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Reviewed, UniProtKB/Swiss-Prot Q0B5Q1 (TDH_BURCM)

Last modified February 9, 2010. Version 33. 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: Bamb_4973
OrganismBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]
Taxonomic identifier339670 [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 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 – 342342L-threonine 3-dehydrogenase HAMAP MF_00627
PRO_1000051619

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
Q0B5Q1-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 2C0485EBA6D90126

FASTA34237,373
        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 EAMNHGGKIA LLGIPPAQTA IDWNQVIFKG LEIKGIYGRE MFETWYKMVA 

       310        320        330        340 
MLQSGLDLSP IITHRFAADD YEKGFAAMLS GESGKVILDW TV 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia cepacia AMMD."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000441 Genomic DNA. Translation: ABI90522.1.
RefSeqYP_776856.1.

3D structure databases

SMRQ0B5Q1. Positions 1-339.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0B5Q1.

Genome annotation databases

GeneID4313864.
GenomeReviewsGene locus Bamb_4973 in contig CP000441_GR.
KEGGbam:Bamb_4973.
NMPDRfig|339670.3.peg.1717.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1063.
HOGENOMHBG753318.
OMAMVDAPKP.

Family and domain databases

HAMAPMF_00627. Thr_dehydrog.
[Tree]
InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR004627. L-Threonine_3-DHase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR00692. tdh. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTDH_BURCM
AccessionPrimary (citable) accession number: Q0B5Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: February 9, 2010
This is version 33 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