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Q5WYJ7 (TDH_LEGPL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-threonine 3-dehydrogenase

EC=1.1.1.103
Gene names
Name:tdh
Ordered Locus Names:lpl0739
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
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. HAMAP MF_00627

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. HAMAP MF_00627

Subcellular location

Cytoplasm By similarity HAMAP MF_00627.

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 processthreonine catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-threonine 3-dehydrogenase activity

Inferred from electronic annotation. Source: EC

nucleotide binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 340340L-threonine 3-dehydrogenase HAMAP MF_00627
PRO_0000160845

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
Q5WYJ7 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: F1D91E3E39A77CF8

FASTA34037,210
        10         20         30         40         50         60 
MKSLVKAKKE PGIWMQDIPV PEYGVNDVLI KIKRTAICGT DIHIYSWDEW AQATIPVPMT 

        70         80         90        100        110        120 
VGHEFYGEIV EVGKEVQGLK VGQRVSGEGH ITCGFCRNCR AGKRHLCRNT LGVGVNRPGC 

       130        140        150        160        170        180 
FAEYLALPAT NVIALPDNIT EEQAAILDPF GNAAHCALAF DVVGEDVLIT GAGPIGIMAA 

       190        200        210        220        230        240 
AIVRHIGARH VVITDVNDHR LELARKMGVS RAVNVKYQKL SDVANELGML EGFDVGLEMS 

       250        260        270        280        290        300 
GNPMALNDMM KAMNHGGHVA LLGIPPQETP IDWNQVIFKG LVIKGIYGRE MFETWYKMIA 

       310        320        330        340 
MLQSGLNISP VITHNFPVDE YQHAFQIMAS GQSGKVILNW 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed: 15467720] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Lens.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628337 Genomic DNA. Translation: CAH14973.1.
RefSeqYP_126101.1. NC_006369.1.

3D structure databases

ProteinModelPortalQ5WYJ7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5WYJ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3114844.
GenomeReviewsGene locus lpl0739 in contig CR628337_GR.
KEGGlpf:lpl0739.
NMPDRfig|297245.3.peg.67.
PATRIC22315031. VBILegPne33733_0850.

Organism-specific databases

LegioListlpl0739.
CMRSearch...

Phylogenomic databases

eggNOGCOG1063.
HOGENOMHBG753318.
OMAHIRAWDG.
PhylomeDBQ5WYJ7.
ProtClustDBPRK05396.

Enzyme and pathway databases

BioCycLPNE297245:LPL0739-MONOMER.

Family and domain databases

HAMAPMF_00627. Thr_dehydrog.
[Tree]
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR004627. L-Threonine_3-DHase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00060.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
TIGRFAMsTIGR00692. Tdh. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTDH_LEGPL
AccessionPrimary (citable) accession number: Q5WYJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: November 23, 2004
Last modified: January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families