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Q8K3F7 (TDH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

General annotation (Comments)

Catalytic activity

L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH. UniProtKB Q8MIR0

Pathway

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

Subcellular location

Mitochondrion By similarity UniProtKB Q8MIR0.

Sequence similarities

Belongs to the sugar epimerase family.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

   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 Potential UniProtKB Q8MIR0
Chain? – 373L-threonine 3-dehydrogenase, mitochondrialPRO_0000298784

Regions

Nucleotide binding9 – 4638NAD By similarity UniProtKB Q8R059

Sites

Active site1951Proton acceptor By similarity UniProtKB Q8R059

Experimental info

Sequence conflict821D → N in AAH58860. Ref.3
Sequence conflict2141G → V in AAF61395. Ref.1
Sequence conflict2321P → R in AAF61395. Ref.1
Sequence conflict3181Y → H in AAH58860. Ref.3
Sequence conflict3611N → S in AAF61395. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8K3F7 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 6A416A079A7EC381

FASTA37341,462
        10         20         30         40         50         60 
MLFLGMLKQV VNGTAQSKAS SCRKLVLPLK FLGTSQHRIP ADANFHSTSI SEAEPPRVLI 

        70         80         90        100        110        120 
TGGLGQLGVG LANLLRKRFG KDNVILSDIR KPPAHVFHSG PFVYANILDY KSLREIVVNH 

       130        140        150        160        170        180 
RISWLFHYSA LLSAVGEANV SLARDVNITG LHNVLDVAAE YNVRLFVPST IGAFGPTSPR 

       190        200        210        220        230        240 
NPAPDLCIQR PRTIYGVSKV HTELMGEYYY YRYGLDFRCL RYPGIISADS QPGGGTTDYA 

       250        260        270        280        290        300 
VQIFHAAAKN GTFECNLEAG TRLPMMYISD CLRATLEVME APAERLSMRT YNISAMSFTP 

       310        320        330        340        350        360 
EELAQALRKH APDFQITYCV DPLRQAIAES WPMILDDSNA RKDWGWKHDF DLPELVATML 

       370 
NFHGVSTRVA QVN 

« Hide

References

« Hide 'large scale' 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].
Strain: BALB/c.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF134346 mRNA. Translation: AAF61395.2.
AY116662 mRNA. Translation: AAM51557.1.
AK077571 mRNA. Translation: BAC36870.1.
BC058860 mRNA. Translation: AAH58860.1.
IPIIPI00331660.
RefSeqNP_067455.5. NM_021480.5.
UniGeneMm.354229.

3D structure databases

ProteinModelPortalQ8K3F7.
SMRQ8K3F7. Positions 55-363.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8K3F7.

Proteomic databases

PRIDEQ8K3F7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022522; ENSMUSP00000022522; ENSMUSG00000021953.
GeneID58865.
KEGGmmu:58865.
UCSCuc007uhs.1. mouse.

Organism-specific databases

CTD157739.
MGIMGI:1926231. Tdh.

Phylogenomic databases

eggNOGroNOG14653.
GeneTreeENSGT00390000014037.
HOGENOMHBG304215.
HOVERGENHBG062086.
InParanoidQ8K3F7.
OMAFRCLRFP.
OrthoDBEOG4B2SXX.
PhylomeDBQ8K3F7.

Enzyme and pathway databases

BRENDA1.1.1.103. 3474.

Gene expression databases

ArrayExpressQ8K3F7.
BgeeQ8K3F7.
CleanExMM_TDH.
GenevestigatorQ8K3F7.

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...

Other

NextBio314424.
SOURCESearch...

Entry information

Entry nameTDH_MOUSE
AccessionPrimary (citable) accession number: Q8K3F7
Secondary accession number(s): Q6PD91, Q9JLU3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: October 1, 2002
Last modified: December 14, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families