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Protein

L-threonine 3-dehydrogenase

Gene

tdh

Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi38 – 381Zinc 1; catalyticUniRule annotation
Active sitei40 – 401Charge relay systemUniRule annotation
Active sitei43 – 431Charge relay systemUniRule annotation
Metal bindingi63 – 631Zinc 1; via tele nitrogen; catalyticUniRule annotation
Metal bindingi64 – 641Zinc 1; catalyticUniRule annotation
Metal bindingi93 – 931Zinc 2UniRule annotation
Metal bindingi96 – 961Zinc 2UniRule annotation
Metal bindingi99 – 991Zinc 2UniRule annotation
Metal bindingi107 – 1071Zinc 2UniRule annotation
Sitei148 – 1481Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atomUniRule annotation
Binding sitei175 – 1751NAD; via amide nitrogenUniRule annotation
Binding sitei195 – 1951NADUniRule annotation
Binding sitei200 – 2001NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi262 – 2643NADUniRule annotation
Nucleotide bindingi286 – 2872NADUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciECOL199310:C4443-MONOMER.
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:c4443
OrganismiEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Taxonomic identifieri199310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000001410 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341L-threonine 3-dehydrogenasePRO_0000160838Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi199310.c4443.

Structurei

3D structure databases

ProteinModelPortaliQ8FCA2.
SMRiQ8FCA2. Positions 1-341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CPQ. Bacteria.
COG1063. LUCA.
HOGENOMiHOG000294686.
KOiK00060.
OMAiVMSEIGM.

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.

Q8FCA2-1 [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 NAFKIPDNIS DDLASIFDPF
160 170 180 190 200
GNAVHTALSF DLVGEDVLVS GAGPIGIMAA AVAKHVGARN VVITDVNEYR
210 220 230 240 250
LELARKMGIT RAVNVAKENL NDVMTELGMT 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):37,285
Last modified:March 1, 2003 - v1
Checksum:iAAB2927DC7E01C1E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA. Translation: AAN82879.1.
RefSeqiWP_000646018.1. NC_004431.1.

Genome annotation databases

EnsemblBacteriaiAAN82879; AAN82879; c4443.
KEGGiecc:c4443.
PATRICi18286587. VBIEscCol75197_4168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA. Translation: AAN82879.1.
RefSeqiWP_000646018.1. NC_004431.1.

3D structure databases

ProteinModelPortaliQ8FCA2.
SMRiQ8FCA2. Positions 1-341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi199310.c4443.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN82879; AAN82879; c4443.
KEGGiecc:c4443.
PATRICi18286587. VBIEscCol75197_4168.

Phylogenomic databases

eggNOGiENOG4105CPQ. Bacteria.
COG1063. LUCA.
HOGENOMiHOG000294686.
KOiK00060.
OMAiVMSEIGM.

Enzyme and pathway databases

UniPathwayiUPA00046; UER00505.
BioCyciECOL199310:C4443-MONOMER.

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_ECOL6
AccessioniPrimary (citable) accession number: Q8FCA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 1, 2003
Last modified: September 7, 2016
This is version 99 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

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.