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P04968 (ILVA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-threonine dehydratase biosynthetic IlvA

EC=4.3.1.19
Alternative name(s):
Threonine deaminase
Gene names
Name:ilvA
Ordered Locus Names:b3772, JW3745
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10

Catalytic activity

L-threonine = 2-oxobutanoate + NH3.

Cofactor

Pyridoxal phosphate. Ref.11

Enzyme regulation

Isoleucine allosterically inhibits whereas valine allosterically activates this enzyme. Ref.9

Pathway

Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.

Subunit structure

Homotetramer. Ref.13

Induction

Constitutively expressed. Ref.9 Ref.10

Sequence similarities

Belongs to the serine/threonine dehydratase family.

Contains 2 ACT-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 514514L-threonine dehydratase biosynthetic IlvA
PRO_0000185573

Regions

Domain339 – 41173ACT-like 1
Domain434 – 50471ACT-like 2
Region189 – 1924Pyridoxal phosphate binding

Sites

Binding site891Pyridoxal phosphate
Binding site3151Pyridoxal phosphate

Amino acid modifications

Modified residue621N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict1201A → R in AAA24014. Ref.2
Sequence conflict1401A → R in AAA24014. Ref.2
Sequence conflict1401A → R in AAA67575. Ref.2
Sequence conflict1951G → C in AAA24014. Ref.2
Sequence conflict2431A → G in AAA24024. Ref.3
Sequence conflict3341G → V in AAA24014. Ref.2

Secondary structure

............................................................................................... 514
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04968 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 9D389A0EDD8DE692

FASTA51456,195
        10         20         30         40         50         60 
MADSQPLSGA PEGAEYLRAV LRAPVYEAAQ VTPLQKMEKL SSRLDNVILV KREDRQPVHS 

        70         80         90        100        110        120 
FKLRGAYAMM AGLTEEQKAH GVITASAGNH AQGVAFSSAR LGVKALIVMP TATADIKVDA 

       130        140        150        160        170        180 
VRGFGGEVLL HGANFDEAKA KAIELSQQQG FTWVPPFDHP MVIAGQGTLA LELLQQDAHL 

       190        200        210        220        230        240 
DRVFVPVGGG GLAAGVAVLI KQLMPQIKVI AVEAEDSACL KAALDAGHPV DLPRVGLFAE 

       250        260        270        280        290        300 
GVAVKRIGDE TFRLCQEYLD DIITVDSDAI CAAMKDLFED VRAVAEPSGA LALAGMKKYI 

       310        320        330        340        350        360 
ALHNIRGERL AHILSGANVN FHGLRYVSER CELGEQREAL LAVTIPEEKG SFLKFCQLLG 

       370        380        390        400        410        420 
GRSVTEFNYR FADAKNACIF VGVRLSRGLE ERKEILQMLN DGGYSVVDLS DDEMAKLHVR 

       430        440        450        460        470        480 
YMVGGRPSHP LQERLYSFEF PESPGALLRF LNTLGTYWNI SLFHYRSHGT DYGRVLAAFE 

       490        500        510 
LGDHEPDFET RLNELGYDCH DETNNPAFRF FLAG 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRDWECTS. B27310.
RefSeqNP_418220.1. NC_000913.3.
YP_491666.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TDJX-ray2.80A1-514[»]
ProteinModelPortalP04968.
SMRP04968. Positions 5-514.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10018N.
IntActP04968. 9 interactions.
MINTMINT-1305200.
STRING511145.b3772.

Proteomic databases

PaxDbP04968.
PRIDEP04968.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77492; AAC77492; b3772.
BAE77525; BAE77525; BAE77525.
GeneID12930592.
948287.
KEGGecj:Y75_p3403.
eco:b3772.
PATRIC32123039. VBIEscCol129921_3889.

Organism-specific databases

EchoBASEEB0488.
EcoGeneEG10493. ilvA.

Phylogenomic databases

eggNOGCOG1171.
HOGENOMHOG000046975.
KOK01754.
OMASDNEMAK.
OrthoDBEOG6ZSP7D.
PhylomeDBP04968.
ProtClustDBPRK09224.

Enzyme and pathway databases

BioCycEcoCyc:THREDEHYDSYN-MONOMER.
ECOL316407:JW3745-MONOMER.
MetaCyc:THREDEHYDSYN-MONOMER.
UniPathwayUPA00047; UER00054.

Gene expression databases

GenevestigatorP04968.

Family and domain databases

InterProIPR001721. ACT-like_dom.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR005787. Thr_deHydtase_biosynth.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
PF00585. Thr_dehydrat_C. 2 hits.
[Graphical view]
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR01124. ilvA_2Cterm. 1 hit.
PROSITEPS51672. ACT_LIKE. 2 hits.
PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04968.
PROP04968.

Entry information

Entry nameILVA_ECOLI
AccessionPrimary (citable) accession number: P04968
Secondary accession number(s): Q2M881
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1988
Last modified: April 16, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene