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Protein

Cystathionine gamma-synthase

Gene

metB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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-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

    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

    EPDiP00935
    PaxDbiP00935
    PRIDEiP00935

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    BioGridi4261102, 19 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
    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
    OMAiHPGRMTH
    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
    IPR015422 PyrdxlP-dep_Trfase_dom1
    IPR015421 PyrdxlP-dep_Trfase_major
    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: March 28, 2018
    This is version 163 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

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