Skip Header

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

Reviewed, UniProtKB/Swiss-Prot Q6AAR3 (TDH_PROAC)

Last modified January 19, 2010. Version 44. 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: PPA0402
OrganismPropionibacterium acnes [Complete proteome] [HAMAP]
Taxonomic identifier1747 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

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 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 – 345345L-threonine 3-dehydrogenase HAMAP MF_00627
PRO_0000160849

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 binding1491Zinc 1; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6AAR3-1 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 1592122C0584062A

FASTA34537,339
        10         20         30         40         50         60 
MKALVKTRPE PGLELVEVPD PVAGPNDVIV KVMRTGICGT DVHIDKWDGW AAKTVHTPLV 

        70         80         90        100        110        120 
LGHEFCGEIV ELGSEVNDLE VGQFVSGEGH YVCGRCRACL AGKRHLCRNT QGIGYAVNGA 

       130        140        150        160        170        180 
YCQYFVMPAG NVWVHHIPDL DPDVAAIFDP FGNAVHTALQ FPCLAEDVLV SGAGPIGIMA 

       190        200        210        220        230        240 
ALVAQFQGAR NVVVTDLSDE RLELAQQLGL KNAVNVSREG LETVWDRFDM KEGFDIGLEM 

       250        260        270        280        290        300 
SGSGTALTSM IDNMTHGGRI ALLGTPSTDI TLDFSKIIFN MITIQGVTGR QIFETWYTMA 

       310        320        330        340 
SLIRSGLDIS GIITDRYPIT EFREAFDVAG SGHGGKVVMN WECLD 

« Hide

References

[1]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed: 15286373] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017283 Genomic DNA. Translation: AAT82153.1.
RefSeqYP_055111.1.

3D structure databases

SMRQ6AAR3. Positions 1-342.
ModBaseSearch...

Genome annotation databases

GeneID2931139.
GenomeReviewsGene locus PPA0402 in contig AE017283_GR.
KEGGpac:PPA0402.
NMPDRfig|267747.1.peg.388.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG753318.
OMAMEIASIF.

Enzyme and pathway databases

BioCycPACN267747:PPA0402-MONOMER.
BRENDA1.1.1.103. 39123.

Family and domain databases

HAMAPMF_00627. Thr_dehydrog.
[Tree]
InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR004627. L-Threonine_3-DHase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTDH_PROAC
AccessionPrimary (citable) accession number: Q6AAR3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: September 13, 2004
Last modified: January 19, 2010
This is version 44 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