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A4SHB7 (TDH_AERS4) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 41. 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:ASA_0090
OrganismAeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]
Taxonomic identifier382245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length342 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 – 342342L-threonine 3-dehydrogenase HAMAP MF_00627
PRO_1000051613

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
A4SHB7 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: ED5BC243717B31D7

FASTA34237,280
        10         20         30         40         50         60 
MKALSKLKAE VGIWMTDVPA PELGHNDLLI KIRKTAICGT DMHIYNWDEW AQKTIPVPMV 

        70         80         90        100        110        120 
VGHEYVGEVV AVGQEVRGFA VGDRVSGEGH ITCGHCRNCR AGRTHLCRNT IGVGVNRPGS 

       130        140        150        160        170        180 
FAEYLVIPAF NAFKLPDNIP DELAAIFDPF GNAVHTALSF DLVGEDVLIT GAGPIGIMAA 

       190        200        210        220        230        240 
AVCRHVGARH VVITDVNEYR LELARKMGAT RAVNVSKEKL ADVMSALGMT EGFDVGLEMS 

       250        260        270        280        290        300 
GVPSAFQDMI DKMNHGGKIA MLGIPPSTMA IDWNKVIFKG LFIKGIYGRE MFETWYKMAS 

       310        320        330        340 
LIQSGLDLTP IITHHFHIDD FQQGFEAMGS GKSGKVILSW DK 

« Hide

References

[1]"The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
BMC Genomics 9:427-427(2008) [PubMed: 18801193] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A449.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000644 Genomic DNA. Translation: ABO88289.1.
RefSeqYP_001140037.1. NC_009348.1.

3D structure databases

ProteinModelPortalA4SHB7.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4SHB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4994813.
GenomeReviewsGene locus ASA_0090 in contig CP000644_GR.
KEGGasa:ASA_0090.
PATRIC20786472. VBIAerSal2987_0101.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1063.
HOGENOMHBG753318.
OMAMMRSGMS.
PhylomeDBA4SHB7.
ProtClustDBPRK05396.

Enzyme and pathway databases

BioCycASAL382245:ASA_0090-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_AERS4
AccessionPrimary (citable) accession number: A4SHB7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 15, 2007
Last modified: December 14, 2011
This is version 41 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