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P00935

- METB_ECOLI

UniProt

P00935 - METB_ECOLI

Protein

Cystathionine gamma-synthase

Gene

metB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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

    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

    GO - Molecular functioni

    1. cystathionine gamma-synthase activity Source: EcoCyc
    2. pyridoxal phosphate binding Source: EcoCyc

    GO - Biological processi

    1. methionine biosynthetic process Source: EcoCyc

    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.
    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10582. metB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriP00935.

    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 – 117
    Turni12 – 154
    Turni18 – 203
    Beta strandi22 – 243
    Beta strandi31 – 333
    Turni47 – 493
    Helixi52 – 6514
    Beta strandi68 – 758
    Helixi76 – 8712
    Beta strandi93 – 975
    Helixi102 – 11211
    Turni113 – 1153
    Beta strandi118 – 1225
    Helixi127 – 1359
    Beta strandi139 – 1446
    Turni148 – 1503
    Helixi156 – 16510
    Beta strandi169 – 1735
    Turni175 – 1773
    Turni179 – 1813
    Helixi184 – 1874
    Beta strandi190 – 1956
    Turni196 – 2016
    Beta strandi209 – 2157
    Helixi216 – 22813
    Helixi235 – 24511
    Helixi248 – 26619
    Beta strandi272 – 2765
    Helixi286 – 2927
    Beta strandi298 – 3069
    Helixi308 – 3169
    Beta strandi319 – 3257
    Beta strandi329 – 3313
    Beta strandi333 – 3364
    Helixi337 – 3393
    Turni340 – 3445
    Helixi347 – 3526
    Beta strandi359 – 3635
    Helixi369 – 38315

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK01739.
    OMAiTNRYFQR.
    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

    MTRKQATIAV RSGLNDDEQY GCVVPPIHLS STYNFTGFNE PRAHDYSRRG    50
    NPTRDVVQRA LAELEGGAGA VLTNTGMSAI HLVTTVFLKP GDLLVAPHDC 100
    YGGSYRLFDS LAKRGCYRVL FVDQGDEQAL RAALAEKPKL VLVESPSNPL 150
    LRVVDIAKIC HLAREVGAVS VVDNTFLSPA LQNPLALGAD LVLHSCTKYL 200
    NGHSDVVAGV VIAKDPDVVT ELAWWANNIG VTGGAFDSYL LLRGLRTLVP 250
    RMELAQRNAQ AIVKYLQTQP LVKKLYHPSL PENQGHEIAA RQQKGFGAML 300
    SFELDGDEQT LRRFLGGLSL FTLAESLGGV ESLISHAATM THAGMAPEAR 350
    AAAGISETLL RISTGIEDGE DLIADLENGF RAANKG 386
    Length:386
    Mass (Da):41,550
    Last modified:July 21, 1986 - v1
    Checksum:i423B825219A42E9E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_491512.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76921; AAC76921; b3939.
    BAE77371; BAE77371; BAE77371.
    GeneIDi12932108.
    948434.
    KEGGiecj:Y75_p3248.
    eco:b3939.
    PATRICi32123397. VBIEscCol129921_4059.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A01158. SYECCG.
    RefSeqi NP_418374.1. NC_000913.3.
    YP_491512.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CS1 X-ray 1.50 A/B/C/D 1-386 [» ]
    ProteinModelPortali P00935.
    SMRi P00935. Positions 3-386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10192N.
    IntActi P00935. 1 interaction.
    STRINGi 511145.b3939.

    Proteomic databases

    PaxDbi P00935.
    PRIDEi P00935.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76921 ; AAC76921 ; b3939 .
    BAE77371 ; BAE77371 ; BAE77371 .
    GeneIDi 12932108.
    948434.
    KEGGi ecj:Y75_p3248.
    eco:b3939.
    PATRICi 32123397. VBIEscCol129921_4059.

    Organism-specific databases

    EchoBASEi EB0577.
    EcoGenei EG10582. metB.

    Phylogenomic databases

    eggNOGi COG0626.
    HOGENOMi HOG000246415.
    KOi K01739.
    OMAi TNRYFQR.
    OrthoDBi EOG67DPN3.
    PhylomeDBi P00935.

    Enzyme and pathway databases

    UniPathwayi UPA00051 ; UER00077 .
    BioCyci EcoCyc:O-SUCCHOMOSERLYASE-MONOMER.
    ECOL316407:JW3910-MONOMER.
    MetaCyc:O-SUCCHOMOSERLYASE-MONOMER.
    SABIO-RK P00935.

    Miscellaneous databases

    EvolutionaryTracei P00935.
    PROi P00935.

    Gene expression databases

    Genevestigatori P00935.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi 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_major_sub2.
    [Graphical view ]
    PANTHERi PTHR11808. PTHR11808. 1 hit.
    Pfami PF01053. Cys_Met_Meta_PP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001434. CGS. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR02080. O_succ_thio_ly. 1 hit.
    PROSITEi PS00868. CYS_MET_METAB_PP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 140 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