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P04968

- ILVA_ECOLI

UniProt

P04968 - ILVA_ECOLI

Protein

L-threonine dehydratase biosynthetic IlvA

Gene

ilvA

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 145 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    Functioni

    Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.1 Publication

    Catalytic activityi

    L-threonine = 2-oxobutanoate + NH3.

    Cofactori

    Pyridoxal phosphate.1 Publication

    Enzyme regulationi

    Isoleucine allosterically inhibits whereas valine allosterically activates this enzyme.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei89 – 891Pyridoxal phosphate1 Publication
    Binding sitei315 – 3151Pyridoxal phosphate1 Publication

    GO - Molecular functioni

    1. amino acid binding Source: EcoliWiki
    2. L-threonine ammonia-lyase activity Source: EcoCyc
    3. pyridoxal phosphate binding Source: EcoCyc

    GO - Biological processi

    1. branched-chain amino acid biosynthetic process Source: EcoliWiki
    2. isoleucine biosynthetic process Source: EcoCyc
    3. threonine metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Isoleucine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:THREDEHYDSYN-MONOMER.
    ECOL316407:JW3745-MONOMER.
    MetaCyc:THREDEHYDSYN-MONOMER.
    UniPathwayiUPA00047; UER00054.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-threonine dehydratase biosynthetic IlvA (EC:4.3.1.19)
    Alternative name(s):
    Threonine deaminase
    Gene namesi
    Name:ilvA
    Ordered Locus Names:b3772, JW3745
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10493. ilvA.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 514514L-threonine dehydratase biosynthetic IlvAPRO_0000185573Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei62 – 621N6-(pyridoxal phosphate)lysine

    Proteomic databases

    PaxDbiP04968.
    PRIDEiP04968.

    Expressioni

    Inductioni

    Constitutively expressed.1 Publication

    Gene expression databases

    GenevestigatoriP04968.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-10018N.
    IntActiP04968. 9 interactions.
    MINTiMINT-1305200.
    STRINGi511145.b3772.

    Structurei

    Secondary structure

    1
    514
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 2210
    Helixi25 – 273
    Beta strandi34 – 363
    Helixi38 – 436
    Beta strandi46 – 516
    Helixi53 – 553
    Beta strandi59 – 613
    Helixi63 – 719
    Turni72 – 754
    Beta strandi79 – 813
    Beta strandi83 – 864
    Beta strandi88 – 903
    Helixi91 – 10010
    Beta strandi105 – 1084
    Helixi115 – 12410
    Beta strandi127 – 1293
    Helixi135 – 14915
    Helixi160 – 17617
    Beta strandi182 – 1865
    Beta strandi188 – 1903
    Helixi191 – 20313
    Beta strandi208 – 2147
    Turni215 – 2173
    Helixi219 – 2268
    Beta strandi237 – 2404
    Helixi250 – 2556
    Beta strandi261 – 2655
    Helixi267 – 27913
    Helixi287 – 30317
    Beta strandi309 – 3135
    Helixi323 – 33513
    Beta strandi338 – 3447
    Beta strandi347 – 3504
    Helixi353 – 3575
    Beta strandi360 – 37011
    Beta strandi374 – 3763
    Beta strandi378 – 3847
    Helixi389 – 39911
    Beta strandi401 – 4033
    Beta strandi405 – 4073
    Helixi413 – 4175
    Helixi419 – 4213
    Beta strandi434 – 4396
    Helixi446 – 4549
    Beta strandi462 – 4643
    Turni468 – 4703
    Beta strandi475 – 4795
    Beta strandi498 – 5014
    Helixi506 – 5116

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TDJX-ray2.80A1-514[»]
    ProteinModelPortaliP04968.
    SMRiP04968. Positions 5-514.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04968.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini339 – 41173ACT-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini434 – 50471ACT-like 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni189 – 1924Pyridoxal phosphate binding

    Sequence similaritiesi

    Contains 2 ACT-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1171.
    HOGENOMiHOG000046975.
    KOiK01754.
    OMAiGMKKYIQ.
    OrthoDBiEOG6ZSP7D.
    PhylomeDBiP04968.

    Family and domain databases

    InterProiIPR001721. ACT-like_dom.
    IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR005787. Thr_deHydtase_biosynth.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    PF00585. Thr_dehydrat_C. 2 hits.
    [Graphical view]
    SUPFAMiSSF53686. SSF53686. 1 hit.
    TIGRFAMsiTIGR01124. ilvA_2Cterm. 1 hit.
    PROSITEiPS51672. ACT_LIKE. 2 hits.
    PS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P04968-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADSQPLSGA PEGAEYLRAV LRAPVYEAAQ VTPLQKMEKL SSRLDNVILV    50
    KREDRQPVHS FKLRGAYAMM AGLTEEQKAH GVITASAGNH AQGVAFSSAR 100
    LGVKALIVMP TATADIKVDA VRGFGGEVLL HGANFDEAKA KAIELSQQQG 150
    FTWVPPFDHP MVIAGQGTLA LELLQQDAHL DRVFVPVGGG GLAAGVAVLI 200
    KQLMPQIKVI AVEAEDSACL KAALDAGHPV DLPRVGLFAE GVAVKRIGDE 250
    TFRLCQEYLD DIITVDSDAI CAAMKDLFED VRAVAEPSGA LALAGMKKYI 300
    ALHNIRGERL AHILSGANVN FHGLRYVSER CELGEQREAL LAVTIPEEKG 350
    SFLKFCQLLG GRSVTEFNYR FADAKNACIF VGVRLSRGLE ERKEILQMLN 400
    DGGYSVVDLS DDEMAKLHVR YMVGGRPSHP LQERLYSFEF PESPGALLRF 450
    LNTLGTYWNI SLFHYRSHGT DYGRVLAAFE LGDHEPDFET RLNELGYDCH 500
    DETNNPAFRF FLAG 514
    Length:514
    Mass (Da):56,195
    Last modified:November 1, 1988 - v1
    Checksum:i9D389A0EDD8DE692
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti120 – 1201A → R in AAA24014. 1 PublicationCurated
    Sequence conflicti140 – 1401A → R in AAA24014. 1 PublicationCurated
    Sequence conflicti140 – 1401A → R in AAA67575. 1 PublicationCurated
    Sequence conflicti195 – 1951G → C in AAA24014. 1 PublicationCurated
    Sequence conflicti243 – 2431A → G in AAA24024. (PubMed:3550695)Curated
    Sequence conflicti334 – 3341G → V in AAA24014. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04890 Genomic DNA. Translation: CAA28577.1.
    K03503 Genomic DNA. Translation: AAA24014.1.
    M10313 Genomic DNA. Translation: AAB59054.1.
    M11689 Genomic DNA. Translation: AAA24027.1.
    M32253 Genomic DNA. Translation: AAA24024.1.
    M87049 Genomic DNA. Translation: AAA67575.1.
    U00096 Genomic DNA. Translation: AAC77492.1.
    AP009048 Genomic DNA. Translation: BAE77525.1.
    M25497 Genomic DNA. Translation: AAA24015.1.
    PIRiB27310. DWECTS.
    RefSeqiNP_418220.1. NC_000913.3.
    YP_491666.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77492; AAC77492; b3772.
    BAE77525; BAE77525; BAE77525.
    GeneIDi12930592.
    948287.
    KEGGiecj:Y75_p3403.
    eco:b3772.
    PATRICi32123039. VBIEscCol129921_3889.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04890 Genomic DNA. Translation: CAA28577.1 .
    K03503 Genomic DNA. Translation: AAA24014.1 .
    M10313 Genomic DNA. Translation: AAB59054.1 .
    M11689 Genomic DNA. Translation: AAA24027.1 .
    M32253 Genomic DNA. Translation: AAA24024.1 .
    M87049 Genomic DNA. Translation: AAA67575.1 .
    U00096 Genomic DNA. Translation: AAC77492.1 .
    AP009048 Genomic DNA. Translation: BAE77525.1 .
    M25497 Genomic DNA. Translation: AAA24015.1 .
    PIRi B27310. DWECTS.
    RefSeqi NP_418220.1. NC_000913.3.
    YP_491666.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TDJ X-ray 2.80 A 1-514 [» ]
    ProteinModelPortali P04968.
    SMRi P04968. Positions 5-514.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10018N.
    IntActi P04968. 9 interactions.
    MINTi MINT-1305200.
    STRINGi 511145.b3772.

    Proteomic databases

    PaxDbi P04968.
    PRIDEi P04968.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77492 ; AAC77492 ; b3772 .
    BAE77525 ; BAE77525 ; BAE77525 .
    GeneIDi 12930592.
    948287.
    KEGGi ecj:Y75_p3403.
    eco:b3772.
    PATRICi 32123039. VBIEscCol129921_3889.

    Organism-specific databases

    EchoBASEi EB0488.
    EcoGenei EG10493. ilvA.

    Phylogenomic databases

    eggNOGi COG1171.
    HOGENOMi HOG000046975.
    KOi K01754.
    OMAi GMKKYIQ.
    OrthoDBi EOG6ZSP7D.
    PhylomeDBi P04968.

    Enzyme and pathway databases

    UniPathwayi UPA00047 ; UER00054 .
    BioCyci EcoCyc:THREDEHYDSYN-MONOMER.
    ECOL316407:JW3745-MONOMER.
    MetaCyc:THREDEHYDSYN-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P04968.
    PROi P04968.

    Gene expression databases

    Genevestigatori P04968.

    Family and domain databases

    InterProi IPR001721. ACT-like_dom.
    IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR005787. Thr_deHydtase_biosynth.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view ]
    Pfami PF00291. PALP. 1 hit.
    PF00585. Thr_dehydrat_C. 2 hits.
    [Graphical view ]
    SUPFAMi SSF53686. SSF53686. 1 hit.
    TIGRFAMsi TIGR01124. ilvA_2Cterm. 1 hit.
    PROSITEi PS51672. ACT_LIKE. 2 hits.
    PS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete nucleotide sequence of the ilvGMEDA cluster of Escherichia coli K-12."
      Cox J.L., Cox B.J., Fidanza V., Calhoun D.H.
      Gene 56:185-198(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. Garrison E., Harms E., Umbarger H.E.
      Submitted (AUG-1986) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The complete nucleotide sequence of the ilvGMEDA operon of Escherichia coli K-12."
      Lawther R.P., Wek R.C., Lopes J.M., Pereira R., Taillon B.E., Hatfield G.W.
      Nucleic Acids Res. 15:2137-2155(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    4. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
      Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
      Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "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.
    7. "Nucleotide sequence and in vivo expression of the ilvY and ilvC genes in Escherichia coli K12. Transcription from divergent overlapping promoters."
      Wek R.C., Hatfield G.W.
      J. Biol. Chem. 261:2441-2450(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 439-514.
      Strain: K12.
    8. "Physical identification of an internal promoter, ilvAp, in the distal portion of the ilvGMEDA operon."
      Lopes J.M., Lawther R.P.
      Gene 76:255-269(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
      Strain: K12.
    9. "Evidence for a negative-feedback mechanism in the biosynthesis of isoleucine."
      Umbarger H.E.
      Science 123:848-848(1956) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    10. "Threonine deamination in Escherichia coli. II. Evidence for two L-threonine deaminases."
      Umbarger H.E., Brown B.
      J. Bacteriol. 73:105-112(1957) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A THREONINE DEHYDRATASE AND IN THE L-ISOLEUCINE BIOSYNTHESIS, INDUCTION.
    11. "The mechanism of action of 5'-adenylic acid-activated threonine dehydrase."
      Phillips A.T., Wood W.A.
      J. Biol. Chem. 240:4703-4709(1965) [PubMed] [Europe PMC] [Abstract]
      Cited for: REACTION MECHANISM, COFACTOR.
    12. "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.
    13. "Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase."
      Gallagher D.T., Gilliland G.L., Xiao G., Zondlo J., Fisher K.E., Chinchilla D., Eisenstein E.
      Structure 6:465-475(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, SUBUNIT.

    Entry informationi

    Entry nameiILVA_ECOLI
    AccessioniPrimary (citable) accession number: P04968
    Secondary accession number(s): Q2M881
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: November 1, 1988
    Last modified: October 1, 2014
    This is version 145 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, Allosteric enzyme, Complete proteome, 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