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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

O4-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

    • methionine biosynthetic process Source: EcoCyc

    Keywordsi

    Molecular functionTransferase
    Biological processAmino-acid biosynthesis, Methionine biosynthesis
    LigandPyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:O-SUCCHOMOSERLYASE-MONOMER.
    MetaCyc:O-SUCCHOMOSERLYASE-MONOMER.
    BRENDAi2.5.1.48. 2026.
    SABIO-RKiP00935.
    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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Chemistry databases

    DrugBankiDB04083. N'-Pyridoxyl-Lysine-5'-Monophosphate.

    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

    PaxDbiP00935.
    PRIDEiP00935.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    BioGridi4261102. 18 interactors.
    DIPiDIP-10192N.
    IntActiP00935. 1 interactor.
    STRINGi316385.ECDH10B_4128.

    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.
    PhylomeDBiP00935.

    Family and domain databases

    CDDicd00614. CGS_like. 1 hit.
    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiView protein in InterPro
    IPR000277. 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_sub2.
    PANTHERiPTHR11808. PTHR11808. 1 hit.
    PfamiView protein in Pfam
    PF01053. Cys_Met_Meta_PP. 1 hit.
    PIRSFiPIRSF001434. CGS. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR02080. O_succ_thio_ly. 1 hit.
    PROSITEiView protein in PROSITE
    PS00868. CYS_MET_METAB_PP. 1 hit.

    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.
    PATRICifig|1411691.4.peg.2766.

    Similar proteinsi

    Entry informationi

    Entry nameiMETB_ECOLI
    AccessioniPrimary (citable) accession number: P00935
    Secondary accession number(s): Q2M8N5
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: August 30, 2017
    This is version 159 of the entry and version 1 of the sequence. See 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