Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2FF63 (ILVA_STAA3) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:SAUSA300_2014
OrganismStaphylococcus aureus (strain USA300) [Complete proteome] [HAMAP]
Taxonomic identifier367830 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length422 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 1 ACT-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422L-threonine dehydratase biosynthetic IlvA
PRO_0000234304

Regions

Domain339 – 41375ACT-like
Region190 – 1934Pyridoxal phosphate binding By similarity

Sites

Binding site831Pyridoxal phosphate By similarity
Binding site3151Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue561N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2FF63 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: A1A085175DA56D90

FASTA42246,937
        10         20         30         40         50         60 
MTVKTTVSTK DIDEAFLRLK DIVKETPLQL DHYLSQKYDC KVYLKREDLQ WVRSFKLRGA 

        70         80         90        100        110        120 
YNAISVLSDE AKSKGITCAS AGNHAQGVAY TAKKLNLNAV IFMPVTTPLQ KVNQVKFFGN 

       130        140        150        160        170        180 
SNVEVVLTGD TFDHCLAEAL TYTSEHQMNF IDPFNNVHTI SGQGTLAKEM LEQAKSDNVN 

       190        200        210        220        230        240 
FDYLFAAIGG GGLISGISTY FKTYSPTTKI IGVEPSGASS MYESVVVNNQ VVTLPNIDKF 

       250        260        270        280        290        300 
VDGASVARVG DITFEIAKEN VDDYVQVDEG AVCSTILDMY SKQAIVAEPA GALSVSALEN 

       310        320        330        340        350        360 
YKDHIKGKTV VCVISGGNND INRMKEIEER SLLYEEMKHY FILNFPQRPG ALREFVNDVL 

       370        380        390        400        410        420 
GPQDDITKFE YLKKSSQNTG TVIIGIQLKD HDDLIQLKQR VNHFDPSNIY INENKMLYSL 


LI 

« Hide

References

[1]"Complete genome sequence of USA300, an epidemic clone of community-acquired meticillin-resistant Staphylococcus aureus."
Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., Perdreau-Remington F.
Lancet 367:731-739(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: USA300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000255 Genomic DNA. Translation: ABD20804.1.
RefSeqYP_494665.1. NC_007793.1.

3D structure databases

ProteinModelPortalQ2FF63.
SMRQ2FF63. Positions 9-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING451515.SAUSA300_2014.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD20804; ABD20804; SAUSA300_2014.
GeneID3915391.
KEGGsaa:SAUSA300_2014.
PATRIC19593533. VBIStaAur129981_2157.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1171.
HOGENOMHOG000046973.
KOK01754.
OMAKERAQRY.
OrthoDBEOG6ZSP7D.
ProtClustDBPRK08639.

Enzyme and pathway databases

BioCycSAUR451515:GH3C-2014-MONOMER.
UniPathwayUPA00047; UER00054.

Family and domain databases

InterProIPR001721. ACT-like_dom.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR011820. Threonine_deHydtase_mt/plastid.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
PF00585. Thr_dehydrat_C. 1 hit.
[Graphical view]
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR02079. THD1. 1 hit.
PROSITEPS51672. ACT_LIKE. 1 hit.
PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameILVA_STAA3
AccessionPrimary (citable) accession number: Q2FF63
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: March 21, 2006
Last modified: March 19, 2014
This is version 52 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