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P06721

- METC_ECOLI

UniProt

P06721 - METC_ECOLI

Protein

Cystathionine beta-lyase MetC

Gene

metC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate.

    Cofactori

    Pyridoxal phosphate.

    Pathwayi

    GO - Molecular functioni

    1. cystathionine beta-lyase activity Source: EcoCyc
    2. L-cysteine desulfhydrase activity Source: EcoCyc
    3. pyridoxal phosphate binding Source: EcoCyc

    GO - Biological processi

    1. methionine biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Methionine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:CYSTATHIONINE-BETA-LYASE-MONOMER.
    ECOL316407:JW2975-MONOMER.
    MetaCyc:CYSTATHIONINE-BETA-LYASE-MONOMER.
    UniPathwayiUPA00051; UER00078.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cystathionine beta-lyase MetC (EC:4.4.1.8)
    Short name:
    CBL
    Alternative name(s):
    Beta-cystathionase
    Cysteine lyase
    Gene namesi
    Name:metC
    Ordered Locus Names:b3008, JW2975
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10583. metC.

    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 – 395395Cystathionine beta-lyase MetCPRO_0000114768Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei210 – 2101N6-(pyridoxal phosphate)lysine

    Proteomic databases

    PaxDbiP06721.
    PRIDEiP06721.

    Expressioni

    Gene expression databases

    GenevestigatoriP06721.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-10193N.
    IntActiP06721. 6 interactions.
    STRINGi511145.b3008.

    Structurei

    Secondary structure

    1
    395
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 127
    Helixi17 – 204
    Beta strandi23 – 253
    Helixi39 – 479
    Turni48 – 525
    Turni57 – 593
    Helixi62 – 7514
    Beta strandi78 – 858
    Helixi86 – 9510
    Beta strandi103 – 1075
    Helixi112 – 1209
    Helixi122 – 1254
    Beta strandi128 – 1325
    Helixi137 – 1437
    Beta strandi148 – 1569
    Turni158 – 1603
    Helixi166 – 17611
    Beta strandi181 – 1855
    Turni187 – 1926
    Helixi196 – 1994
    Beta strandi202 – 2076
    Turni208 – 2136
    Beta strandi215 – 2173
    Beta strandi221 – 2255
    Turni227 – 2293
    Helixi230 – 23910
    Helixi246 – 27833
    Beta strandi283 – 2875
    Helixi297 – 3037
    Beta strandi309 – 3179
    Helixi321 – 3288
    Beta strandi342 – 3443
    Beta strandi346 – 3505
    Helixi352 – 3565
    Beta strandi370 – 3745
    Helixi380 – 39213

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CL1X-ray1.83A/B1-395[»]
    1CL2X-ray2.20A/B1-395[»]
    2FQ6X-ray1.78A/B1-395[»]
    2GQNX-ray1.80A/B1-395[»]
    ProteinModelPortaliP06721.
    SMRiP06721. Positions 4-395.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06721.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the trans-sulfuration enzymes family.Curated

    Phylogenomic databases

    eggNOGiCOG0626.
    HOGENOMiHOG000246416.
    KOiK01760.
    OMAiEQSYLMG.
    OrthoDBiEOG67DPN3.
    PhylomeDBiP06721.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
    IPR006233. Cys_b_lyase_bac.
    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.
    TIGRFAMsiTIGR01324. cysta_beta_ly_B. 1 hit.
    PROSITEiPS00868. CYS_MET_METAB_PP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06721-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADKKLDTQL VNAGRSKKYT LGAVNSVIQR ASSLVFDSVE AKKHATRNRA    50
    NGELFYGRRG TLTHFSLQQA MCELEGGAGC VLFPCGAAAV ANSILAFIEQ 100
    GDHVLMTNTA YEPSQDFCSK ILSKLGVTTS WFDPLIGADI VKHLQPNTKI 150
    VFLESPGSIT MEVHDVPAIV AAVRSVVPDA IIMIDNTWAA GVLFKALDFG 200
    IDVSIQAATK YLVGHSDAMI GTAVCNARCW EQLRENAYLM GQMVDADTAY 250
    ITSRGLRTLG VRLRQHHESS LKVAEWLAEH PQVARVNHPA LPGSKGHEFW 300
    KRDFTGSSGL FSFVLKKKLN NEELANYLDN FSLFSMAYSW GGYESLILAN 350
    QPEHIAAIRP QGEIDFSGTL IRLHIGLEDV DDLIADLDAG FARIV 395
    Length:395
    Mass (Da):43,212
    Last modified:January 1, 1988 - v1
    Checksum:iFD3308423D6427C6
    GO

    Sequence cautioni

    The sequence AAA69175.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12858 Genomic DNA. Translation: AAA24158.1.
    U28377 Genomic DNA. Translation: AAA69175.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76044.1.
    AP009048 Genomic DNA. Translation: BAE77065.1.
    PIRiA25153. WZECCB.
    RefSeqiNP_417481.1. NC_000913.3.
    YP_491201.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76044; AAC76044; b3008.
    BAE77065; BAE77065; BAE77065.
    GeneIDi12932425.
    946240.
    KEGGiecj:Y75_p2935.
    eco:b3008.
    PATRICi32121430. VBIEscCol129921_3102.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12858 Genomic DNA. Translation: AAA24158.1 .
    U28377 Genomic DNA. Translation: AAA69175.1 . Different initiation.
    U00096 Genomic DNA. Translation: AAC76044.1 .
    AP009048 Genomic DNA. Translation: BAE77065.1 .
    PIRi A25153. WZECCB.
    RefSeqi NP_417481.1. NC_000913.3.
    YP_491201.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CL1 X-ray 1.83 A/B 1-395 [» ]
    1CL2 X-ray 2.20 A/B 1-395 [» ]
    2FQ6 X-ray 1.78 A/B 1-395 [» ]
    2GQN X-ray 1.80 A/B 1-395 [» ]
    ProteinModelPortali P06721.
    SMRi P06721. Positions 4-395.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10193N.
    IntActi P06721. 6 interactions.
    STRINGi 511145.b3008.

    Chemistry

    ChEMBLi CHEMBL1075079.

    Proteomic databases

    PaxDbi P06721.
    PRIDEi P06721.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76044 ; AAC76044 ; b3008 .
    BAE77065 ; BAE77065 ; BAE77065 .
    GeneIDi 12932425.
    946240.
    KEGGi ecj:Y75_p2935.
    eco:b3008.
    PATRICi 32121430. VBIEscCol129921_3102.

    Organism-specific databases

    EchoBASEi EB0578.
    EcoGenei EG10583. metC.

    Phylogenomic databases

    eggNOGi COG0626.
    HOGENOMi HOG000246416.
    KOi K01760.
    OMAi EQSYLMG.
    OrthoDBi EOG67DPN3.
    PhylomeDBi P06721.

    Enzyme and pathway databases

    UniPathwayi UPA00051 ; UER00078 .
    BioCyci EcoCyc:CYSTATHIONINE-BETA-LYASE-MONOMER.
    ECOL316407:JW2975-MONOMER.
    MetaCyc:CYSTATHIONINE-BETA-LYASE-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P06721.
    PROi P06721.

    Gene expression databases

    Genevestigatori P06721.

    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.
    IPR006233. Cys_b_lyase_bac.
    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 TIGR01324. cysta_beta_ly_B. 1 hit.
    PROSITEi PS00868. CYS_MET_METAB_PP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region."
      Belfaiza J., Parsot C., Martel A., de la Tour C.B., Margarita D., Cohen G.N., Saint-Girons I.
      Proc. Natl. Acad. Sci. U.S.A. 83:867-871(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "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 194-221.
    5. "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.
    6. "Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A."
      Clausen T., Huber R., Laber B., Pohlenz H.-D., Messerschmidt A.
      J. Mol. Biol. 262:202-224(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS), SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-210.

    Entry informationi

    Entry nameiMETC_ECOLI
    AccessioniPrimary (citable) accession number: P06721
    Secondary accession number(s): Q2M9J1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 134 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