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Reviewed, UniProtKB/Swiss-Prot Q3IHW0 (TDH_PSEHT)

Last modified November 3, 2009. Version 43. 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: PSHAa2315
OrganismPseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]
Taxonomic identifier326442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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 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 – 341341L-threonine 3-dehydrogenase HAMAP MF_00627
PRO_1000051646

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
Q3IHW0-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 78E3E098A8EC6F60

FASTA34137,262
        10         20         30         40         50         60 
MKALSKLKAE PGIWMTDAPK PEVGHNDLLI KIRKTAICGT DVHIYKWDEW AQKTIPTPMV 

        70         80         90        100        110        120 
VGHEYVGEVV DMGQEVRGFK VGDRVSGEGH ITCGHCRNCR AGRVHLCRNT TGVGVNREGA 

       130        140        150        160        170        180 
FAEYLVIPAF NAFKIPDNIS DELASIFDPF GNAVHTALSF DLVGEDVLIT GAGPIGIMAA 

       190        200        210        220        230        240 
AVAKHVGARH VVISDVNEYR LELARKMGAT RAVNVANEKL EDVIKELGMT EGFDIGLEMS 

       250        260        270        280        290        300 
GVPSAFNSML NNMNHGGKVA MLGIPPSDMA VDWNQVIFKG LVIKGIYGRE MFETWYKMAS 

       310        320        330        340 
LIQSGLDLNP IITHQYSIDD FQAGFDMMIS GQSGKVILNW D 

« Hide

References

[1]"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125."
Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. expand/collapse author list , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.
Genome Res. 15:1325-1335(2005) [PubMed: 16169927] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CR954246 Genomic DNA. Translation: CAI87371.1.
RefSeqYP_340813.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ3IHW0.

Genome annotation databases

GeneID3709585.
GenomeReviewsGene locus PSHAa2315 in contig CR954246_GR.
KEGGpha:PSHAa2315.
NMPDRfig|326442.4.peg.2328.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3IHW0.
OMAIWMVDAP.

Enzyme and pathway databases

BioCycPHAL326442:PSHAA2315-MON.

Family and domain databases

HAMAPMF_00627.
[Tree]
InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
IPR004627. L-Threonine_3-DHase.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
ProDomPD040557. GroES_related. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00692. tdh. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTDH_PSEHT
AccessionPrimary (citable) accession number: Q3IHW0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 8, 2005
Last modified: November 3, 2009
This is version 43 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