR006233; Cys_b_lyase_bac.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43500; PTHR43500; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01324; cysta_beta_ly_B; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Lyase; Methionine biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..340
FT /note="Putative cystathionine beta-lyase"
FT /id="PRO_0000114774"
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 36971 MW; 75FF4C7BDA038B8F CRC64;
MIDRTELSKF GITTQLSVIG RNPDEQSGFV NPPLYKGSTI ILKKLSDLEQ RKGRFYGTAG
SPTIDNLENA WTHLTGGAGT VLSASGLGSI SLALLALSKA GDHILMTDSV YVPTRMLCDG
LLAKFGVETD YYDPSIGKDI EKLVKPNTTV IFLESPGSGT MEVQDIPALV SVAKKHGIKT
ILDNTWATPL FFDAHAHGID ISVEAGTKYL GGHSDLLIGL ASANEECWPL LRSTYDAMAM
LPGAEDCQLA LRGMRTLHLR LKEVERKALD LAAWLGNRDE VEKVLHPAFE DCPGHEYWVR
DYKGSSGLFS IVLKNGFTRA GLEKMVEGMK VLQLGFSWGG
