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A1SVW5 (TDH_PSYIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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:Ping_1853
OrganismPsychromonas ingrahamii (strain 37) [Complete proteome] [HAMAP]
Taxonomic identifier357804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPsychromonadaceaePsychromonas

Protein attributes

Sequence length344 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 – 344344L-threonine 3-dehydrogenase HAMAP MF_00627
PRO_1000051647

Sites

Metal binding401Zinc 1; catalytic By similarity
Metal binding651Zinc 1; catalytic By similarity
Metal binding951Zinc 2 By similarity
Metal binding981Zinc 2 By similarity
Metal binding1011Zinc 2 By similarity
Metal binding1091Zinc 2 By similarity
Metal binding1501Zinc 1; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A1SVW5 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: FF035FE3358B8FA9

FASTA34437,405
        10         20         30         40         50         60 
MKIKALAKLK PEVGIWMTTV DKPEPGHNDL LIKIHKTAIC GTDIHIYNWD EWSQNTIPVP 

        70         80         90        100        110        120 
MVVGHEYVGE VVGMGQEVRG FSVGDRVSGE GHITCGHCRN CRAGRTHLCR NTIGVGVNRT 

       130        140        150        160        170        180 
GAFAEYLVIP AFNAFKIPAG ISDDLASIFD PFGNAVHSAL SFDVVGEDVL ITGAGPIGIM 

       190        200        210        220        230        240 
AAAVAKHAGA RYVVITDINE YRLDLARKMG VTRAVNVAQQ KLEDVIAQLG MTEGFDVGLE 

       250        260        270        280        290        300 
MSGAPVAFNS MLKNMSHGGK IALLGIPPSD MSIDWNMVIF KGLVIKGIYG REMFETWYKM 

       310        320        330        340 
ASLIQSGLDL DPIITHTFPV DKFQEGFDMM RSGKSGKVIL DWSI 

« Hide

References

[1]"Complete sequence of Psychromonas ingrahamii 37."
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., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Ivanova N., Staley J., Richardson P.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 37.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000510 Genomic DNA. Translation: ABM03630.1.
RefSeqYP_943229.1. NC_008709.1.

3D structure databases

ProteinModelPortalA1SVW5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1SVW5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4625040.
GenomeReviewsGene locus Ping_1853 in contig CP000510_GR.
KEGGpin:Ping_1853.
PATRIC23068863. VBIPsyIng103130_2033.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1063.
HOGENOMHBG753318.
OMANATHCAL.
PhylomeDBA1SVW5.
ProtClustDBPRK05396.

Enzyme and pathway databases

BioCycPING357804:PING_1853-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_PSYIN
AccessionPrimary (citable) accession number: A1SVW5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 46 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