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B1YXP0 (TDH_BURA4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:BamMC406_3116
OrganismBurkholderia ambifaria (strain MC40-6) [Complete proteome] [HAMAP]
Taxonomic identifier398577 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

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_1000130537

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
B1YXP0 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: D2EB85FDDC65C75C

FASTA34237,359
        10         20         30         40         50         60 
MKALAKLERG PGLTLTRVKR PEVGHNDVLI KIHRTAICGT DIHIWKWDDW AQKTIPVPMH 

        70         80         90        100        110        120 
VGHEYVGEIV EMGQEVRGFA IGDRVSGEGH ITCGFCRNCR AGRRHLCRNT VGVGVNREGA 

       130        140        150        160        170        180 
FAEYLAIPAF NAFKIPPEIS DDLASIFDPF GNATHTALSF NLVGEDVLIT GAGPIGVMAA 

       190        200        210        220        230        240 
AIAKHVGARN VVITDINDYR LELARKMGAT RAVNVSRESL RDVMADLHMT EGFDVGLEMS 

       250        260        270        280        290        300 
GVPSAFTSML EAMNHGGKVA LLGIPPAQTA IDWNQVIFKG LEIKGIYGRE MFETWYKMVA 

       310        320        330        340 
MLQSGLDLSP IITHRFAADD YEKGFAAMLS GESGKVILDW TV 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia ambifaria MC40-6."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A. expand/collapse author list , Ramette A., Konstantinidis K., Tiedje J., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC40-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001026 Genomic DNA. Translation: ACB65590.1.
RefSeqYP_001809806.1. NC_010552.1.

3D structure databases

ProteinModelPortalB1YXP0.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1YXP0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6181075.
GenomeReviewsGene locus BamMC406_3116 in contig CP001026_GR.
KEGGbac:BamMC406_3116.
PATRIC19035860. VBIBurAmb82852_3223.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG753318.
OMAMMRSGMS.
ProtClustDBPRK05396.

Enzyme and pathway databases

BioCycBAMB398577:BAMMC406_3116-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_BURA4
AccessionPrimary (citable) accession number: B1YXP0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 33 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