METB_MYCTU
ID METB_MYCTU Reviewed; 388 AA.
AC P9WGB7; 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 40.
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=Rv1079; ORFNames=MTV017.32;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, COFACTOR, KINETIC PARAMETERS, SUBUNIT, AND 3D-STRUCTURE MODELING.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19428471; DOI=10.1016/j.ijbiomac.2009.02.007;
RA Saha B., Mukherjee S., Das A.K.;
RT "Molecular characterization of Mycobacterium tuberculosis cystathionine
RT gamma synthase--apo- and holoforms.";
RL Int. J. Biol. Macromol. 44:385-392(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the formation of L-cystathionine from O-succinyl-L-
CC homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction (By
CC similarity). In the absence of thiol, catalyzes gamma-elimination to
CC form 2-oxobutanoate, succinate and ammonia. {ECO:0000250,
CC ECO:0000269|PubMed:19428471}.
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:0000269|PubMed:19428471};
CC Note=Binds 1 pyridoxal phosphate per subunit.
CC {ECO:0000269|PubMed:19428471};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.32 mM for O-succinyl-L-homoserine (at pH 7.5 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:19428471};
CC Note=The KM value was measured when assaying the gamma-elimination
CC reaction.;
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:0000269|PubMed:19428471}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP43830.1; -; Genomic_DNA.
DR PIR; E70894; E70894.
DR RefSeq; NP_215595.1; NC_000962.3.
DR RefSeq; WP_003405736.1; NZ_NVQJ01000080.1.
DR AlphaFoldDB; P9WGB7; -.
DR SMR; P9WGB7; -.
DR STRING; 83332.Rv1079; -.
DR PaxDb; P9WGB7; -.
DR DNASU; 887103; -.
DR GeneID; 45425051; -.
DR GeneID; 887103; -.
DR KEGG; mtu:Rv1079; -.
DR TubercuList; Rv1079; -.
DR eggNOG; COG0626; Bacteria.
DR OMA; YKQDGVG; -.
DR PhylomeDB; P9WGB7; -.
DR Reactome; R-MTU-937250; Sulfur amino acid metabolism.
DR UniPathway; UPA00051; UER00077.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IDA:MTBBASE.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IDA:MTBBASE.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IMP:MTBBASE.
DR GO; GO:0019279; P:L-methionine biosynthetic process from L-homoserine via cystathionine; IMP:MTBBASE.
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..388
FT /note="Cystathionine gamma-synthase"
FT /id="PRO_0000114762"
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:0000305"
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
