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Q1BK24 (TDH_BURCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-threonine 3-dehydrogenase

EC=1.1.1.103
Gene names
Name:tdh
Ordered Locus Names:Bcen_5157
OrganismBurkholderia cenocepacia (strain AU 1054) [Complete proteome] [HAMAP]
Taxonomic identifier331271 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH. HAMAP-Rule 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-Rule 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_processL-threonine catabolic process to glycine

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-threonine 3-dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

nucleotide binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342L-threonine 3-dehydrogenase HAMAP-Rule MF_00627
PRO_1000051617

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
Q1BK24 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 71AA3DC7F3ECF29C

FASTA34237,358
        10         20         30         40         50         60 
MKALAKLERG PGLTLTRVKR PEVGHNDVLI KIRRTAICGT DIHIWKWDDW AQKTIPVPMH 

        70         80         90        100        110        120 
VGHEYVGEIV EMGQEVRGFA IGDRVSGEGH ITCGFCRNCR AGRRHLCRNT VGVGVNREGA 

       130        140        150        160        170        180 
FAEYLAIPAF NAFKIPPEIS DDLASIFDPF GNATHTALSF NLVGEDVLIT GAGPIGIMAV 

       190        200        210        220        230        240 
AIAKHVGARN VVITDINDYR LELARKMGAT RAVNVARESL RDVMADLHMT EGFDVGLEMS 

       250        260        270        280        290        300 
GVPSAFTSLL EAMNHGGKVA LLGIPPAQTA IDWNQVIFKG LEIKGIYGRE MFETWYKMVA 

       310        320        330        340 
MLQSGLDLSP IITHRFAADD YEQGFAAMLS GESGKVILDW TA 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia cenocepacia AU 1054."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K., Tiedje J.M., Richardson P.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AU 1054.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000379 Genomic DNA. Translation: ABF80031.1.
RefSeqYP_625004.1. NC_008061.1.

3D structure databases

ProteinModelPortalQ1BK24.
ModBaseSearch...

Protein-protein interaction databases

STRING331271.Bcen_5157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF80031; ABF80031; Bcen_5157.
GeneID4095105.
KEGGbcn:Bcen_5157.
PATRIC19054282. VBIBurCen11237_5345.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1063.
HOGENOMHOG000294686.
KOK00060.
OMAMSIDWNK.
ProtClustDBPRK05396.

Enzyme and pathway databases

BioCycBCEN331271:GHKX-3254-MONOMER.
UniPathwayUPA00046; UER00505.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00627. Thr_dehydrog.
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]
PANTHERPTHR11695. PTHR11695. 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_BURCA
AccessionPrimary (citable) accession number: Q1BK24
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 11, 2006
Last modified: May 1, 2013
This is version 61 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