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P04968

- ILVA_ECOLI

UniProt

P04968 - ILVA_ECOLI

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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

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
Complete GO annotation...

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)lysine1 Publication

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 binding1 Publication

Sequence similaritiesi

Contains 2 ACT-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1171.
HOGENOMiHOG000046975.
InParanoidiP04968.
KOiK01754.
OMAiGMKKYIQ.
OrthoDBiEOG6ZSP7D.
PhylomeDBiP04968.

Family and domain databases

InterProiIPR001721. ACT-like_dom.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR005787. Thr_deHydtase_biosynth.
IPR001926. TrpB-like_PLP-dep.
[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

        10         20         30         40         50
MADSQPLSGA PEGAEYLRAV LRAPVYEAAQ VTPLQKMEKL SSRLDNVILV
60 70 80 90 100
KREDRQPVHS FKLRGAYAMM AGLTEEQKAH GVITASAGNH AQGVAFSSAR
110 120 130 140 150
LGVKALIVMP TATADIKVDA VRGFGGEVLL HGANFDEAKA KAIELSQQQG
160 170 180 190 200
FTWVPPFDHP MVIAGQGTLA LELLQQDAHL DRVFVPVGGG GLAAGVAVLI
210 220 230 240 250
KQLMPQIKVI AVEAEDSACL KAALDAGHPV DLPRVGLFAE GVAVKRIGDE
260 270 280 290 300
TFRLCQEYLD DIITVDSDAI CAAMKDLFED VRAVAEPSGA LALAGMKKYI
310 320 330 340 350
ALHNIRGERL AHILSGANVN FHGLRYVSER CELGEQREAL LAVTIPEEKG
360 370 380 390 400
SFLKFCQLLG GRSVTEFNYR FADAKNACIF VGVRLSRGLE ERKEILQMLN
410 420 430 440 450
DGGYSVVDLS DDEMAKLHVR YMVGGRPSHP LQERLYSFEF PESPGALLRF
460 470 480 490 500
LNTLGTYWNI SLFHYRSHGT DYGRVLAAFE LGDHEPDFET RLNELGYDCH
510
DETNNPAFRF FLAG
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.
InParanoidi P04968.
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. TrpB-like_PLP-dep.
[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

« Hide 'large scale' publications
  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 29, 2014
This is version 146 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