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Protein

L-threonine dehydratase biosynthetic IlvA

Gene

ilvA

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

Catalytic activityi

L-threonine = 2-oxobutanoate + NH3.

Cofactori

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei90 – 901Pyridoxal phosphateBy similarity
Binding sitei319 – 3191Pyridoxal phosphateBy similarity

GO - Molecular functioni

GO - Biological processi

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

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:ML1209
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML1209.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427L-threonine dehydratase biosynthetic IlvAPRO_0000185576Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631N6-(pyridoxal phosphate)lysineBy similarity

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi272631.ML1209.

Structurei

3D structure databases

ProteinModelPortaliQ9X7F1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini343 – 41775ACT-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni194 – 1974Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Contains 1 ACT-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105C7B. Bacteria.
COG1171. LUCA.
HOGENOMiHOG000046973.
KOiK01754.
OMAiILMAHNC.
OrthoDBiPOG091H03MP.

Family and domain databases

InterProiIPR001721. ACT-like_dom.
IPR011820. IlvA.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
PF00585. Thr_dehydrat_C. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR02079. THD1. 1 hit.
PROSITEiPS51672. ACT_LIKE. 1 hit.
PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9X7F1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAEPSRNPR TPPVSAVDID GAAKRIAPVV TPTPLQLSDR LSAITGAAVY
60 70 80 90 100
LKREDLQTVR SYKLRGAYNL LVQLTDEEIA AGVVCSSAGN HAQGVAYACR
110 120 130 140 150
SLGVHGRVYV PAKTPKQKWD RIRYHGGAFI ELIVGRSTYD LAAAAAVDDI
160 170 180 190 200
ERTGATLVPP YDDVRVIAGQ GTIAVELLEQ LNTEPDLVVV PVGGGGCIAG
210 220 230 240 250
MTTYLAERTA NTAVLGVEPA GAAAMMAALA AGEPVTLDYV DQFVDGAAVN
260 270 280 290 300
RVGTLPYAAL TAAGDMVSIT TVDEGAVCTA MLDLYQNEGI IAEPAGALSV
310 320 330 340 350
AGLLETDIEP GSTVVCLISG GNNDVLRYGE VLERSLIHLG LKHYFLVDFP
360 370 380 390 400
QKPGALRRFL DEVLGPNDDI TLFEYVKRNN RETGEALVGI QLGSAVDLDV
410 420
LLARMQGTEM HVETLQPGSP AYRYLLL
Length:427
Mass (Da):45,172
Last modified:November 1, 1999 - v1
Checksum:i86FB44221369682E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL049478 Genomic DNA. Translation: CAB39589.1.
AL583921 Genomic DNA. Translation: CAC31590.1.
PIRiC87060.
RefSeqiNP_301876.1. NC_002677.1.
WP_010908197.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC31590; CAC31590; CAC31590.
GeneIDi910312.
KEGGimle:ML1209.
PATRICi18054558. VBIMycLep78757_2219.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL049478 Genomic DNA. Translation: CAB39589.1.
AL583921 Genomic DNA. Translation: CAC31590.1.
PIRiC87060.
RefSeqiNP_301876.1. NC_002677.1.
WP_010908197.1. NC_002677.1.

3D structure databases

ProteinModelPortaliQ9X7F1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML1209.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC31590; CAC31590; CAC31590.
GeneIDi910312.
KEGGimle:ML1209.
PATRICi18054558. VBIMycLep78757_2219.

Organism-specific databases

LepromaiML1209.

Phylogenomic databases

eggNOGiENOG4105C7B. Bacteria.
COG1171. LUCA.
HOGENOMiHOG000046973.
KOiK01754.
OMAiILMAHNC.
OrthoDBiPOG091H03MP.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00054.

Family and domain databases

InterProiIPR001721. ACT-like_dom.
IPR011820. IlvA.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
PF00585. Thr_dehydrat_C. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR02079. THD1. 1 hit.
PROSITEiPS51672. ACT_LIKE. 1 hit.
PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiILVA_MYCLE
AccessioniPrimary (citable) accession number: Q9X7F1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 1, 1999
Last modified: September 7, 2016
This is version 93 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.