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Protein

L-threonine 3-dehydrogenase

Gene

tdh

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD+-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate. To a lesser extent, also catalyzes the oxidation of D-allo-threonine and L-threonine amide, but not that of D-threonine and L-allothreonine. Cannot utilize NADP+ instead of NAD+.1 Publication

Catalytic activityi

L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH.UniRule annotation1 Publication

Cofactori

Zn2+UniRule annotation1 Publication1 Publication, Co2+1 Publication, Cd2+1 PublicationNote: Binds 2 Zn2+ ions per subunit. Co2+ and Cd2+ can exchange for Zn2+ (PubMed:2007567). Probably contains one structural ion and one catalytic ion that seems to be less tightly bound at the site (PubMed:9784233).UniRule annotation1 Publication1 Publication

Enzyme regulationi

Is totally inhibited by EDTA in vitro.1 Publication

Kineticsi

  1. KM=1.43 mM for L-threonine (at 37 degrees Celsius and pH 8.4)1 Publication
  2. KM=0.19 mM for NAD+ (at 37 degrees Celsius and pH 8.4)1 Publication
  1. Vmax=57 µmol/min/mg enzyme for the NAD+ oxidation of L-threonine1 Publication

pH dependencei

Optimum pH is 10.3. At pH 9.0 and 11.0, the activity is 35% and only 6%, respectively, of the optimal level.1 Publication

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 annotation1 Publication
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

  • cadmium ion binding Source: EcoliWiki
  • ferrous iron binding Source: EcoCyc
  • L-threonine 3-dehydrogenase activity Source: EcoCyc
  • manganese ion binding Source: EcoliWiki
  • oxidoreductase activity Source: EcoliWiki
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

  • L-serine biosynthetic process Source: EcoliWiki
  • L-threonine catabolic process to glycine Source: UniProtKB-UniPathway
  • threonine catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Cobalt, Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:THREODEHYD-MONOMER.
ECOL316407:JW3591-MONOMER.
MetaCyc:THREODEHYD-MONOMER.
SABIO-RKP07913.
UniPathwayiUPA00046; UER00505.

Names & Taxonomyi

Protein namesi
Recommended name:
L-threonine 3-dehydrogenaseUniRule annotation (EC:1.1.1.103UniRule annotation1 Publication)
Short name:
TDH1 PublicationUniRule annotation
Alternative name(s):
L-threonine dehydrogenase2 Publications
Gene namesi
Name:tdh1 Publication
Ordered Locus Names:b3616, JW3591
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10993. tdh.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381C → D: Shows only 1% of wild-type catalytic activity. This mutant can be stimulated to the wild-type activity level after incubation with Zn(+). 1 Publication
Mutagenesisi38 – 381C → S: Loss of catalytic activity. This mutant cannot be stimulated to the wild-type activity level after incubation with Zn(+). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341L-threonine 3-dehydrogenasePRO_0000160837Add
BLAST

Proteomic databases

EPDiP07913.
PaxDbiP07913.
PRIDEiP07913.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi4263307. 21 interactions.
DIPiDIP-6855N.
IntActiP07913. 6 interactions.
STRINGi511145.b3616.

Structurei

3D structure databases

ProteinModelPortaliP07913.
SMRiP07913. Positions 1-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CPQ. Bacteria.
COG1063. LUCA.
HOGENOMiHOG000294686.
InParanoidiP07913.
KOiK00060.
OMAiDGIFAEY.
PhylomeDBiP07913.

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.

P07913-1 [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 DDLAAIFDPF
160 170 180 190 200
GNAVHTALSF DLVGEDVLVS GAGPIGIMAA AVAKHVGARN VVITDVNEYR
210 220 230 240 250
LELARKMGIT RAVNVAKENL 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):37,239
Last modified:November 1, 1988 - v1
Checksum:i039FBD6B1CE8C2B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06690 Genomic DNA. Translation: CAA29884.1.
U00039 Genomic DNA. Translation: AAB18593.1.
U00096 Genomic DNA. Translation: AAC76640.1.
AP009048 Genomic DNA. Translation: BAE77676.1.
PIRiA33276. DEECTH.
RefSeqiNP_418073.1. NC_000913.3.
WP_000646007.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76640; AAC76640; b3616.
BAE77676; BAE77676; BAE77676.
GeneIDi948139.
KEGGiecj:JW3591.
eco:b3616.
PATRICi32122719. VBIEscCol129921_3736.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06690 Genomic DNA. Translation: CAA29884.1.
U00039 Genomic DNA. Translation: AAB18593.1.
U00096 Genomic DNA. Translation: AAC76640.1.
AP009048 Genomic DNA. Translation: BAE77676.1.
PIRiA33276. DEECTH.
RefSeqiNP_418073.1. NC_000913.3.
WP_000646007.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP07913.
SMRiP07913. Positions 1-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263307. 21 interactions.
DIPiDIP-6855N.
IntActiP07913. 6 interactions.
STRINGi511145.b3616.

Proteomic databases

EPDiP07913.
PaxDbiP07913.
PRIDEiP07913.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76640; AAC76640; b3616.
BAE77676; BAE77676; BAE77676.
GeneIDi948139.
KEGGiecj:JW3591.
eco:b3616.
PATRICi32122719. VBIEscCol129921_3736.

Organism-specific databases

EchoBASEiEB0986.
EcoGeneiEG10993. tdh.

Phylogenomic databases

eggNOGiENOG4105CPQ. Bacteria.
COG1063. LUCA.
HOGENOMiHOG000294686.
InParanoidiP07913.
KOiK00060.
OMAiDGIFAEY.
PhylomeDBiP07913.

Enzyme and pathway databases

UniPathwayiUPA00046; UER00505.
BioCyciEcoCyc:THREODEHYD-MONOMER.
ECOL316407:JW3591-MONOMER.
MetaCyc:THREODEHYD-MONOMER.
SABIO-RKP07913.

Miscellaneous databases

PROiP07913.

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_ECOLI
AccessioniPrimary (citable) accession number: P07913
Secondary accession number(s): Q2M7T0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1988
Last modified: September 7, 2016
This is version 157 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, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.