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Protein

L-threonine dehydratase biosynthetic IlvA

Gene

ilvA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

Activity 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

GO - Biological processi

  • branched-chain amino acid biosynthetic process Source: EcoliWiki
  • isoleucine biosynthetic process Source: EcoCyc
  • threonine metabolic process Source: UniProtKB

Keywordsi

Molecular functionAllosteric enzyme, Lyase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis, Isoleucine biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:THREDEHYDSYN-MONOMER
MetaCyc:THREDEHYDSYN-MONOMER
UniPathwayi
UPA00047;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

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, 10 interactors
STRINGi316385.ECDH10B_3961

Structurei

Secondary structure

1514
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
Regioni188 – 192Pyridoxal phosphate binding1 Publication5

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105C7B Bacteria
COG1171 LUCA
HOGENOMiHOG000046975
InParanoidiP04968
KOiK01754
OMAiRNHGAAY
PhylomeDBiP04968

Family and domain databases

Gene3Di3.40.1020.10, 1 hit
InterProiView protein in InterPro
IPR001926 PLP-dep
IPR000634 Ser/Thr_deHydtase_PyrdxlP-BS
IPR001721 TD_ACT-like
IPR038110 TD_ACT-like_sf
IPR005787 Thr_deHydtase_biosynth
IPR036052 Trypto_synt_PLP_dependent
PfamiView protein in Pfam
PF00291 PALP, 1 hit
PF00585 Thr_dehydrat_C, 2 hits
SUPFAMiSSF53686 SSF53686, 1 hit
TIGRFAMsiTIGR01124 ilvA_2Cterm, 1 hit
PROSITEiView protein in PROSITE
PS51672 ACT_LIKE, 2 hits
PS00165 DEHYDRATASE_SER_THR, 1 hit

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
PATRICifig|1411691.4.peg.2934

Similar proteinsi

Entry informationi

Entry nameiILVA_ECOLI
AccessioniPrimary (citable) accession number: P04968
Secondary accession number(s): Q2M881
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1988
Last modified: September 12, 2018
This is version 171 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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