METC_SALTY
ID METC_SALTY Reviewed; 395 AA.
AC P18949;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Cystathionine beta-lyase;
DE Short=CBL;
DE EC=4.4.1.13 {ECO:0000250|UniProtKB:P06721};
DE AltName: Full=Beta-cystathionase;
DE AltName: Full=Cysteine lyase;
DE AltName: Full=Cysteine-S-conjugate beta-lyase;
GN Name=metC; OrderedLocusNames=STM3161;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=2659970; DOI=10.1007/bf00332246;
RA Park Y.M., Stauffer G.V.;
RT "DNA sequence of the metC gene and its flanking regions from Salmonella
RT typhimurium LT2 and homology with the corresponding sequence of Escherichia
RT coli.";
RL Mol. Gen. Genet. 216:164-169(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Catalyzes the cleavage of cystathionine to homocysteine,
CC pyruvate and ammonia during methionine biosynthesis.
CC {ECO:0000250|UniProtKB:P06721}.
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 Evidence={ECO:0000250|UniProtKB:P06721};
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 Evidence={ECO:0000250|UniProtKB:P06721};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P06721};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homocysteine from L-cystathionine: step 1/1.
CC {ECO:0000250|UniProtKB:P06721}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P06721}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06721}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL22035.1; -; Genomic_DNA.
DR PIR; JV0020; JV0020.
DR RefSeq; NP_462076.1; NC_003197.2.
DR RefSeq; WP_000130262.1; NC_003197.2.
DR AlphaFoldDB; P18949; -.
DR SMR; P18949; -.
DR STRING; 99287.STM3161; -.
DR PaxDb; P18949; -.
DR EnsemblBacteria; AAL22035; AAL22035; STM3161.
DR GeneID; 1254684; -.
DR KEGG; stm:STM3161; -.
DR PATRIC; fig|99287.12.peg.3350; -.
DR HOGENOM; CLU_018986_5_1_6; -.
DR OMA; GPYTYGR; -.
DR PhylomeDB; P18949; -.
DR BioCyc; SENT99287:STM3161-MON; -.
DR UniPathway; UPA00051; UER00078.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IBA:GO_Central.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019450; P:L-cysteine catabolic process to pyruvate; IBA:GO_Central.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Lyase; Methionine biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..395
FT /note="Cystathionine beta-lyase"
FT /id="PRO_0000114769"
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P06721"
FT CONFLICT 195
FT /note="K -> E (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="D -> H (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 42872 MW; 38B0A41A1A063447 CRC64;
MTDKQLDTKL VNAGRSKKYT LGSVNSVIQR ASSLVFDTVE AKKHATRNLA NGELFYGRRG
TLTHFSLQEA MCELEGGAGC ALFPCGAAAV ANTILAFVEQ GDHILMTNTA YEPSQDFCSK
ILGKLGVTTS WFDPLIGADI TQHIQPNTKV VFLESPGSIT MEVHDIPSIV SAVRRVAPEA
VIMIDNTWAA GVLFKALEFD IDISIQAGTK YLIGHSDAMV GTAVANARCW EQLRENAYLM
GQMLDADTAY MTSRGLRTLG VRLRQHQESS LKIAAWLANH PQVARVNHPA LPGSKGHAFW
KRDFTGSSGL FSFVLNKKLT EAELSAYLDN FSLFSMAYSW GGYESLIIAN QPEQIAAIRP
AGGVDFTGTL VRVHIGLESV DDLIADLAAG FARIV
