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A8FPE0 (TDH_SHESH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 38. 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:Ssed_0100
OrganismShewanella sediminis (strain HAW-EB3) [Complete proteome] [HAMAP]
Taxonomic identifier425104 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length341 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 – 341341L-threonine 3-dehydrogenase HAMAP MF_00627
PRO_1000082618

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
A8FPE0 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: E45E4D77D30DA450

FASTA34137,266
        10         20         30         40         50         60 
MKALSKLKPE EGIWMVDAPK PEMGHNDLLI KIRKTAICGT DIHIYNWDEW SQKTIPVPMV 

        70         80         90        100        110        120 
VGHEYVGEVI DMGIEVRGFD VGDRVSGEGH ITCGHCRNCR GGRTHLCRNT SGVGVNRDGA 

       130        140        150        160        170        180 
FAEYLVIPAF NAFKIPDDIS DDLASIFDPF GNAVHTALSF DLVGEDVLIT GAGPIGIMAA 

       190        200        210        220        230        240 
AVCRHVGARH VVITDVNEYR LELANKMGAT RAVNVAKESL EGVMEELGMT EGFDVGLEMS 

       250        260        270        280        290        300 
GVPSAFHSML DTMNHGGKIA MLGIPGGEMA IDWSKVIFKG LILKGIYGRE MFETWYKMAS 

       310        320        330        340 
LIQSGLDISP IITHHFKIDD FQQGFDAMRS GQSGKVILNW D 

« Hide

References

[1]"Complete sequence of Shewanella sediminis HAW-EB3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Zhao J.-S., Richardson P.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAW-EB3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000821 Genomic DNA. Translation: ABV34713.1.
RefSeqYP_001471841.1. NC_009831.1.

3D structure databases

ProteinModelPortalA8FPE0.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8FPE0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5612913.
GenomeReviewsGene locus Ssed_0100 in contig CP000821_GR.
KEGGsse:Ssed_0100.
NMPDRfig|425104.3.peg.91.
PATRIC23557340. VBISheSed62411_0105.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1063.
HOGENOMHBG753318.
OMAMMRSGMS.
ProtClustDBPRK05396.

Enzyme and pathway databases

BioCycSSED425104:SSED_0100-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_SHESH
AccessionPrimary (citable) accession number: A8FPE0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: January 25, 2012
This is version 38 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