METB_ECOLI
ID METB_ECOLI Reviewed; 386 AA.
AC P00935; Q2M8N5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 187.
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=b3939, JW3910;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6361020; DOI=10.1016/s0021-9258(17)43743-4;
RA Duchange N., Zakin M.M., Ferrara P., Saint-Girons I., Park I., Tran S.V.,
RA Py M.-C., Cohen G.N.;
RT "Structure of the metJBLF cluster in Escherichia coli K12. Sequence of the
RT metB structural gene and of the 5'- and 3'-flanking regions of the metBL
RT operon.";
RL J. Biol. Chem. 258:14868-14871(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 182-209.
RX PubMed=3307782; DOI=10.1016/0006-291x(87)90968-5;
RA Martel A., Bouthier de la Tour C., Le Goffic F.;
RT "Pyridoxal 5'phosphate binding site of Escherichia coli beta cystathionase
RT and cystathionine gamma synthase comparison of their sequences.";
RL Biochem. Biophys. Res. Commun. 147:565-571(1987).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=2405903; DOI=10.1021/bi00454a019;
RA Holbrook E.L., Greene R.C., Krueger J.H.;
RT "Purification and properties of cystathionine gamma-synthase from
RT overproducing strains of Escherichia coli.";
RL Biochemistry 29:435-442(1990).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), SUBUNIT, AND PYRIDOXAL PHOSPHATE AT
RP LYS-198.
RX PubMed=9843488; DOI=10.1093/emboj/17.23.6827;
RA Clausen T., Huber R., Prade L., Wahl M.C., Messerschmidt A.;
RT "Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5-
RT A resolution.";
RL EMBO J. 17:6827-6838(1998).
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. {ECO:0000269|PubMed:2405903}.
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 Evidence={ECO:0000269|PubMed:2405903};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:2405903};
CC Note=Binds 1 pyridoxal phosphate per subunit.
CC {ECO:0000269|PubMed:2405903};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.33 mM for O-succinyl-L-homoserine (at pH 8.2 and 25 degrees
CC Celsius, when assaying the gamma-elimination reaction)
CC {ECO:0000269|PubMed:2405903};
CC KM=1.0 mM for O-succinyl-L-homoserine (at pH 8.2 and 25 degrees
CC Celsius, when assaying the gamma-replacement reaction)
CC {ECO:0000269|PubMed:2405903};
CC KM=0.05 mM for L-cysteine (at pH 8.2 and 25 degrees Celsius, when
CC assaying the gamma-replacement reaction)
CC {ECO:0000269|PubMed:2405903};
CC Note=kcat are 700 min(-1) and 460 min (-1) for the gamma-replacement
CC and gamma-elimination reaction, respectively.;
CC pH dependence:
CC Optimum pH is 7.8 for the gamma-replacement reaction.
CC {ECO:0000269|PubMed:2405903};
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:2405903,
CC ECO:0000269|PubMed:9843488}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; K01546; AAA24167.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03071.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76921.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77371.1; -; Genomic_DNA.
DR PIR; A01158; SYECCG.
DR RefSeq; NP_418374.1; NC_000913.3.
DR RefSeq; WP_001295694.1; NZ_SSZK01000014.1.
DR PDB; 1CS1; X-ray; 1.50 A; A/B/C/D=1-386.
DR PDBsum; 1CS1; -.
DR AlphaFoldDB; P00935; -.
DR SMR; P00935; -.
DR BioGRID; 4261102; 19.
DR DIP; DIP-10192N; -.
DR IntAct; P00935; 1.
DR STRING; 511145.b3939; -.
DR DrugBank; DB04083; N(6)-(pyridoxal phosphate)-L-lysine.
DR jPOST; P00935; -.
DR PaxDb; P00935; -.
DR PRIDE; P00935; -.
DR EnsemblBacteria; AAC76921; AAC76921; b3939.
DR EnsemblBacteria; BAE77371; BAE77371; BAE77371.
DR GeneID; 66672150; -.
DR GeneID; 948434; -.
DR KEGG; ecj:JW3910; -.
DR KEGG; eco:b3939; -.
DR PATRIC; fig|1411691.4.peg.2766; -.
DR EchoBASE; EB0577; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_6; -.
DR InParanoid; P00935; -.
DR OMA; YKQDGVG; -.
DR PhylomeDB; P00935; -.
DR BioCyc; EcoCyc:O-SUCCHOMOSERLYASE-MON; -.
DR BioCyc; MetaCyc:O-SUCCHOMOSERLYASE-MON; -.
DR BRENDA; 2.5.1.48; 2026.
DR SABIO-RK; P00935; -.
DR UniPathway; UPA00051; UER00077.
DR EvolutionaryTrace; P00935; -.
DR PRO; PR:P00935; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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:0003962; F:cystathionine gamma-synthase activity; IDA:EcoCyc.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IBA:GO_Central.
DR GO; GO:0009086; P:methionine biosynthetic process; IMP:EcoCyc.
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; IPR011821; O_succ_thio_ly.
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 TIGRFAMs; TIGR02080; O_succ_thio_ly; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm;
KW Direct protein sequencing; Methionine biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..386
FT /note="Cystathionine gamma-synthase"
FT /id="PRO_0000114756"
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:3307782"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:1CS1"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:1CS1"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1CS1"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1CS1"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:1CS1"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:1CS1"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:1CS1"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:1CS1"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1CS1"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:1CS1"
FT HELIX 156..165
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1CS1"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:1CS1"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1CS1"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:1CS1"
FT HELIX 216..228
FT /evidence="ECO:0007829|PDB:1CS1"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:1CS1"
FT HELIX 248..266
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:1CS1"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 298..306
FT /evidence="ECO:0007829|PDB:1CS1"
FT HELIX 308..316
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:1CS1"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:1CS1"
FT TURN 340..344
FT /evidence="ECO:0007829|PDB:1CS1"
FT HELIX 347..352
FT /evidence="ECO:0007829|PDB:1CS1"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:1CS1"
FT HELIX 369..383
FT /evidence="ECO:0007829|PDB:1CS1"
SQ SEQUENCE 386 AA; 41550 MW; 423B825219A42E9E CRC64;
MTRKQATIAV RSGLNDDEQY GCVVPPIHLS STYNFTGFNE PRAHDYSRRG NPTRDVVQRA
LAELEGGAGA VLTNTGMSAI HLVTTVFLKP GDLLVAPHDC YGGSYRLFDS LAKRGCYRVL
FVDQGDEQAL RAALAEKPKL VLVESPSNPL LRVVDIAKIC HLAREVGAVS VVDNTFLSPA
LQNPLALGAD LVLHSCTKYL NGHSDVVAGV VIAKDPDVVT ELAWWANNIG VTGGAFDSYL
LLRGLRTLVP RMELAQRNAQ AIVKYLQTQP LVKKLYHPSL PENQGHEIAA RQQKGFGAML
SFELDGDEQT LRRFLGGLSL FTLAESLGGV ESLISHAATM THAGMAPEAR AAAGISETLL
RISTGIEDGE DLIADLENGF RAANKG
