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Protein

L-threonine dehydratase biosynthetic IlvA

Gene

ilvA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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 5'-phosphate1 Publication

Enzyme regulationi

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

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 2-oxobutanoate from L-threonine.
Proteins known to be involved in this subpathway in this organism are:
  1. L-threonine dehydratase biosynthetic IlvA (ilvA)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-oxobutanoate from L-threonine, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei89Pyridoxal phosphate1 Publication1
Binding sitei315Pyridoxal phosphate1 Publication1

GO - Molecular functioni

  • amino acid binding Source: EcoliWiki
  • L-threonine ammonia-lyase activity Source: EcoliWiki
  • pyridoxal phosphate binding Source: EcoCyc

GO - Biological processi

  • branched-chain amino acid biosynthetic process Source: EcoliWiki
  • cellular amino acid biosynthetic process Source: UniProtKB-KW
  • isoleucine biosynthetic process Source: EcoCyc
  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10493. ilvA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001855731 – 514L-threonine dehydratase biosynthetic IlvAAdd BLAST514

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei62N6-(pyridoxal phosphate)lysine1 Publication1

Proteomic databases

EPDiP04968.
PaxDbiP04968.
PRIDEiP04968.

Expressioni

Inductioni

Constitutively expressed.1 Publication

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi4259586. 18 interactors.
DIPiDIP-10018N.
IntActiP04968. 9 interactors.
MINTiMINT-1305200.
STRINGi511145.b3772.

Structurei

Secondary structure

1514
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 22Combined sources10
Helixi25 – 27Combined sources3
Beta strandi34 – 36Combined sources3
Helixi38 – 43Combined sources6
Beta strandi46 – 51Combined sources6
Helixi53 – 55Combined sources3
Beta strandi59 – 61Combined sources3
Helixi63 – 71Combined sources9
Turni72 – 75Combined sources4
Beta strandi79 – 81Combined sources3
Beta strandi83 – 86Combined sources4
Beta strandi88 – 90Combined sources3
Helixi91 – 100Combined sources10
Beta strandi105 – 108Combined sources4
Helixi115 – 124Combined sources10
Beta strandi127 – 129Combined sources3
Helixi135 – 149Combined sources15
Helixi160 – 176Combined sources17
Beta strandi182 – 186Combined sources5
Beta strandi188 – 190Combined sources3
Helixi191 – 203Combined sources13
Beta strandi208 – 214Combined sources7
Turni215 – 217Combined sources3
Helixi219 – 226Combined sources8
Beta strandi237 – 240Combined sources4
Helixi250 – 255Combined sources6
Beta strandi261 – 265Combined sources5
Helixi267 – 279Combined sources13
Helixi287 – 303Combined sources17
Beta strandi309 – 313Combined sources5
Helixi323 – 335Combined sources13
Beta strandi338 – 344Combined sources7
Beta strandi347 – 350Combined sources4
Helixi353 – 357Combined sources5
Beta strandi360 – 370Combined sources11
Beta strandi374 – 376Combined sources3
Beta strandi378 – 384Combined sources7
Helixi389 – 399Combined sources11
Beta strandi401 – 403Combined sources3
Beta strandi405 – 407Combined sources3
Helixi413 – 417Combined sources5
Helixi419 – 421Combined sources3
Beta strandi434 – 439Combined sources6
Helixi446 – 454Combined sources9
Beta strandi462 – 464Combined sources3
Turni468 – 470Combined sources3
Beta strandi475 – 479Combined sources5
Beta strandi498 – 501Combined sources4
Helixi506 – 511Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TDJX-ray2.80A1-514[»]
ProteinModelPortaliP04968.
SMRiP04968.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04968.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini339 – 411ACT-like 1PROSITE-ProRule annotationAdd BLAST73
Domaini434 – 504ACT-like 2PROSITE-ProRule annotationAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni189 – 192Pyridoxal phosphate binding1 Publication4

Sequence similaritiesi

Contains 2 ACT-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105C7B. Bacteria.
COG1171. LUCA.
HOGENOMiHOG000046975.
InParanoidiP04968.
KOiK01754.
OMAiKENARVF.
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)DescriptionActionsGraphical viewLength
Sequence conflicti120A → R in AAA24014 (Ref. 2) Curated1
Sequence conflicti140A → R in AAA24014 (Ref. 2) Curated1
Sequence conflicti140A → R in AAA67575 (Ref. 2) Curated1
Sequence conflicti195G → C in AAA24014 (Ref. 2) Curated1
Sequence conflicti243A → G in AAA24024 (PubMed:3550695).Curated1
Sequence conflicti334G → V in AAA24014 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000785596.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77492; AAC77492; b3772.
BAE77525; BAE77525; BAE77525.
GeneIDi948287.
KEGGiecj:JW3745.
eco:b3772.
PATRICi32123039. VBIEscCol129921_3889.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000785596.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TDJX-ray2.80A1-514[»]
ProteinModelPortaliP04968.
SMRiP04968.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259586. 18 interactors.
DIPiDIP-10018N.
IntActiP04968. 9 interactors.
MINTiMINT-1305200.
STRINGi511145.b3772.

Proteomic databases

EPDiP04968.
PaxDbiP04968.
PRIDEiP04968.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77492; AAC77492; b3772.
BAE77525; BAE77525; BAE77525.
GeneIDi948287.
KEGGiecj:JW3745.
eco:b3772.
PATRICi32123039. VBIEscCol129921_3889.

Organism-specific databases

EchoBASEiEB0488.
EcoGeneiEG10493. ilvA.

Phylogenomic databases

eggNOGiENOG4105C7B. Bacteria.
COG1171. LUCA.
HOGENOMiHOG000046975.
InParanoidiP04968.
KOiK01754.
OMAiKENARVF.
PhylomeDBiP04968.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP04968.
PROiP04968.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 160 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.