tdh:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

Tdh

Synonyms

threonine 3-dehydrogenase, NAD(P)-binding[1], B3616[2][1], Tdh[2][1] , ECK3606, JW3591, b3616

Product description

Tdh[2][3];

Component of threonine dehydrogenase[2][3]

Threonine dehydrogenase[4]

EC number (for enzymes)
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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0008743

L-threonine 3-dehydrogenase activity

PMID:6780553[5]

IDA: Inferred from Direct Assay

F

complete

GO:0005488

binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR016040

F

Seeded from EcoCyc (v14.0)

complete

GO:0005829

cytosol

PMID:16858726[6]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0006564

L-serine biosynthetic process

PMID:3108237[7]

IGI: Inferred from Genetic Interaction

EcoliWiki:serC


P

tdh serC double mutants are unable to synthesize serine by the alternate pathway (Tut cycle) and cannot grow on LRKTM:240 medium (minimal medium containing 240 mg/liter of leucine, arginine, lysine, threonine, and methionine)

complete

GO:0006567

threonine catabolic process

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00627

P

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

PMID:6780553[5]

IDA: Inferred from Direct Assay

C

complete

GO:0006567

threonine catabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004627

P

Seeded from EcoCyc (v14.0)

complete

GO:0008270

zinc ion binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002085

F

Seeded from EcoCyc (v14.0)

complete

GO:0016491

oxidoreductase activity

PMID:6780553[5]

IDA: Inferred from Direct Assay

F

complete

GO:0008270

zinc ion binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002328

F

Seeded from EcoCyc (v14.0)

complete

GO:0030145

manganese ion binding

PMID:6780553[5]

IDA: Inferred from Direct Assay

F

complete

GO:0046870

cadmium ion binding

PMID:3056527[8]

IDA: Inferred from Direct Assay

F

complete

GO:0008270

zinc ion binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013149

F

Seeded from EcoCyc (v14.0)

complete

GO:0008270

zinc ion binding

PMID:2007567[9]

IDA: Inferred from Direct Assay

F

complete

GO:0008270

zinc ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0862

F

Seeded from EcoCyc (v14.0)

complete

GO:0008743

L-threonine 3-dehydrogenase activity

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00627

F

Seeded from EcoCyc (v14.0)

complete

GO:0006564

L-serine biosynthetic process

PMID:3108237[7]

IGI: Inferred from Genetic Interaction

EcoliWiki:serB


P

tdh serB double mutants are unable to synthesize serine by the alternate pathway (Tut cycle) and cannot grow on LRKTM:240 medium (minimal medium containing 240 mg/liter of leucine, arginine, lysine, threonine, and methionine)

complete

GO:0008743

L-threonine 3-dehydrogenase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004627

F

Seeded from EcoCyc (v14.0)

complete

GO:0006564

L-serine biosynthetic process

PMID:3108237[7]

IGI: Inferred from Genetic Interaction

EcoliWiki:serA


P

tdh serA double mutants are unable to synthesize serine by the alternate pathway (Tut cycle) and cannot grow on LRKTM:240 medium (minimal medium containing 240 mg/liter of leucine, arginine, lysine, threonine, and methionine)

complete

GO:0008743

L-threonine 3-dehydrogenase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:1.1.1.103

F

Seeded from EcoCyc (v14.0)

complete

GO:0030145

manganese ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0464

F

Seeded from EcoCyc (v14.0)

complete

GO:0050897

cobalt ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0170

F

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002328

P

Seeded from EcoCyc (v14.0)

complete

GO:0030145

manganese ion binding

PMID:3518793[10]

IDA: Inferred from Direct Assay

F

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of threonine dehydrogenase

could be indirect

Protein

ebgR

PMID:16606699[11]

Experiment(s):EBI-1146260

Protein

groL

PMID:16606699[11]

Experiment(s):EBI-1146260

Protein

nadE

PMID:16606699[11]

Experiment(s):EBI-1146260
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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes
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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MKALSKLKAE EGIWMTDVPV PELGHNDLLI KIRKTAICGT DVHIYNWDEW SQKTIPVPMV
VGHEYVGEVV GIGQEVKGFK IGDRVSGEGH ITCGHCRNCR GGRTHLCRNT IGVGVNRPGC
FAEYLVIPAF NAFKIPDNIS DDLAAIFDPF GNAVHTALSF DLVGEDVLVS GAGPIGIMAA
AVAKHVGARN VVITDVNEYR LELARKMGIT RAVNVAKENL NDVMAELGMT EGFDVGLEMS
GAPPAFRTML DTMNHGGRIA MLGIPPSDMS IDWTKVIFKG LFIKGIYGRE MFETWYKMAA
LIQSGLDLSP IITHRFSIDD FQKGFDAMRS GQSGKVILSW D
Length

341

Mol. Wt

37.239 kDa

pI

6.4 (calculated)

Extinction coefficient

41,940 - 42,690 (calc based on 6 Y, 6 W, and 6 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

174..304

PF00107 Zinc-binding dehydrogenase

PMID:19920124[12]

Domain

25..135

PF08240 Alcohol dehydrogenase GroES-like domain

PMID:19920124[12]

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Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=tdh taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16131487

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:948139

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0011830

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P07913

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10993

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10993

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:948139

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000982

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0986

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 5.2 5.3 Boylan, SA & Dekker, EE (1981) L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12. J. Biol. Chem. 256 1809-15 PubMed
  6. ↑ Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed
  7. ↑ 7.0 7.1 7.2 Ravnikar, PD & Somerville, RL (1987) Genetic characterization of a highly efficient alternate pathway of serine biosynthesis in Escherichia coli. J. Bacteriol. 169 2611-7 PubMed
  8. ↑ Craig, PA & Dekker, EE (1988) Cd2+ activation of L-threonine dehydrogenase from Escherichia coli K-12. Biochim. Biophys. Acta 957 222-9 PubMed
  9. ↑ Epperly, BR & Dekker, EE (1991) L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies. J. Biol. Chem. 266 6086-92 PubMed
  10. ↑ Craig, PA & Dekker, EE (1986) L-threonine dehydrogenase from Escherichia coli K-12: thiol-dependent activation by Mn2+. Biochemistry 25 1870-6 PubMed
  11. ↑ 11.0 11.1 11.2 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  12. ↑ 12.0 12.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

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