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P30140

- THIH_ECOLI

UniProt

P30140 - THIH_ECOLI

Protein

2-iminoacetate synthase

Gene

thiH

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 114 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the radical-mediated cleavage of tyrosine to 2-iminoacetate and 4-cresol.2 Publications

    Catalytic activityi

    L-tyrosine + S-adenosyl-L-methionine + reduced acceptor = 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + acceptor + 2 H+.2 Publications

    Cofactori

    Binds 1 4Fe-4S cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi85 – 851Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
    Metal bindingi89 – 891Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
    Metal bindingi92 – 921Iron-sulfur (4Fe-4S-S-AdoMet)By similarity

    GO - Molecular functioni

    1. 2-iminoacetate synthase activity Source: UniProtKB-EC
    2. 4 iron, 4 sulfur cluster binding Source: EcoCyc
    3. iron ion binding Source: InterPro
    4. iron-sulfur cluster binding Source: EcoCyc
    5. lyase activity Source: EcoCyc
    6. protein binding Source: IntAct

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: EcoliWiki
    2. thiamine biosynthetic process Source: EcoCyc
    3. thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Thiamine biosynthesis

    Keywords - Ligandi

    4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciEcoCyc:THIH-MONOMER.
    ECOL316407:JW3953-MONOMER.
    MetaCyc:THIH-MONOMER.
    UniPathwayiUPA00060.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-iminoacetate synthase (EC:4.1.99.19)
    Alternative name(s):
    Dehydroglycine synthase
    Tyrosine lyase
    Gene namesi
    Name:thiH
    Ordered Locus Names:b3990, JW3953
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11590. thiH.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3773772-iminoacetate synthasePRO_0000072514Add
    BLAST

    Proteomic databases

    PaxDbiP30140.
    PRIDEiP30140.

    Expressioni

    Gene expression databases

    GenevestigatoriP30140.

    Interactioni

    Subunit structurei

    Forms a heterodimer with ThiG.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    thiGP301392EBI-1125553,EBI-547059

    Protein-protein interaction databases

    DIPiDIP-6869N.
    IntActiP30140. 4 interactions.
    STRINGi511145.b3990.

    Structurei

    3D structure databases

    ProteinModelPortaliP30140.
    SMRiP30140. Positions 24-228.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the radical SAM superfamily. ThiH family.Curated

    Phylogenomic databases

    eggNOGiCOG1060.
    HOGENOMiHOG000270732.
    KOiK03150.
    OMAiWQSRYSI.
    OrthoDBiEOG6RNQB0.
    PhylomeDBiP30140.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR010722. BATS_dom.
    IPR007197. rSAM.
    IPR012726. ThiH.
    [Graphical view]
    PfamiPF06968. BATS. 1 hit.
    PF04055. Radical_SAM. 1 hit.
    [Graphical view]
    SMARTiSM00876. BATS. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02351. thiH. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P30140-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTFSDRWRQ LDWDDIRLRI NGKTAADVER ALNASQLTRD DMMALLSPAA    50
    SGYLEQLAQR AQRLTRQRFG NTVSFYVPLY LSNLCANDCT YCGFSMSNRI 100
    KRKTLDEADI ARESAAIREM GFEHLLLVTG EHQAKVGMDY FRRHLPALRE 150
    QFSSLQMEVQ PLAETEYAEL KQLGLDGVMV YQETYHEATY ARHHLKGKKQ 200
    DFFWRLETPD RLGRAGIDKI GLGALIGLSD NWRVDSYMVA EHLLWLQQHY 250
    WQSRYSVSFP RLRPCTGGIE PASIMDERQL VQTICAFRLL APEIELSLST 300
    RESPWFRDRV IPLAINNVSA FSKTQPGGYA DNHPELEQFS PHDDRRPEAV 350
    AAALTAQGLQ PVWKDWDSYL GRASQRL 377
    Length:377
    Mass (Da):43,320
    Last modified:January 23, 2007 - v3
    Checksum:iF45A0859372F5ED6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88701 Genomic DNA. Translation: AAB95619.1.
    U00006 Genomic DNA. Translation: AAC43088.1.
    U00096 Genomic DNA. Translation: AAC76964.1.
    AP009048 Genomic DNA. Translation: BAE77330.1.
    PIRiS35121.
    RefSeqiNP_418417.1. NC_000913.3.
    YP_491471.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76964; AAC76964; b3990.
    BAE77330; BAE77330; BAE77330.
    GeneIDi12933915.
    948494.
    KEGGiecj:Y75_p3207.
    eco:b3990.
    PATRICi32123501. VBIEscCol129921_4103.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88701 Genomic DNA. Translation: AAB95619.1 .
    U00006 Genomic DNA. Translation: AAC43088.1 .
    U00096 Genomic DNA. Translation: AAC76964.1 .
    AP009048 Genomic DNA. Translation: BAE77330.1 .
    PIRi S35121.
    RefSeqi NP_418417.1. NC_000913.3.
    YP_491471.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P30140.
    SMRi P30140. Positions 24-228.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6869N.
    IntActi P30140. 4 interactions.
    STRINGi 511145.b3990.

    Proteomic databases

    PaxDbi P30140.
    PRIDEi P30140.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76964 ; AAC76964 ; b3990 .
    BAE77330 ; BAE77330 ; BAE77330 .
    GeneIDi 12933915.
    948494.
    KEGGi ecj:Y75_p3207.
    eco:b3990.
    PATRICi 32123501. VBIEscCol129921_4103.

    Organism-specific databases

    EchoBASEi EB1548.
    EcoGenei EG11590. thiH.

    Phylogenomic databases

    eggNOGi COG1060.
    HOGENOMi HOG000270732.
    KOi K03150.
    OMAi WQSRYSI.
    OrthoDBi EOG6RNQB0.
    PhylomeDBi P30140.

    Enzyme and pathway databases

    UniPathwayi UPA00060 .
    BioCyci EcoCyc:THIH-MONOMER.
    ECOL316407:JW3953-MONOMER.
    MetaCyc:THIH-MONOMER.

    Miscellaneous databases

    PROi P30140.

    Gene expression databases

    Genevestigatori P30140.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR010722. BATS_dom.
    IPR007197. rSAM.
    IPR012726. ThiH.
    [Graphical view ]
    Pfami PF06968. BATS. 1 hit.
    PF04055. Radical_SAM. 1 hit.
    [Graphical view ]
    SMARTi SM00876. BATS. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02351. thiH. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in Escherichia coli K-12."
      Vander Horn P.B., Backstrom A.D., Stewart V., Begley T.P.
      J. Bacteriol. 175:982-992(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(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. "Efficient sequence analysis of the six gene products (7-74 kDa) from the Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass spectrometry."
      Kelleher N.L., Taylor S.V., Grannis D., Kinsland C., Chiu H.-J., Begley T.P., McLafferty F.W.
      Protein Sci. 7:1796-1801(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 41-47, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "Thiamine biosynthesis in Escherichia coli: isolation and initial characterisation of the ThiGH complex."
      Leonardi R., Fairhurst S.A., Kriek M., Lowe D.J., Roach P.L.
      FEBS Lett. 539:95-99(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THIG, SUBUNIT, EPR SPECTROSCOPY, COFACTOR.
    7. "Thiamine biosynthesis in Escherichia coli: identification of the intermediate and by-product derived from tyrosine."
      Kriek M., Martins F., Challand M.R., Croft A., Roach P.L.
      Angew. Chem. Int. Ed. 46:9223-9226(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION PRODUCTS, REACTION MECHANISM.
    8. "Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro."
      Kriek M., Martins F., Leonardi R., Fairhurst S.A., Lowe D.J., Roach P.L.
      J. Biol. Chem. 282:17413-17423(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, EPR SPECTROSCOPY, COFACTOR, CATALYTIC ACTIVITY, REACTION MECHANISM.

    Entry informationi

    Entry nameiTHIH_ECOLI
    AccessioniPrimary (citable) accession number: P30140
    Secondary accession number(s): Q2M8S6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 114 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The product 2-iminoacetate hydrates in vitro to yield glyoxylate and ammonium.

    Keywords - Technical termi

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3