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Q8MIR0 (TDH_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. 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, mitochondrial

EC=1.1.1.103
Gene names
Name:TDH
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH. Ref.2

Pathway

Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2.

Subcellular location

Mitochondrion Ref.2.

Sequence similarities

Belongs to the sugar epimerase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processcellular metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-threonine 3-dehydrogenase activity

Inferred from electronic annotation. Source: EC

coenzyme binding

Inferred from electronic annotation. Source: InterPro

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion
Chain? – 373L-threonine 3-dehydrogenase, mitochondrialPRO_0000298785

Regions

Nucleotide binding9 – 4638NAD By similarity UniProtKB Q8R059

Sites

Active site1951Proton acceptor By similarity UniProtKB Q8R059

Experimental info

Sequence conflict651G → Q AA sequence Ref.2
Sequence conflict3091K → R AA sequence Ref.2
Sequence conflict3311W → I AA sequence Ref.2
Sequence conflict3411R → A AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8MIR0 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 6F3CCB6879E66480

FASTA37341,432
        10         20         30         40         50         60 
MPVVKMLKQV ASRTLGSPAC GCQPPTLPRR FLGTSPRQIP ADANFHSTSF SEANQPRVLI 

        70         80         90        100        110        120 
TGGLGQLGVG LASLLRKRFG KDNVILSDIR KPPEHVFLSG PFIYSDILDY KNLREIVVNN 

       130        140        150        160        170        180 
RVTWLFHYSA LLSAVGEANV SLARAVNITG LHNVLDVAAE HGLRLFVPST IGAFGPTSPR 

       190        200        210        220        230        240 
NPTPDLCIQR PRTIYGVSKV HAELMGEYYY YRYGLDFRCL RYPGIISADS QPGGGTTDYA 

       250        260        270        280        290        300 
VQIFQDAVKN GRFECNLNPG TKLPMMYIDD CLRATLEVME APAEALSLRT YNVNAMSFTP 

       310        320        330        340        350        360 
AELAQEVLKH IPEFQITYNV DSVRQAIADS WPMNFDDSTA RRDWGWKHDF DLPELVTTML 

       370 
NFHGAHSRVA QAN 

« Hide

References

[1]"Molecular cloning and tissue distribution of mammalian L-threonine 3-dehydrogenases."
Edgar A.J.
BMC Biochem. 3:19-19(2002) [PubMed: 12097150] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Purification and structural characterization of porcine L-threonine dehydrogenase."
Kao Y.-C., Davis L.
Protein Expr. Purif. 5:423-431(1994) [PubMed: 7827500] [Abstract]
Cited for: PROTEIN SEQUENCE OF 51-111; 145-180; 200-218; 222-249 AND 274-342, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY095535 mRNA. Translation: AAM18208.1.
RefSeqNP_999169.1. NM_214004.1.
UniGeneSsc.51.

3D structure databases

ProteinModelPortalQ8MIR0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397065.
KEGGssc:397065.

Organism-specific databases

CTD157739.

Phylogenomic databases

HOVERGENHBG062086.

Enzyme and pathway databases

BRENDA1.1.1.103. 6170.

Family and domain databases

InterProIPR001509. Epimerase_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00060.
PfamPF01370. Epimerase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTDH_PIG
AccessionPrimary (citable) accession number: Q8MIR0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: October 1, 2002
Last modified: December 14, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families