Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot B1LK55 (TDH_ECOSM)

Last modified November 3, 2009. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    L-threonine 3-dehydrogenase
    EC=1.1.1.103
Gene names
Name: tdh
Ordered Locus Names: EcSMS35_3953
OrganismEscherichia coli (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP]
Taxonomic identifier439855 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH. HAMAP MF_00627

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2. HAMAP MF_00627

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

threonine catabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-threonine 3-dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341L-threonine 3-dehydrogenase HAMAP MF_00627
PRO_1000130551

Sites

Metal binding381Zinc 1; catalytic By similarity
Metal binding631Zinc 1; catalytic By similarity
Metal binding931Zinc 2 By similarity
Metal binding961Zinc 2 By similarity
Metal binding991Zinc 2 By similarity
Metal binding1071Zinc 2 By similarity
Metal binding1481Zinc 1; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
B1LK55-1 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: AAB2927DC7E01C1E

FASTA34137,285
        10         20         30         40         50         60 
MKALSKLKAE EGIWMTDVPV PELGHNDLLI KIRKTAICGT DVHIYNWDEW SQKTIPVPMV 

        70         80         90        100        110        120 
VGHEYVGEVV GIGQEVKGFK IGDRVSGEGH ITCGHCRNCR GGRTHLCRNT IGVGVNRPGC 

       130        140        150        160        170        180 
FAEYLVIPAF NAFKIPDNIS DDLASIFDPF GNAVHTALSF DLVGEDVLVS GAGPIGIMAA 

       190        200        210        220        230        240 
AVAKHVGARN VVITDVNEYR LELARKMGIT RAVNVAKENL NDVMTELGMT EGFDVGLEMS 

       250        260        270        280        290        300 
GAPPAFRTML DTMNHGGRIA MLGIPPSDMS IDWTKVIFKG LFIKGIYGRE MFETWYKMAA 

       310        320        330        340 
LIQSGLDLSP IITHRFSIDD FQKGFDAMRS GQSGKVILSW D 

« Hide

References

[1]"Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
J. Bacteriol. 190:6779-6794(2008) [PubMed: 18708504] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000970 Genomic DNA. Translation: ACB19735.1.
RefSeqYP_001745918.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6143740.
GenomeReviewsGene locus EcSMS35_3953 in contig CP000970_GR.
KEGGecm:EcSMS35_3953.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAIWMVDAP.

Family and domain databases

HAMAPMF_00627.
[Tree]
InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
IPR004627. L-Threonine_3-DHase.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
ProDomPD040557. GroES_related. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00692. tdh. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTDH_ECOSM
AccessionPrimary (citable) accession number: B1LK55
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: November 3, 2009
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents