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Protein

L-threonine dehydratase catabolic TdcB

Gene

BLX71_00520

Organism
Salmonella newport
Status
Unreviewed-Annotation score: -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.UniRule annotation
TdcB also dehydrates serine to yield pyruvate via analogous enamine/imine intermediates.UniRule annotation

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Catalytic activityi

L-serine = pyruvate + NH3.UniRule annotation
L-threonine = 2-oxobutanoate + NH3.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi: L-threonine degradation via propanoate pathway

This protein is involved in step 1 of the subpathway that synthesizes propanoate from L-threonine.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. L-threonine dehydratase catabolic TdcB (BLX71_00520)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Propionate kinase (tdcD)
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.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyaseUniRule annotationImported
LigandNucleotide-bindingUniRule annotation, Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00052; UER00507

Names & Taxonomyi

Protein namesi
Recommended name:
L-threonine dehydratase catabolic TdcBUniRule annotation (EC:4.3.1.17UniRule annotation, EC:4.3.1.19UniRule annotation)
Alternative name(s):
L-serine dehydrataseUniRule annotation
Threonine deaminaseUniRule annotation
Gene namesi
ORF Names:BLX71_00520Imported, C4823_03405Imported, C4825_14455Imported, C4831_20360Imported, C4834_07145Imported, C4837_04285Imported, C4844_04870Imported, C4845_08245Imported, C4848_06965Imported, C4851_08705Imported, C4854_00530Imported, C4877_11980Imported
OrganismiSalmonella newportImported
Taxonomic identifieri108619 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000187320 Componenti: Unassembled WGS sequence

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).UniRule annotation

Structurei

3D structure databases

SMRiA0A0R9MXH5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 312PALPInterPro annotationAdd BLAST289

Sequence similaritiesi

Belongs to the serine/threonine dehydratase family.UniRule annotation

Family and domain databases

InterProiView protein in InterPro
IPR001926 PLP-dep
IPR000634 Ser/Thr_deHydtase_PyrdxlP-BS
IPR005789 Thr_deHydtase_catblc
IPR036052 Trypto_synt_PLP_dependent
PfamiView protein in Pfam
PF00291 PALP, 1 hit
SUPFAMiSSF53686 SSF53686, 1 hit
TIGRFAMsiTIGR01127 ilvA_1Cterm, 1 hit
PROSITEiView protein in PROSITE
PS00165 DEHYDRATASE_SER_THR, 1 hit

Sequencei

Sequence statusi: Complete.

A0A0R9MXH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHITYDLPVA IEDILEAKKR LAGKIYKTGM PRSNYFSERC KGEIFLKFEN
60 70 80 90 100
MQRTGSFKIR GAFNKLSSLT EAEKRKGVVA CSAGNHAQGV SLSCAMLGID
110 120 130 140 150
GKVVMPKGAP KSKVAATCDY SAEVVLHGDN FNDTIAKVSE IVETEGRIFI
160 170 180 190 200
PPYDDPKVIA GQGTIGLEIM EDLYDVDNVI VPIGGGGLIA GIAIAIKSIN
210 220 230 240 250
PTIKVIGVQA ENVHGMAASY YTGEITTHRT TGTLADGCDV SRPGNLTYEI
260 270 280 290 300
VRELVDDIVL VSEDEIRNSM IALIQRNKVI TEGAGALACA ALLSGKLDSH
310 320
IQNRKTVSII SGGNIDLSRV SQITGLVDA
Length:329
Mass (Da):35,141
Last modified:February 17, 2016 - v1
Checksum:iC1C619B021DE817C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
MODC01000003 Genomic DNA Translation: OMB09272.1
QDKZ01000025 Genomic DNA Translation: PVI59784.1
QDLW01000001 Genomic DNA Translation: PVJ09319.1
QDMC01000003 Genomic DNA Translation: PVJ42396.1
QDLZ01000004 Genomic DNA Translation: PVJ50578.1
QDMG01000002 Genomic DNA Translation: PVJ78174.1
QDMN01000002 Genomic DNA Translation: PVJ88190.1
QDMF01000028 Genomic DNA Translation: PVJ95997.1
QDMQ01000003 Genomic DNA Translation: PVK01881.1
QDMT01000012 Genomic DNA Translation: PVK18311.1
QDMZ01000017 Genomic DNA Translation: PVK31483.1
QDNB01000002 Genomic DNA Translation: PVK48462.1
RefSeqiWP_000548370.1, NZ_PJLN01000004.1

Genome annotation databases

PATRICifig|108619.17.peg.2351

Similar proteinsi

Entry informationi

Entry nameiA0A0R9MXH5_SALNE
AccessioniPrimary (citable) accession number: A0A0R9MXH5
Entry historyiIntegrated into UniProtKB/TrEMBL: February 17, 2016
Last sequence update: February 17, 2016
Last modified: July 18, 2018
This is version 20 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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