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Protein

L-threonine dehydratase

Gene

ilvA

Organism
Acinetobacter oleivorans (strain JCM 16667 / KCTC 23045 / DR1)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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.UniRule annotation

Catalytic activityi

L-threonine = 2-oxobutanoate + NH3.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi

GO - Molecular functioni

  1. L-threonine ammonia-lyase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. isoleucine biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationImported

Keywords - Biological processi

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

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

BioCyciAOLE436717:GHCD-1684-MONOMER.
UniPathwayiUPA00047; UER00054.

Names & Taxonomyi

Protein namesi
Recommended name:
L-threonine dehydrataseUniRule annotation (EC:4.3.1.19UniRule annotation)
Alternative name(s):
Threonine deaminaseUniRule annotation
Gene namesi
Name:ilvAUniRule annotation
Ordered Locus Names:AOLE_08245Imported
OrganismiAcinetobacter oleivorans (strain JCM 16667 / KCTC 23045 / DR1)Imported
Taxonomic identifieri436717 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter
ProteomesiUP000000392 Componenti: Chromosome

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Family & Domainsi

Sequence similaritiesi

Belongs to the serine/threonine dehydratase family.UniRule annotation
Contains 2 ACT-like domains.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000046975.
KOiK01754.

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.

D8JIS5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRVVRQIL QATVYDVAIE TPLEAAPRIS QKLNNTIRFK REDLQPVFSF
60 70 80 90 100
KLRGAYNRIS QLPKEQLERG VICASAGNHA QGVALSGQRL GIPAIIVMPS
110 120 130 140 150
TTPDIKVQAV KRLGGQVVLH GDSFDVANKY AQQRAEVEGL VFIPPYDDEL
160 170 180 190 200
VIAGQGTIAN EILRQWRDVE YVFVAVGGGG LISGVAAYLG EVAPHVKIIG
210 220 230 240 250
VEYEESACLK AALEANERVI LPHVGLFADG TAVAQIGALP FDIIRLRKSD
260 270 280 290 300
NSGPIVDPDI VTVNTDEICA AIKDTFDENR SIVEPSGAMA LAGIKKYITE
310 320 330 340 350
HKISNKNMVS IVCGANMNFD RLRYIAERTE LGEQREAIYA VTLSEEKGAF
360 370 380 390 400
LGFCRALQGR NITEFNYRAN NTDEAQVFVG ISLKGGDAER HEILEQLKQQ
410 420 430 440 450
NYVVDDLSDD EVAKLHIRYL IGGHANIDDE RLFRVEFPER PGALLTFLTR
460 470 480 490 500
LGPTHNITLF HYRNHGAAEG RVLVGLQATD AKQNPDGLIE TLEQISYPYA
510
EITNNVGYKR FLK
Length:513
Mass (Da):56,578
Last modified:October 5, 2010 - v1
Checksum:i5B92C2F81F0F74DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002080 Genomic DNA. Translation: ADI90538.1.
RefSeqiYP_003731911.1. NC_014259.1.

Genome annotation databases

EnsemblBacteriaiADI90538; ADI90538; AOLE_08245.
KEGGiacd:AOLE_08245.
PATRICi42142335. VBIAciSp20010_1639.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002080 Genomic DNA. Translation: ADI90538.1.
RefSeqiYP_003731911.1. NC_014259.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADI90538; ADI90538; AOLE_08245.
KEGGiacd:AOLE_08245.
PATRICi42142335. VBIAciSp20010_1639.

Phylogenomic databases

HOGENOMiHOG000046975.
KOiK01754.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00054.
BioCyciAOLE436717:GHCD-1684-MONOMER.

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...

Publicationsi

  1. "Complete genome sequence of the diesel-degrading Acinetobacter sp. strain DR1."
    Jung J., Baek J.H., Park W.
    J. Bacteriol. 192:4794-4795(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCM 1667 / KCTC 23045 / DR1Imported.

Entry informationi

Entry nameiD8JIS5_ACISD
AccessioniPrimary (citable) accession number: D8JIS5
Entry historyi
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: April 1, 2015
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

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 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.