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Protein

L-threonine dehydratase biosynthetic IlvA

Gene

ilvA

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei90 – 901Pyridoxal phosphateBy similarity
Binding sitei316 – 3161Pyridoxal 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:HI_0738.1
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513L-threonine dehydratase biosynthetic IlvAPRO_0000185574Add
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

STRINGi71421.HI0738.1.

Structurei

3D structure databases

ProteinModelPortaliP46493.
SMRiP46493. Positions 10-512.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini340 – 41172ACT-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini433 – 50472ACT-like 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 1934Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Contains 2 ACT-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1171.
KOiK01754.
OMAiPQNTPSI.
OrthoDBiEOG6ZSP7D.
PhylomeDBiP46493.

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.

P46493-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNLLTNPQP SQSDYINAIV KLGSRVYEAA QVTPLQKMGK LSERLHNNIW
60 70 80 90 100
IKREDRQPVN SFKLRGAYAM ISSLSAEQKA AGVIAASAGN HAQGVALSAK
110 120 130 140 150
QLGLKALIVM PQNTPSIKVD AVRGFGGEVL LHGANFDEAK AKAIELSKEK
160 170 180 190 200
NMTFIPPFDH PLVIAGQGTL AMEMLQQVAD LDYVFVQVGG GGLAAGVAIL
210 220 230 240 250
LKQFMPEIKI IGVESKDSAC LKAALDKGEP TDLTHIGLFA DGVAVKRIGD
260 270 280 290 300
ETFRLCQQYL DDMVLVDSDE VCAAMKDLFE NVRAVAEPSG ALGLAGLKKY
310 320 330 340 350
VKQNHIEGKN MAAILSGANL NFHTLRYVSE RCEIGENREA LLAVTMPEQP
360 370 380 390 400
GSFLKFAYVL GNRAVTEFSY RYADDKRACV FVGVRTTNEQ EKADIIADLT
410 420 430 440 450
KNGFDVEDMS DDDIAKTHVR YLMGGRAAND NERLYTFEFP EQKGALLKFL
460 470 480 490 500
ETLQNRWNIS LFHYRAHGAD YGNILAGFQI EQREQAEFEQ GLAQLNYVFE
510
DVTKSKSYRY FLR
Length:513
Mass (Da):56,663
Last modified:November 1, 1995 - v1
Checksum:iDF42CA8B6FDE4CD7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22398.1.
RefSeqiNP_438898.1. NC_000907.1.
WP_010869046.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22398; AAC22398; HI_0738.1.
GeneIDi950764.
KEGGihin:HI0738.1.
PATRICi20190119. VBIHaeInf48452_0775.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22398.1.
RefSeqiNP_438898.1. NC_000907.1.
WP_010869046.1. NC_000907.1.

3D structure databases

ProteinModelPortaliP46493.
SMRiP46493. Positions 10-512.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI0738.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC22398; AAC22398; HI_0738.1.
GeneIDi950764.
KEGGihin:HI0738.1.
PATRICi20190119. VBIHaeInf48452_0775.

Phylogenomic databases

eggNOGiCOG1171.
KOiK01754.
OMAiPQNTPSI.
OrthoDBiEOG6ZSP7D.
PhylomeDBiP46493.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00054.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
  2. Koonin E.V., Rudd K.E.
    Submitted (SEP-1995) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiILVA_HAEIN
AccessioniPrimary (citable) accession number: P46493
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 27, 2015
This is version 106 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. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.