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Q65JE7 (TDH_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. 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:BLi01923, BL03658
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length346 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 – 346346L-threonine 3-dehydrogenase HAMAP MF_00627
PRO_0000160830

Sites

Metal binding421Zinc 1; catalytic By similarity
Metal binding671Zinc 1; catalytic By similarity
Metal binding971Zinc 2 By similarity
Metal binding1001Zinc 2 By similarity
Metal binding1031Zinc 2 By similarity
Metal binding1111Zinc 2 By similarity
Metal binding1521Zinc 1; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65JE7 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 80F6CC46AA96215F

FASTA34637,240
        10         20         30         40         50         60 
MDGNMKALIK KPGEPGASFE LVPIPKIDKH EVLIKVKAAS ICGTDVHIYN WDEWAKSRVK 

        70         80         90        100        110        120 
PPYVFGHEFS GEVVQVGENV TTVKEGEYVS AETHIVCGKC LPCLTGKEHV CKKTLILGVD 

       130        140        150        160        170        180 
TDGCFAEYVK MPAANIWKNP AGMPEDLASI QEPLGNAVHT VLTGMTAGVK VAVVGCGPIG 

       190        200        210        220        230        240 
LMAVAVAKAS GAAQVIAIDK NEYRLDLALQ MGATDIISVE KEDPLKNVSA LTNGEGADLV 

       250        260        270        280        290        300 
CEMSGHPTAI RQSLKMAANG GRVHVLSLPE HPVCIDMTND IVFKGLTVQG ITGRKMFETW 

       310        320        330        340 
RQVSGLLQSG TIQIKPVITH RFPMEEFEKG FELMRKGQCG KVVLIP 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000002 Genomic DNA. Translation: AAU23458.1.
AE017333 Genomic DNA. Translation: AAU40817.1.
RefSeqYP_079096.1. NC_006270.3.
YP_091510.1. NC_006322.1.

3D structure databases

ProteinModelPortalQ65JE7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65JE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000054394; EBBACP00000052925; EBBACG00000054385.
EBBACT00000060787; EBBACP00000059220; EBBACG00000060778.
GeneID3031140.
3099859.
GenomeReviewsGene locus BLi01923 in contig AE017333_GR.
Gene locus BL03658 in contig CP000002_GR.
KEGGbld:BLi01923.
bli:BL03658.
NMPDRfig|279010.5.peg.2626.
PATRIC18949453. VBIBacLic203714_1930.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1063.
GeneTreeEBGT00050000000383.
HOGENOMHBG753318.
OMAADLVCEM.
PhylomeDBQ65JE7.
ProtClustDBPRK05396.

Enzyme and pathway databases

BioCycBLIC279010-1:BLI01923-MONOMER.
BLIC279010:BL03658-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_BACLD
AccessionPrimary (citable) accession number: Q65JE7
Secondary accession number(s): Q62UV1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 64 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