ID   METB_MYCTO              Reviewed;         388 AA.
AC   P9WGB6; L0T5M9; O53427; P66875;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
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=MT1110;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the formation of L-cystathionine from O-succinyl-L-
CC       homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteine + O-succinyl-L-homoserine = H(+) + L,L-
CC         cystathionine + succinate; 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   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-cystathionine from O-succinyl-L-homoserine: step 1/1.
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; AE000516; AAK45366.1; -; Genomic_DNA.
DR   PIR; E70894; E70894.
DR   RefSeq; WP_003405736.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGB6; -.
DR   SMR; P9WGB6; -.
DR   EnsemblBacteria; AAK45366; AAK45366; MT1110.
DR   GeneID; 45425051; -.
DR   KEGG; mtc:MT1110; -.
DR   PATRIC; fig|83331.31.peg.1195; -.
DR   HOGENOM; CLU_018986_2_0_11; -.
DR   UniPathway; UPA00051; UER00077.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Methionine biosynthesis;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..388
FT                   /note="Cystathionine gamma-synthase"
FT                   /id="PRO_0000428390"
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