METI_BACSU
ID METI_BACSU Reviewed; 373 AA.
AC O31631;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cystathionine gamma-synthase/O-acetylhomoserine (thiol)-lyase;
DE Short=CGS/OAH thiolyase;
DE EC=2.5.1.-;
DE AltName: Full=O-acetylhomoserine sulfhydrylase;
DE Short=OAH sulfhydrylase;
GN Name=metI; Synonyms=yjcI; OrderedLocusNames=BSU11870;
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).
CC -!- FUNCTION: Catalyzes the formation of L-cystathionine from O-acetyl-L-
CC homoserine and L-cysteine. Cannot use O-succinyl-L-homoserine as
CC substrate. Also exhibits O-acetylhomoserine thiolyase activity,
CC catalyzing the synthesis of L-homocysteine from O-acetyl-L-homoserine
CC and sulfide. {ECO:0000269|PubMed:11832514}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine + O-acetyl-L-homoserine = acetate + H(+) + L,L-
CC cystathionine; Xref=Rhea:RHEA:30931, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:35235, ChEBI:CHEBI:57716,
CC ChEBI:CHEBI:58161; Evidence={ECO:0000269|PubMed:11832514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-acetyl-L-homoserine = acetate + L-
CC homocysteine; Xref=Rhea:RHEA:27822, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57716, ChEBI:CHEBI:58199;
CC Evidence={ECO:0000269|PubMed:11832514};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305|PubMed:11832514};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway.
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 are unable to grow in the
CC presence of sulfate or cysteine as sole sulfur source, whereas their
CC growth in the presence of homocysteine, cystathionine or methionine is
CC similar to that of the wild-type strain. {ECO:0000269|PubMed:11832514}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB13044.1; -; Genomic_DNA.
DR PIR; A69847; A69847.
DR RefSeq; NP_389069.1; NC_000964.3.
DR RefSeq; WP_003232857.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31631; -.
DR SMR; O31631; -.
DR IntAct; O31631; 1.
DR MINT; O31631; -.
DR STRING; 224308.BSU11870; -.
DR PaxDb; O31631; -.
DR PRIDE; O31631; -.
DR EnsemblBacteria; CAB13044; CAB13044; BSU_11870.
DR GeneID; 939812; -.
DR KEGG; bsu:BSU11870; -.
DR PATRIC; fig|224308.179.peg.1279; -.
DR eggNOG; COG0626; Bacteria.
DR InParanoid; O31631; -.
DR OMA; YKQDGVG; -.
DR PhylomeDB; O31631; -.
DR BioCyc; BSUB:BSU11870-MON; -.
DR UniPathway; UPA00051; -.
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:0004123; F:cystathionine gamma-lyase activity; IBA:GO_Central.
DR GO; GO:0051009; F:O-acetylhomoserine sulfhydrylase activity; IEA:RHEA.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; Methionine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..373
FT /note="Cystathionine gamma-synthase/O-acetylhomoserine
FT (thiol)-lyase"
FT /id="PRO_0000360654"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 373 AA; 41705 MW; A7B849C730213602 CRC64;
MSQHVETKLA QIGNRSDEVT GTVSAPIYLS TAYRHRGIGE STGFDYVRTK NPTRQLVEDA
IANLENGARG LAFSSGMAAI QTIMALFKSG DELIVSSDLY GGTYRLFENE WKKYGLTFHY
DDFSDEDCLR SKITPNTKAV FVETPTNPLM QEADIEHIAR ITKEHGLLLI VDNTFYTPVL
QRPLELGADI VIHSATKYLG GHNDLLAGLV VVKDERLGEE MFQHQNAIGA VLPPFDSWLL
MRGMKTLSLR MRQHQANAQE LAAFLEEQEE ISDVLYPGKG GMLSFRLQKE EWVNPFLKAL
KTICFAESLG GVESFITYPA TQTHMDIPEE IRIANGVCNR LLRFSVGIEH AEDLKEDLKQ
ALCQVKEGAV SFE
