ID   METB_MYCBO              Reviewed;         388 AA.
AC   P66876; A0A1R3XXA4; O53427; X2BGV2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 114.
DE   RecName: Full=Cystathionine gamma-synthase;
DE            Short=CGS;
DE            EC=2.5.1.48;
DE   AltName: Full=O-succinylhomoserine (thiol)-lyase;
GN   Name=metB; OrderedLocusNames=BQ2027_MB1108;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Catalyzes the formation of L-cystathionine from O-succinyl-L-
CC       homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In
CC       the absence of thiol, catalyzes gamma-elimination to form 2-
CC       oxobutanoate, succinate and ammonia (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-succinyl-L-homoserine + L-cysteine = L,L-cystathionine +
CC         succinate + H(+); Xref=Rhea:RHEA:20397, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:35235, ChEBI:CHEBI:57661,
CC         ChEBI:CHEBI:58161; EC=2.5.1.48;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000305}.
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DR   EMBL; LT708304; SIT99707.1; -; Genomic_DNA.
DR   RefSeq; WP_003405736.1; NC_002945.4.
DR   AlphaFoldDB; P66876; -.
DR   SMR; P66876; -.
DR   GeneID; 45425051; -.
DR   KEGG; mbo:BQ2027_MB1108; -.
DR   PATRIC; fig|233413.5.peg.1209; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:TreeGrafter.
DR   GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 1.
DR   FunFam; 3.90.1150.10:FF:000008; Cystathionine gamma-synthase; 1.
DR   FunFam; 3.40.640.10:FF:000009; Cystathionine gamma-synthase homolog; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR054542; Cys_met_metab_PP.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF005871; PRK07811.1; 1.
DR   PANTHER; PTHR11808:SF15; CYSTATHIONINE GAMMA-LYASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Methionine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..388
FT                   /note="Cystathionine gamma-synthase"
FT                   /id="PRO_0000114763"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         208
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  40982 MW;  B6D9C0F78F3EAE71 CRC64;
     MSEDRTGHQG ISGPATRAIH AGYRPDPATG AVNVPIYASS TFAQDGVGGL RGGFEYARTG
     NPTRAALEAS LAAVEEGAFA RAFSSGMAAT DCALRAMLRP GDHVVIPDDA YGGTFRLIDK
     VFTRWDVQYT PVRLADLDAV GAAITPRTRL IWVETPTNPL LSIADITAIA ELGTDRSAKV
     LVDNTFASPA LQQPLRLGAD VVLHSTTKYI GGHSDVVGGA LVTNDEELDE EFAFLQNGAG
     AVPGPFDAYL TMRGLKTLVL RMQRHSENAC AVAEFLADHP SVSSVLYPGL PSHPGHEIAA
     RQMRGFGGMV SVRMRAGRRA AQDLCAKTRV FILAESLGGV ESLIEHPSAM THASTAGSQL
     EVPDDLVRLS VGIEDIADLL GDLEQALG
//