Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

L-threonine 3-dehydrogenase

Gene

tdh

Organism
Shigella dysenteriae serotype 1 (strain Sd197)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the NAD+-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.UniRule annotation

Catalytic activityi

L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 2 Zn2+ ions per subunit.UniRule annotation

Pathwayi: L-threonine degradation via oxydo-reductase pathway

This protein is involved in step 1 of the subpathway that synthesizes glycine from L-threonine.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. L-threonine 3-dehydrogenase (tdh)
  2. 2-amino-3-ketobutyrate coenzyme A ligase (kbl)
This subpathway is part of the pathway L-threonine degradation via oxydo-reductase 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 glycine from L-threonine, the pathway L-threonine degradation via oxydo-reductase pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi38Zinc 1; catalyticUniRule annotation1
Active sitei40Charge relay systemUniRule annotation1
Active sitei43Charge relay systemUniRule annotation1
Metal bindingi63Zinc 1; via tele nitrogen; catalyticUniRule annotation1
Metal bindingi64Zinc 1; catalyticUniRule annotation1
Metal bindingi93Zinc 2UniRule annotation1
Metal bindingi96Zinc 2UniRule annotation1
Metal bindingi99Zinc 2UniRule annotation1
Metal bindingi107Zinc 2UniRule annotation1
Sitei148Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atomUniRule annotation1
Binding sitei175NAD; via amide nitrogenUniRule annotation1
Binding sitei195NADUniRule annotation1
Binding sitei200NADUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi262 – 264NADUniRule annotation3
Nucleotide bindingi286 – 287NADUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

UniPathwayiUPA00046; UER00505.

Names & Taxonomyi

Protein namesi
Recommended name:
L-threonine 3-dehydrogenaseUniRule annotation (EC:1.1.1.103UniRule annotation)
Short name:
TDHUniRule annotation
Gene namesi
Name:tdhUniRule annotation
Ordered Locus Names:SDY_4049
OrganismiShigella dysenteriae serotype 1 (strain Sd197)
Taxonomic identifieri300267 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002716 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000516621 – 341L-threonine 3-dehydrogenaseAdd BLAST341

Proteomic databases

PRIDEiQ329N8.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ329N8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the zinc-containing alcohol dehydrogenase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000294686.
KOiK00060.
OMAiDGIFAEY.
OrthoDBiPOG091H03K6.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
HAMAPiMF_00627. Thr_dehydrog. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR004627. L-Threonine_3-DHase.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00692. tdh. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q329N8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALSKLKAE EGIWMTDVPV PELGHNDLLI KIRKTAICGT DVHIYNWDEW
60 70 80 90 100
SQKTIPVPMV VGHEYVGEVV GIGQEVKGFK IGDRVSGEGH ITCGHCRNCR
110 120 130 140 150
GGRTHLCRNT IGVGVNRPGC FAEYLVIPAF NAFKIPGNIS DDLASIFDPF
160 170 180 190 200
GNAVHTALSF DLVGEDVLVS GAGPIGIMAA AVAKHVGARN VVITDVNEYR
210 220 230 240 250
LELARKMGIT RAANVAKENL NDVMAELGMT EGFDVGLEMS GAPPAFRTML
260 270 280 290 300
DTMNHGGRIA MLGIPPSDMS IDWTKVIFKG LFIKGIYGRE MFETWYKMAA
310 320 330 340
LIQSGLDLSP IITHRFSIDD FQKGFDAMRS GQSGKVILSW D
Length:341
Mass (Da):37,169
Last modified:December 6, 2005 - v1
Checksum:i354556FFA47BEDAE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000034 Genomic DNA. Translation: ABB63967.1.
RefSeqiWP_000646020.1. NC_007606.1.
YP_405458.1. NC_007606.1.

Genome annotation databases

EnsemblBacteriaiABB63967; ABB63967; SDY_4049.
GeneIDi3795531.
KEGGisdy:SDY_4049.
PATRICi18698819. VBIShiDys99784_4765.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000034 Genomic DNA. Translation: ABB63967.1.
RefSeqiWP_000646020.1. NC_007606.1.
YP_405458.1. NC_007606.1.

3D structure databases

ProteinModelPortaliQ329N8.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ329N8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB63967; ABB63967; SDY_4049.
GeneIDi3795531.
KEGGisdy:SDY_4049.
PATRICi18698819. VBIShiDys99784_4765.

Phylogenomic databases

HOGENOMiHOG000294686.
KOiK00060.
OMAiDGIFAEY.
OrthoDBiPOG091H03K6.

Enzyme and pathway databases

UniPathwayiUPA00046; UER00505.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
HAMAPiMF_00627. Thr_dehydrog. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR004627. L-Threonine_3-DHase.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00692. tdh. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTDH_SHIDS
AccessioniPrimary (citable) accession number: Q329N8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: November 2, 2016
This is version 88 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, Reference 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.