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Q6MD15 (TDH_PARUW) 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:pc0810
OrganismProtochlamydia amoebophila (strain UWE25) [Complete proteome] [HAMAP]
Taxonomic identifier264201 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesParachlamydiaceaeCandidatus Protochlamydia

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_0000160846

Sites

Metal binding391Zinc 1; catalytic By similarity
Metal binding641Zinc 1; catalytic By similarity
Metal binding941Zinc 2 By similarity
Metal binding971Zinc 2 By similarity
Metal binding1001Zinc 2 By similarity
Metal binding1081Zinc 2 By similarity
Metal binding1491Zinc 1; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6MD15 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 58991DDAE45E1449

FASTA34237,546
        10         20         30         40         50         60 
MKGLVKKISA PGLWMENLPI PSHVKDDEVL IKTIKTSICG TDVHIYKWDA WAQKNVPVPL 

        70         80         90        100        110        120 
VIGHEFIGEI AEFGKNVKGF KIGERVCGEG HIVCNQCPNC RMGRKHVCMH TKGLGYHISG 

       130        140        150        160        170        180 
CFAEYFVLPA ENVFSLPPSI SDDLGAIFDP YGNAVHTTLA FNLIGEDVLI TGAGPIGIMA 

       190        200        210        220        230        240 
AAIAKQAGAR HIVITDVNDY RLDLARTMGV SHAINVNRES LDNFMQSLGI KYGFTVGLEM 

       250        260        270        280        290        300 
SGHPDGLKTL TEKIRHGGNI ALLGILPPAT SIDWNLVIFK MLTLKGIYGR EIFSTWYQMV 

       310        320        330        340 
HLLEIGLNLA PIITHHFSVD NFEKGFEVML SGQSGKVILD WV 

« Hide

References

[1]"Illuminating the evolutionary history of chlamydiae."
Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T., Mewes H.-W., Wagner M.
Science 304:728-730(2004) [PubMed: 15073324] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UWE25.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX908798 Genomic DNA. Translation: CAF23534.1.
RefSeqYP_007809.1. NC_005861.1.

3D structure databases

ProteinModelPortalQ6MD15.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6MD15.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2781402.
GenomeReviewsGene locus pc0810 in contig BX908798_GR.
KEGGpcu:pc0810.
NMPDRfig|264201.1.peg.810.
PATRIC31996954. VBICanPro72727_0821.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1063.
HOGENOMHBG753318.
OMAGRCRNCL.
PhylomeDBQ6MD15.
ProtClustDBPRK05396.

Enzyme and pathway databases

BioCycCPRO264201:PC0810-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_PARUW
AccessionPrimary (citable) accession number: Q6MD15
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 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