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Q0BKV5 (TDH_FRATO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:FTH_1473
OrganismFrancisella tularensis subsp. holarctica (strain OSU18) [Complete proteome] [HAMAP]
Taxonomic identifier393011 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length351 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. HAMAP-Rule MF_00627

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. HAMAP-Rule MF_00627

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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_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: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 351351L-threonine 3-dehydrogenase HAMAP-Rule MF_00627
PRO_1000051640

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
Q0BKV5 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 1E07E9CCC5A58A79

FASTA35138,400
        10         20         30         40         50         60 
MKALAKLKKQ PGIWMINDAP IPEYGYNDVL IKIKKTAICG TDLHIYNWDK WSQNTIPVPM 

        70         80         90        100        110        120 
ITGHEFAGEV VAKGDGVTSV DIGDRVSGEG HLVCGQCRNC RAGKRHLCRK TIGIGVNVQG 

       130        140        150        160        170        180 
AFAEYLVMPA VNVFKIPDSI SDDIASTFDP MGNAIHTALS FNLTGEDVLI TGAGPIGLMA 

       190        200        210        220        230        240 
VKIARFCGAR RIVITDINEY RLQMARDFGA TVALNVAPFK NQDELVKQMR KVMSDIGMTE 

       250        260        270        280        290        300 
GFDVGLEMSG INSAISMMLD VMNHGGKLSL LGISAGDISV DWGAILFKGL TLKGIYGREM 

       310        320        330        340        350 
FETWYLMTSM LQAGMDMNPI ITHRLHIDEF QKGFEIMKSG QCGKVILDWS S 

« Hide

References

[1]"Chromosome rearrangement and diversification of Francisella tularensis revealed by the type B (OSU18) genome sequence."
Petrosino J.F., Xiang Q., Karpathy S.E., Jiang H., Yerrapragada S., Liu Y., Gioia J., Hemphill L., Gonzalez A., Raghavan T.M., Uzman A., Fox G.E., Highlander S., Reichard M., Morton R.J., Clinkenbeard K.D., Weinstock G.M.
J. Bacteriol. 188:6977-6985(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OSU18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000437 Genomic DNA. Translation: ABI83279.1.
RefSeqYP_763916.1. NC_008369.1.

3D structure databases

ProteinModelPortalQ0BKV5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393011.FTH_1473.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI83279; ABI83279; FTH_1473.
GeneID4307881.
KEGGfth:FTH_1473.
PATRIC17953132. VBIFraTul3936_1691.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1063.
HOGENOMHOG000294686.
KOK00060.
OMAFELMRAG.
OrthoDBEOG60PH85.
ProtClustDBPRK05396.

Enzyme and pathway databases

BioCycFTUL393011:GHFN-1509-MONOMER.
UniPathwayUPA00046; UER00505.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 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. SSF50129. 1 hit.
TIGRFAMsTIGR00692. tdh. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTDH_FRATO
AccessionPrimary (citable) accession number: Q0BKV5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: February 19, 2014
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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways