METC_BACSU
ID METC_BACSU Reviewed; 390 AA.
AC O31632;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cystathionine beta-lyase MetC;
DE Short=CBL;
DE EC=4.4.1.13;
DE AltName: Full=Beta-cystathionase MetC;
DE AltName: Full=Cysteine lyase MetC;
DE AltName: Full=Cysteine-S-conjugate beta-lyase MetC;
GN Name=metC; Synonyms=yjcJ; OrderedLocusNames=BSU11880;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, COFACTOR, DISRUPTION PHENOTYPE, AND
RP INDUCTION.
RC STRAIN=168;
RX PubMed=11832514; DOI=10.1099/00221287-148-2-507;
RA Auger S., Yuen W.H., Danchin A., Martin-Verstraete I.;
RT "The metIC operon involved in methionine biosynthesis in Bacillus subtilis
RT is controlled by transcription antitermination.";
RL Microbiology 148:507-518(2002).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=15760717; DOI=10.1016/j.biochi.2004.09.007;
RA Auger S., Gomez M.P., Danchin A., Martin-Verstraete I.;
RT "The PatB protein of Bacillus subtilis is a C-S-lyase.";
RL Biochimie 87:231-238(2005).
CC -!- FUNCTION: Catalyzes the transformation of cystathionine into
CC homocysteine. Also exhibits cysteine desulfhydrase activity in vitro,
CC producing sulfide from cysteine. {ECO:0000269|PubMed:11832514,
CC ECO:0000269|PubMed:15760717}.
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:0000269|PubMed:11832514};
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 Evidence={ECO:0000305|PubMed:11832514};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.64 mM for cystathionine {ECO:0000269|PubMed:15760717};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homocysteine from L-cystathionine: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Up-regulated at the transcriptional level when sulfate,
CC cysteine, cystathionine or homocysteine are the sulfur sources.
CC Repressed by methionine. {ECO:0000269|PubMed:11832514}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow as well as the wild-
CC type in the presence of sulfate, cysteine, homocysteine or methionine
CC as sole sulfur source, but do not grow in the presence of
CC cystathionine. {ECO:0000269|PubMed:11832514,
CC ECO:0000269|PubMed:15760717}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB13045.1; -; Genomic_DNA.
DR PIR; B69847; B69847.
DR RefSeq; NP_389070.1; NC_000964.3.
DR RefSeq; WP_003244787.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31632; -.
DR SMR; O31632; -.
DR STRING; 224308.BSU11880; -.
DR PaxDb; O31632; -.
DR PRIDE; O31632; -.
DR EnsemblBacteria; CAB13045; CAB13045; BSU_11880.
DR GeneID; 936424; -.
DR KEGG; bsu:BSU11880; -.
DR PATRIC; fig|224308.179.peg.1280; -.
DR eggNOG; COG0626; Bacteria.
DR InParanoid; O31632; -.
DR OMA; THGGIIV; -.
DR PhylomeDB; O31632; -.
DR BioCyc; BSUB:BSU11880-MON; -.
DR SABIO-RK; O31632; -.
DR UniPathway; UPA00051; UER00078.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:RHEA.
DR GO; GO:0004123; F:cystathionine gamma-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; IBA:GO_Central.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IBA:GO_Central.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808; PTHR11808; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cytoplasm; Lyase; Methionine biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..390
FT /note="Cystathionine beta-lyase MetC"
FT /id="PRO_0000360655"
FT MOD_RES 200
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 390 AA; 42491 MW; 8E8C058802DFDD7F CRC64;
MSKHNWTLET QLVHNPFKTD GGTGAVSVPI QHASTFHQSS FEEFGAYDYS RSGTPTRTAL
EETIAALEGG TRGFAFSSGM AAISTAFLLL SQGDHVLVTE DVYGGTFRMV TEVLTRFGIE
HTFVDMTDRN EVARSIKPNT KVIYMETPSN PTLGITDIKA VVQLAKENGC LTFLDNTFMT
PALQRPLDLG VDIVLHSATK FLSGHSDVLS GLAAVKDEEL GKQLYKLQNA FGAVLGVQDC
WLVLRGLKTL QVRLEKASQT AQRLAEFFQK HPAVKRVYYP GLADHPGAET HKSQSTGAGA
VLSFELESKE AVKKLVENVS LPVFAVSLGA VESILSYPAT MSHAAMPKEE REKRGITDGL
LRLSVGVEHA DDLEHDFEQA LKEIAPVSVR
