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Protein

L-threonine dehydratase catabolic TdcB

Gene

tdcB

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

Enzyme regulationi

Each protein molecule can bind up to four molecules of AMP, which act as an allosteric activator to the enzyme.By similarity

Pathwayi: L-threonine degradation via propanoate pathway

This protein is involved in step 1 of the subpathway that synthesizes propanoate from L-threonine.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. L-threonine dehydratase catabolic TdcB (tdcB)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
This subpathway is part of the pathway L-threonine degradation via propanoate pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes propanoate from L-threonine, the pathway L-threonine degradation via propanoate pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei94 – 941AMPBy similarity
Binding sitei321 – 3211AMPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi59 – 602AMPBy similarity
Nucleotide bindingi125 – 1262AMPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Nucleotide-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-1339-MONOMER.
UniPathwayiUPA00052; UER00507.

Names & Taxonomyi

Protein namesi
Recommended name:
L-threonine dehydratase catabolic TdcB (EC:4.3.1.19)
Alternative name(s):
Threonine deaminase
Gene namesi
Name:tdcB
Ordered Locus Names:SA1271
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000751 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 346346L-threonine dehydratase catabolic TdcBPRO_0000287332Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641N6-(pyridoxal phosphate)lysineBy similarity

Interactioni

Subunit structurei

In the native structure, TdcB is in a dimeric form, whereas in the TdcB-AMP complex, it exists in a tetrameric form (dimer of dimers).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ7A5L8.
SMRiQ7A5L8. Positions 14-330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000046972.
OMAiDTPCVES.
OrthoDBiEOG6ZSP7D.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR005789. Thr_deHydtase_catblc.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01127. ilvA_1Cterm. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7A5L8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTNTVTLQT AHIVSLGDIE EAKASIKPFI RRTPLIKSMY LSQNITKGNV
60 70 80 90 100
YLKLENMQFT GSFKFRGASN KINHLSDEQK AKGIIGASAG NHAQGVALTA
110 120 130 140 150
KLLGIDATIV MPETAPIAKQ NATKGYGAKV ILKGKNFNET RLYMEELAKE
160 170 180 190 200
NGMTIVHPYD DKFVMAGQGT IGLEILDDIW NVNTVIVPVG GGGLIAGIAT
210 220 230 240 250
ALKSFNPSIH IIGVQAENVH GMAESFYKRA LTEHREDSTI ADGCDVKVPG
260 270 280 290 300
EKTYEVVKHL VDEFILVSEE EIEHAMQDLM QRAKIITEGA GALPTAAILS
310 320 330 340
GKIDKKWLEG KNVVALVSGG NVDLTRVSGV IEHGLNIADT SKGVVG
Length:346
Mass (Da):37,147
Last modified:July 5, 2004 - v1
Checksum:i4435206B7E89CC10
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB42531.1.
PIRiF89921.
RefSeqiWP_000210817.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB42531; BAB42531; BAB42531.
PATRICi19574800. VBIStaAur116463_1369.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB42531.1.
PIRiF89921.
RefSeqiWP_000210817.1. NC_002745.2.

3D structure databases

ProteinModelPortaliQ7A5L8.
SMRiQ7A5L8. Positions 14-330.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB42531; BAB42531; BAB42531.
PATRICi19574800. VBIStaAur116463_1369.

Phylogenomic databases

HOGENOMiHOG000046972.
OMAiDTPCVES.
OrthoDBiEOG6ZSP7D.

Enzyme and pathway databases

UniPathwayiUPA00052; UER00507.
BioCyciSAUR158879:GJCB-1339-MONOMER.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR005789. Thr_deHydtase_catblc.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01127. ilvA_1Cterm. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: N315.
  2. "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
    Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
    Submitted (OCT-2007) to UniProtKB
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: N315.

Entry informationi

Entry nameiTDCB_STAAN
AccessioniPrimary (citable) accession number: Q7A5L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: July 5, 2004
Last modified: March 16, 2016
This is version 78 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

Allosteric enzyme, Complete proteome

Documents

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

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 one 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.