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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

    Pathwayi: L-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-lyase activity Source: GO_Central
    • cystathionine gamma-synthase activity Source: EcoCyc
    • pyridoxal phosphate binding Source: EcoCyc

    GO - Biological processi

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 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)DescriptionActionsGraphical viewLength
    ChainiPRO_00001147561 – 386Cystathionine gamma-synthaseAdd BLAST386

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei198N6-(pyridoxal phosphate)lysine1 Publication1

    Proteomic databases

    EPDiP00935.
    PaxDbiP00935.
    PRIDEiP00935.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    BioGridi4261102. 18 interactors.
    DIPiDIP-10192N.
    IntActiP00935. 1 interactor.
    STRINGi511145.b3939.

    Structurei

    Secondary structure

    1386
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi5 – 11Combined sources7
    Turni12 – 15Combined sources4
    Turni18 – 20Combined sources3
    Beta strandi22 – 24Combined sources3
    Beta strandi31 – 33Combined sources3
    Turni47 – 49Combined sources3
    Helixi52 – 65Combined sources14
    Beta strandi68 – 75Combined sources8
    Helixi76 – 87Combined sources12
    Beta strandi93 – 97Combined sources5
    Helixi102 – 112Combined sources11
    Turni113 – 115Combined sources3
    Beta strandi118 – 122Combined sources5
    Helixi127 – 135Combined sources9
    Beta strandi139 – 144Combined sources6
    Turni148 – 150Combined sources3
    Helixi156 – 165Combined sources10
    Beta strandi169 – 173Combined sources5
    Turni175 – 177Combined sources3
    Turni179 – 181Combined sources3
    Helixi184 – 187Combined sources4
    Beta strandi190 – 195Combined sources6
    Turni196 – 201Combined sources6
    Beta strandi209 – 215Combined sources7
    Helixi216 – 228Combined sources13
    Helixi235 – 245Combined sources11
    Helixi248 – 266Combined sources19
    Beta strandi272 – 276Combined sources5
    Helixi286 – 292Combined sources7
    Beta strandi298 – 306Combined sources9
    Helixi308 – 316Combined sources9
    Beta strandi319 – 325Combined sources7
    Beta strandi329 – 331Combined sources3
    Beta strandi333 – 336Combined sources4
    Helixi337 – 339Combined sources3
    Turni340 – 344Combined sources5
    Helixi347 – 352Combined sources6
    Beta strandi359 – 363Combined sources5
    Helixi369 – 383Combined sources15

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP00935.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the trans-sulfuration enzymes family.Curated

    Phylogenomic databases

    eggNOGiENOG4105C28. Bacteria.
    COG0626. LUCA.
    HOGENOMiHOG000246415.
    InParanoidiP00935.
    KOiK01739.
    OMAiTHACIPK.
    PhylomeDBiP00935.

    Family and domain databases

    CDDicd00614. CGS_like. 1 hit.
    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_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76921; AAC76921; b3939.
    BAE77371; BAE77371; BAE77371.
    GeneIDi948434.
    KEGGiecj:JW3910.
    eco: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_LN832404.1.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi4261102. 18 interactors.
    DIPiDIP-10192N.
    IntActiP00935. 1 interactor.
    STRINGi511145.b3939.

    Proteomic databases

    EPDiP00935.
    PaxDbiP00935.
    PRIDEiP00935.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76921; AAC76921; b3939.
    BAE77371; BAE77371; BAE77371.
    GeneIDi948434.
    KEGGiecj:JW3910.
    eco:b3939.
    PATRICi32123397. VBIEscCol129921_4059.

    Organism-specific databases

    EchoBASEiEB0577.
    EcoGeneiEG10582. metB.

    Phylogenomic databases

    eggNOGiENOG4105C28. Bacteria.
    COG0626. LUCA.
    HOGENOMiHOG000246415.
    InParanoidiP00935.
    KOiK01739.
    OMAiTHACIPK.
    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

    CDDicd00614. CGS_like. 1 hit.
    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...

    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: November 2, 2016
    This is version 153 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

    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 one 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.