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Protein

L-threonine dehydratase biosynthetic IlvA

Gene

ilvA

Organism
Staphylococcus aureus (strain USA300)
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

Pathway: 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 sitei83 – 831Pyridoxal phosphateBy similarity
Binding sitei315 – 3151Pyridoxal 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

BioCyciSAUR451515:GH3C-2014-MONOMER.
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:SAUSA300_2014
OrganismiStaphylococcus aureus (strain USA300)
Taxonomic identifieri367830 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422L-threonine dehydratase biosynthetic IlvAPRO_0000234304Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 561N6-(pyridoxal phosphate)lysineBy similarity

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ2FF63.
SMRiQ2FF63. Positions 11-329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini339 – 41375ACT-likePROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

Contains 1 ACT-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1171.
HOGENOMiHOG000046973.
KOiK01754.
OMAiKERAMRY.
OrthoDBiEOG6ZSP7D.

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.

Q2FF63-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVKTTVSTK DIDEAFLRLK DIVKETPLQL DHYLSQKYDC KVYLKREDLQ
60 70 80 90 100
WVRSFKLRGA YNAISVLSDE AKSKGITCAS AGNHAQGVAY TAKKLNLNAV
110 120 130 140 150
IFMPVTTPLQ KVNQVKFFGN SNVEVVLTGD TFDHCLAEAL TYTSEHQMNF
160 170 180 190 200
IDPFNNVHTI SGQGTLAKEM LEQAKSDNVN FDYLFAAIGG GGLISGISTY
210 220 230 240 250
FKTYSPTTKI IGVEPSGASS MYESVVVNNQ VVTLPNIDKF VDGASVARVG
260 270 280 290 300
DITFEIAKEN VDDYVQVDEG AVCSTILDMY SKQAIVAEPA GALSVSALEN
310 320 330 340 350
YKDHIKGKTV VCVISGGNND INRMKEIEER SLLYEEMKHY FILNFPQRPG
360 370 380 390 400
ALREFVNDVL GPQDDITKFE YLKKSSQNTG TVIIGIQLKD HDDLIQLKQR
410 420
VNHFDPSNIY INENKMLYSL LI
Length:422
Mass (Da):46,937
Last modified:March 21, 2006 - v1
Checksum:iA1A085175DA56D90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000255 Genomic DNA. Translation: ABD20804.1.
RefSeqiYP_494665.1. NC_007793.1.

Genome annotation databases

EnsemblBacteriaiABD20804; ABD20804; SAUSA300_2014.
KEGGisaa:SAUSA300_2014.
PATRICi19593533. VBIStaAur129981_2157.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000255 Genomic DNA. Translation: ABD20804.1.
RefSeqiYP_494665.1. NC_007793.1.

3D structure databases

ProteinModelPortaliQ2FF63.
SMRiQ2FF63. Positions 11-329.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD20804; ABD20804; SAUSA300_2014.
KEGGisaa:SAUSA300_2014.
PATRICi19593533. VBIStaAur129981_2157.

Phylogenomic databases

eggNOGiCOG1171.
HOGENOMiHOG000046973.
KOiK01754.
OMAiKERAMRY.
OrthoDBiEOG6ZSP7D.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00054.
BioCyciSAUR451515:GH3C-2014-MONOMER.

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...

Publicationsi

  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.

Entry informationi

Entry nameiILVA_STAA3
AccessioniPrimary (citable) accession number: Q2FF63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: March 21, 2006
Last modified: June 24, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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