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Q2IJN4 (TDH_ANADE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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:Adeh_2095
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length345 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 – 345345L-threonine 3-dehydrogenase HAMAP MF_00627
PRO_1000051614

Sites

Metal binding391Zinc 1; catalytic By similarity
Metal binding641Zinc 1; catalytic By similarity
Metal binding941Zinc 2 By similarity
Metal binding971Zinc 2 By similarity
Metal binding1001Zinc 2 By similarity
Metal binding1081Zinc 2 By similarity
Metal binding1491Zinc 1; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2IJN4 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 1EA58B8901D05EF0

FASTA34538,025
        10         20         30         40         50         60 
MKALVKAKRE EGIWMQHDVP VPEVGVHDVM IRVTKSAICG TDVHIYNWDE WSQKTVPVPM 

        70         80         90        100        110        120 
VVGHEYVGRV ERVGAEVEAF RPGERVSGEG HVTCGFCRNC RAGRRHLCRH TVGVGVNRPG 

       130        140        150        160        170        180 
SFAEYVVIPA DNVYRIPDDI PDDIAAIFDP FGNATHTALS FDLVGEDVLV TGAGPIGVMA 

       190        200        210        220        230        240 
AAIARHVGAR HVVVTDVNDY RLDLARRMGA SRAVNVARED LRAVMSELGM REGFDVGLEM 

       250        260        270        280        290        300 
SGNGRAFRQL LEVMNHGGRI ALLGIMPGPE PIDWSQVVFK GLQLKGVYGR EMYETWYKMV 

       310        320        330        340 
AMLQSGLDLS AVVTHRFSID DFQQGFDVMR SGRSGKVVLD WGVAR 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000251 Genomic DNA. Translation: ABC81865.1.
RefSeqYP_465302.1. NC_007760.1.

3D structure databases

ProteinModelPortalQ2IJN4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2IJN4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3888333.
GenomeReviewsGene locus Adeh_2095 in contig CP000251_GR.
KEGGade:Adeh_2095.
PATRIC20920347. VBIAnaDeh31384_2153.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1063.
HOGENOMHBG753318.
OMAMMRSGMS.
PhylomeDBQ2IJN4.
ProtClustDBPRK05396.

Enzyme and pathway databases

BioCycADEH290397:ADEH_2095-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_ANADE
AccessionPrimary (citable) accession number: Q2IJN4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 53 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