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Q2FF63

- ILVA_STAA3

UniProt

Q2FF63 - ILVA_STAA3

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Protein

L-threonine dehydratase biosynthetic IlvA

Gene

ilvA

Organism
Staphylococcus aureus (strain USA300)
Status
Reviewed - 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 sitei83 – 831Pyridoxal phosphateBy similarity
Binding sitei315 – 3151Pyridoxal phosphateBy similarity

GO - Molecular functioni

  1. L-threonine ammonia-lyase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. isoleucine biosynthetic process Source: UniProtKB-UniPathway
  2. threonine metabolic process Source: UniProtKB
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
ProteomesiUP000001939: Chromosome

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

Protein-protein interaction databases

STRINGi451515.SAUSA300_2014.

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.
OMAiEMLANFV.
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.
GeneIDi3915391.
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 .
RefSeqi YP_494665.1. NC_007793.1.

3D structure databases

ProteinModelPortali Q2FF63.
SMRi Q2FF63. Positions 11-329.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 451515.SAUSA300_2014.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABD20804 ; ABD20804 ; SAUSA300_2014 .
GeneIDi 3915391.
KEGGi saa:SAUSA300_2014.
PATRICi 19593533. VBIStaAur129981_2157.

Phylogenomic databases

eggNOGi COG1171.
HOGENOMi HOG000046973.
KOi K01754.
OMAi EMLANFV.
OrthoDBi EOG6ZSP7D.

Enzyme and pathway databases

UniPathwayi UPA00047 ; UER00054 .
BioCyci SAUR451515:GH3C-2014-MONOMER.

Family and domain databases

InterProi IPR001721. ACT-like_dom.
IPR011820. IlvA.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
PF00585. Thr_dehydrat_C. 1 hit.
[Graphical view ]
SUPFAMi SSF53686. SSF53686. 1 hit.
TIGRFAMsi TIGR02079. THD1. 1 hit.
PROSITEi PS51672. ACT_LIKE. 1 hit.
PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 58 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3