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Protein

Cystathionine gamma-synthase

Gene

metB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia.1 Publication

Catalytic activityi

O(4)-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate.1 Publication

Cofactori

pyridoxal 5'-phosphate1 PublicationNote: Binds 1 pyridoxal phosphate per subunit.1 Publication

Kineticsi

kcat are 700 min(-1) and 460 min (-1) for the gamma-replacement and gamma-elimination reaction, respectively.

  1. KM=0.33 mM for O-succinyl-L-homoserine (at pH 8.2 and 25 degrees Celsius, when assaying the gamma-elimination reaction)1 Publication
  2. KM=1.0 mM for O-succinyl-L-homoserine (at pH 8.2 and 25 degrees Celsius, when assaying the gamma-replacement reaction)1 Publication
  3. KM=0.05 mM for L-cysteine (at pH 8.2 and 25 degrees Celsius, when assaying the gamma-replacement reaction)1 Publication

    pH dependencei

    Optimum pH is 7.8 for the gamma-replacement reaction.1 Publication

    Pathway:iL-methionine biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes L-cystathionine from O-succinyl-L-homoserine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Cystathionine gamma-synthase (metB)
    This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-cystathionine from O-succinyl-L-homoserine, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

    GO - Molecular functioni

    • cystathionine gamma-synthase activity Source: EcoCyc
    • pyridoxal phosphate binding Source: EcoCyc

    GO - Biological processi

    • methionine biosynthetic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Methionine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:O-SUCCHOMOSERLYASE-MONOMER.
    ECOL316407:JW3910-MONOMER.
    MetaCyc:O-SUCCHOMOSERLYASE-MONOMER.
    BRENDAi2.5.1.48. 2026.
    SABIO-RKP00935.
    UniPathwayiUPA00051; UER00077.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cystathionine gamma-synthase (EC:2.5.1.48)
    Short name:
    CGS
    Alternative name(s):
    O-succinylhomoserine (thiol)-lyase
    Gene namesi
    Name:metB
    Ordered Locus Names:b3939, JW3910
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10582. metB.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 386386Cystathionine gamma-synthasePRO_0000114756Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei198 – 1981N6-(pyridoxal phosphate)lysine1 Publication

    Proteomic databases

    PaxDbiP00935.
    PRIDEiP00935.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    DIPiDIP-10192N.
    IntActiP00935. 1 interaction.
    STRINGi511145.b3939.

    Structurei

    Secondary structure

    1
    386
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 117Combined sources
    Turni12 – 154Combined sources
    Turni18 – 203Combined sources
    Beta strandi22 – 243Combined sources
    Beta strandi31 – 333Combined sources
    Turni47 – 493Combined sources
    Helixi52 – 6514Combined sources
    Beta strandi68 – 758Combined sources
    Helixi76 – 8712Combined sources
    Beta strandi93 – 975Combined sources
    Helixi102 – 11211Combined sources
    Turni113 – 1153Combined sources
    Beta strandi118 – 1225Combined sources
    Helixi127 – 1359Combined sources
    Beta strandi139 – 1446Combined sources
    Turni148 – 1503Combined sources
    Helixi156 – 16510Combined sources
    Beta strandi169 – 1735Combined sources
    Turni175 – 1773Combined sources
    Turni179 – 1813Combined sources
    Helixi184 – 1874Combined sources
    Beta strandi190 – 1956Combined sources
    Turni196 – 2016Combined sources
    Beta strandi209 – 2157Combined sources
    Helixi216 – 22813Combined sources
    Helixi235 – 24511Combined sources
    Helixi248 – 26619Combined sources
    Beta strandi272 – 2765Combined sources
    Helixi286 – 2927Combined sources
    Beta strandi298 – 3069Combined sources
    Helixi308 – 3169Combined sources
    Beta strandi319 – 3257Combined sources
    Beta strandi329 – 3313Combined sources
    Beta strandi333 – 3364Combined sources
    Helixi337 – 3393Combined sources
    Turni340 – 3445Combined sources
    Helixi347 – 3526Combined sources
    Beta strandi359 – 3635Combined sources
    Helixi369 – 38315Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CS1X-ray1.50A/B/C/D1-386[»]
    ProteinModelPortaliP00935.
    SMRiP00935. Positions 3-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00935.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the trans-sulfuration enzymes family.Curated

    Phylogenomic databases

    eggNOGiCOG0626.
    HOGENOMiHOG000246415.
    InParanoidiP00935.
    KOiK01739.
    OMAiTHACIPK.
    OrthoDBiEOG67DPN3.
    PhylomeDBiP00935.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
    IPR011821. O_succ_thio_ly.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR11808. PTHR11808. 1 hit.
    PfamiPF01053. Cys_Met_Meta_PP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001434. CGS. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR02080. O_succ_thio_ly. 1 hit.
    PROSITEiPS00868. CYS_MET_METAB_PP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00935-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTRKQATIAV RSGLNDDEQY GCVVPPIHLS STYNFTGFNE PRAHDYSRRG
    60 70 80 90 100
    NPTRDVVQRA LAELEGGAGA VLTNTGMSAI HLVTTVFLKP GDLLVAPHDC
    110 120 130 140 150
    YGGSYRLFDS LAKRGCYRVL FVDQGDEQAL RAALAEKPKL VLVESPSNPL
    160 170 180 190 200
    LRVVDIAKIC HLAREVGAVS VVDNTFLSPA LQNPLALGAD LVLHSCTKYL
    210 220 230 240 250
    NGHSDVVAGV VIAKDPDVVT ELAWWANNIG VTGGAFDSYL LLRGLRTLVP
    260 270 280 290 300
    RMELAQRNAQ AIVKYLQTQP LVKKLYHPSL PENQGHEIAA RQQKGFGAML
    310 320 330 340 350
    SFELDGDEQT LRRFLGGLSL FTLAESLGGV ESLISHAATM THAGMAPEAR
    360 370 380
    AAAGISETLL RISTGIEDGE DLIADLENGF RAANKG
    Length:386
    Mass (Da):41,550
    Last modified:July 21, 1986 - v1
    Checksum:i423B825219A42E9E
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    K01546 Genomic DNA. Translation: AAA24167.1.
    L19201 Genomic DNA. Translation: AAB03071.1.
    U00096 Genomic DNA. Translation: AAC76921.1.
    AP009048 Genomic DNA. Translation: BAE77371.1.
    PIRiA01158. SYECCG.
    RefSeqiNP_418374.1. NC_000913.3.
    WP_001295694.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76921; AAC76921; b3939.
    BAE77371; BAE77371; BAE77371.
    GeneIDi948434.
    KEGGieco:b3939.
    PATRICi32123397. VBIEscCol129921_4059.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    K01546 Genomic DNA. Translation: AAA24167.1.
    L19201 Genomic DNA. Translation: AAB03071.1.
    U00096 Genomic DNA. Translation: AAC76921.1.
    AP009048 Genomic DNA. Translation: BAE77371.1.
    PIRiA01158. SYECCG.
    RefSeqiNP_418374.1. NC_000913.3.
    WP_001295694.1. NZ_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CS1X-ray1.50A/B/C/D1-386[»]
    ProteinModelPortaliP00935.
    SMRiP00935. Positions 3-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-10192N.
    IntActiP00935. 1 interaction.
    STRINGi511145.b3939.

    Proteomic databases

    PaxDbiP00935.
    PRIDEiP00935.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76921; AAC76921; b3939.
    BAE77371; BAE77371; BAE77371.
    GeneIDi948434.
    KEGGieco:b3939.
    PATRICi32123397. VBIEscCol129921_4059.

    Organism-specific databases

    EchoBASEiEB0577.
    EcoGeneiEG10582. metB.

    Phylogenomic databases

    eggNOGiCOG0626.
    HOGENOMiHOG000246415.
    InParanoidiP00935.
    KOiK01739.
    OMAiTHACIPK.
    OrthoDBiEOG67DPN3.
    PhylomeDBiP00935.

    Enzyme and pathway databases

    UniPathwayiUPA00051; UER00077.
    BioCyciEcoCyc:O-SUCCHOMOSERLYASE-MONOMER.
    ECOL316407:JW3910-MONOMER.
    MetaCyc:O-SUCCHOMOSERLYASE-MONOMER.
    BRENDAi2.5.1.48. 2026.
    SABIO-RKP00935.

    Miscellaneous databases

    EvolutionaryTraceiP00935.
    PROiP00935.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
    IPR011821. O_succ_thio_ly.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR11808. PTHR11808. 1 hit.
    PfamiPF01053. Cys_Met_Meta_PP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001434. CGS. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR02080. O_succ_thio_ly. 1 hit.
    PROSITEiPS00868. CYS_MET_METAB_PP. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Structure of the metJBLF cluster in Escherichia coli K12. Sequence of the metB structural gene and of the 5'- and 3'-flanking regions of the metBL operon."
      Duchange N., Zakin M.M., Ferrara P., Saint-Girons I., Park I., Tran S.V., Py M.-C., Cohen G.N.
      J. Biol. Chem. 258:14868-14871(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
      Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Pyridoxal 5'phosphate binding site of Escherichia coli beta cystathionase and cystathionine gamma synthase comparison of their sequences."
      Martel A., Bouthier de la Tour C., Le Goffic F.
      Biochem. Biophys. Res. Commun. 147:565-571(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 182-209.
    6. "Purification and properties of cystathionine gamma-synthase from overproducing strains of Escherichia coli."
      Holbrook E.L., Greene R.C., Krueger J.H.
      Biochemistry 29:435-442(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    7. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    8. "Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5-A resolution."
      Clausen T., Huber R., Prade L., Wahl M.C., Messerschmidt A.
      EMBO J. 17:6827-6838(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-198.

    Entry informationi

    Entry nameiMETB_ECOLI
    AccessioniPrimary (citable) accession number: P00935
    Secondary accession number(s): Q2M8N5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: July 22, 2015
    This is version 147 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.