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P46493 (ILVA_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-threonine dehydratase biosynthetic IlvA

EC=4.3.1.19
Alternative name(s):
Threonine deaminase
Gene names
Name:ilvA
Ordered Locus Names:HI_0738.1
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Catalytic activity

L-threonine = 2-oxobutanoate + NH3.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the serine/threonine dehydratase family.

Contains 2 ACT-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 513513L-threonine dehydratase biosynthetic IlvA
PRO_0000185574

Regions

Domain340 – 41172ACT-like 1
Domain433 – 50472ACT-like 2
Region190 – 1934Pyridoxal phosphate binding By similarity

Sites

Binding site901Pyridoxal phosphate By similarity
Binding site3161Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue631N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P46493 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: DF42CA8B6FDE4CD7

FASTA51356,663
        10         20         30         40         50         60 
MKNLLTNPQP SQSDYINAIV KLGSRVYEAA QVTPLQKMGK LSERLHNNIW IKREDRQPVN 

        70         80         90        100        110        120 
SFKLRGAYAM ISSLSAEQKA AGVIAASAGN HAQGVALSAK QLGLKALIVM PQNTPSIKVD 

       130        140        150        160        170        180 
AVRGFGGEVL LHGANFDEAK AKAIELSKEK NMTFIPPFDH PLVIAGQGTL AMEMLQQVAD 

       190        200        210        220        230        240 
LDYVFVQVGG GGLAAGVAIL LKQFMPEIKI IGVESKDSAC LKAALDKGEP TDLTHIGLFA 

       250        260        270        280        290        300 
DGVAVKRIGD ETFRLCQQYL DDMVLVDSDE VCAAMKDLFE NVRAVAEPSG ALGLAGLKKY 

       310        320        330        340        350        360 
VKQNHIEGKN MAAILSGANL NFHTLRYVSE RCEIGENREA LLAVTMPEQP GSFLKFAYVL 

       370        380        390        400        410        420 
GNRAVTEFSY RYADDKRACV FVGVRTTNEQ EKADIIADLT KNGFDVEDMS DDDIAKTHVR 

       430        440        450        460        470        480 
YLMGGRAAND NERLYTFEFP EQKGALLKFL ETLQNRWNIS LFHYRAHGAD YGNILAGFQI 

       490        500        510 
EQREQAEFEQ GLAQLNYVFE DVTKSKSYRY FLR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC22398.1.
RefSeqNP_438898.1. NC_000907.1.

3D structure databases

ProteinModelPortalP46493.
SMRP46493. Positions 10-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI0738.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC22398; AAC22398; HI_0738.1.
GeneID950764.
KEGGhin:HI0738.1.
PATRIC20190119. VBIHaeInf48452_0775.

Phylogenomic databases

eggNOGCOG1171.
KOK01754.
OMASDNEMAK.
OrthoDBEOG6ZSP7D.
ProtClustDBPRK09224.

Enzyme and pathway databases

UniPathwayUPA00047; UER00054.

Family and domain databases

InterProIPR001721. ACT-like_dom.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR005787. Thr_deHydtase_biosynth.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
PF00585. Thr_dehydrat_C. 2 hits.
[Graphical view]
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR01124. ilvA_2Cterm. 1 hit.
PROSITEPS51672. ACT_LIKE. 2 hits.
PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameILVA_HAEIN
AccessionPrimary (citable) accession number: P46493
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 22, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names