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Protein

L-threonine 3-dehydrogenase, mitochondrial

Gene

Tdh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: L-threonine degradation via oxydo-reductase pathway

This protein is involved in step 1 of the subpathway that synthesizes glycine from L-threonine.Curated
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. L-threonine 3-dehydrogenase, mitochondrial (Tdh)
  2. 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial (Gcat)
This subpathway is part of the pathway L-threonine degradation via oxydo-reductase pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycine from L-threonine, the pathway L-threonine degradation via oxydo-reductase pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei195 – 1951Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 4638NADBy similarityAdd
BLAST

GO - Molecular functioni

  • coenzyme binding Source: InterPro
  • L-threonine 3-dehydrogenase activity Source: MGI

GO - Biological processi

  • L-threonine catabolic process to glycine Source: UniProtKB-UniPathway
  • threonine catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.1.1.103. 3474.
UniPathwayiUPA00046; UER00505.

Names & Taxonomyi

Protein namesi
Recommended name:
L-threonine 3-dehydrogenase, mitochondrial (EC:1.1.1.103)
Gene namesi
Name:TdhImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1926231. Tdh.

Subcellular locationi

  • Mitochondrion By similarity

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 373L-threonine 3-dehydrogenase, mitochondrialPRO_0000298784
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

PaxDbiQ8K3F7.
PRIDEiQ8K3F7.

PTM databases

iPTMnetiQ8K3F7.

Expressioni

Gene expression databases

BgeeiQ8K3F7.
CleanExiMM_TDH.
ExpressionAtlasiQ8K3F7. baseline and differential.
GenevisibleiQ8K3F7. MM.

Interactioni

Protein-protein interaction databases

BioGridi208451. 2 interactions.
STRINGi10090.ENSMUSP00000022522.

Structurei

Secondary structure

1
373
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi58 – 614Combined sources
Turni62 – 643Combined sources
Helixi66 – 7914Combined sources
Helixi81 – 833Combined sources
Beta strandi84 – 885Combined sources
Helixi94 – 974Combined sources
Beta strandi102 – 1043Combined sources
Helixi110 – 11910Combined sources
Beta strandi124 – 1274Combined sources
Helixi133 – 1386Combined sources
Helixi146 – 16015Combined sources
Beta strandi164 – 1663Combined sources
Helixi171 – 1733Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi185 – 1873Combined sources
Helixi194 – 21219Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi224 – 2263Combined sources
Helixi236 – 2383Combined sources
Helixi239 – 24810Combined sources
Beta strandi252 – 2576Combined sources
Beta strandi263 – 2675Combined sources
Helixi268 – 28013Combined sources
Helixi283 – 2853Combined sources
Beta strandi289 – 2924Combined sources
Beta strandi295 – 2984Combined sources
Helixi300 – 3089Combined sources
Beta strandi315 – 3184Combined sources
Helixi322 – 3309Combined sources
Helixi338 – 3447Combined sources
Helixi352 – 36211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YR9X-ray2.80A/B/C/D/E/F47-373[»]
4YRAX-ray2.65A/B/C/D/E/F/G/H/I/J/K/L47-373[»]
4YRBX-ray3.25A/B/C/D/E/F47-373[»]
ProteinModelPortaliQ8K3F7.
SMRiQ8K3F7. Positions 56-360.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2774. Eukaryota.
COG0451. LUCA.
GeneTreeiENSGT00390000014037.
HOGENOMiHOG000034276.
HOVERGENiHBG062086.
InParanoidiQ8K3F7.
KOiK15789.
OMAiVFWPSSI.
OrthoDBiEOG74J98K.
PhylomeDBiQ8K3F7.
TreeFamiTF314544.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR001509. Epimerase_deHydtase_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8K3F7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFLGMLKQV VNGTAQSKAS SCRKLVLPLK FLGTSQHRIP ADANFHSTSI
60 70 80 90 100
SEAEPPRVLI TGGLGQLGVG LANLLRKRFG KDNVILSDIR KPPAHVFHSG
110 120 130 140 150
PFVYANILDY KSLREIVVNH RISWLFHYSA LLSAVGEANV SLARDVNITG
160 170 180 190 200
LHNVLDVAAE YNVRLFVPST IGAFGPTSPR NPAPDLCIQR PRTIYGVSKV
210 220 230 240 250
HTELMGEYYY YRYGLDFRCL RYPGIISADS QPGGGTTDYA VQIFHAAAKN
260 270 280 290 300
GTFECNLEAG TRLPMMYISD CLRATLEVME APAERLSMRT YNISAMSFTP
310 320 330 340 350
EELAQALRKH APDFQITYCV DPLRQAIAES WPMILDDSNA RKDWGWKHDF
360 370
DLPELVATML NFHGVSTRVA QVN
Length:373
Mass (Da):41,462
Last modified:October 1, 2002 - v1
Checksum:i6A416A079A7EC381
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821D → N in AAH58860 (PubMed:15489334).Curated
Sequence conflicti214 – 2141G → V in AAF61395 (PubMed:12097150).Curated
Sequence conflicti232 – 2321P → R in AAF61395 (PubMed:12097150).Curated
Sequence conflicti318 – 3181Y → H in AAH58860 (PubMed:15489334).Curated
Sequence conflicti361 – 3611N → S in AAF61395 (PubMed:12097150).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF134346 mRNA. Translation: AAF61395.2.
AY116662 mRNA. Translation: AAM51557.1.
AK077571 mRNA. Translation: BAC36870.1.
BC058860 mRNA. Translation: AAH58860.1.
CCDSiCCDS27202.1.
RefSeqiNP_067455.5. NM_021480.5.
UniGeneiMm.354229.

Genome annotation databases

EnsembliENSMUST00000022522; ENSMUSP00000022522; ENSMUSG00000021953.
GeneIDi58865.
KEGGimmu:58865.
UCSCiuc007uhs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF134346 mRNA. Translation: AAF61395.2.
AY116662 mRNA. Translation: AAM51557.1.
AK077571 mRNA. Translation: BAC36870.1.
BC058860 mRNA. Translation: AAH58860.1.
CCDSiCCDS27202.1.
RefSeqiNP_067455.5. NM_021480.5.
UniGeneiMm.354229.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YR9X-ray2.80A/B/C/D/E/F47-373[»]
4YRAX-ray2.65A/B/C/D/E/F/G/H/I/J/K/L47-373[»]
4YRBX-ray3.25A/B/C/D/E/F47-373[»]
ProteinModelPortaliQ8K3F7.
SMRiQ8K3F7. Positions 56-360.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208451. 2 interactions.
STRINGi10090.ENSMUSP00000022522.

PTM databases

iPTMnetiQ8K3F7.

Proteomic databases

PaxDbiQ8K3F7.
PRIDEiQ8K3F7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022522; ENSMUSP00000022522; ENSMUSG00000021953.
GeneIDi58865.
KEGGimmu:58865.
UCSCiuc007uhs.1. mouse.

Organism-specific databases

CTDi157739.
MGIiMGI:1926231. Tdh.

Phylogenomic databases

eggNOGiKOG2774. Eukaryota.
COG0451. LUCA.
GeneTreeiENSGT00390000014037.
HOGENOMiHOG000034276.
HOVERGENiHBG062086.
InParanoidiQ8K3F7.
KOiK15789.
OMAiVFWPSSI.
OrthoDBiEOG74J98K.
PhylomeDBiQ8K3F7.
TreeFamiTF314544.

Enzyme and pathway databases

UniPathwayiUPA00046; UER00505.
BRENDAi1.1.1.103. 3474.

Miscellaneous databases

PROiQ8K3F7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K3F7.
CleanExiMM_TDH.
ExpressionAtlasiQ8K3F7. baseline and differential.
GenevisibleiQ8K3F7. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR001509. Epimerase_deHydtase_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and tissue distribution of mammalian L-threonine 3-dehydrogenases."
    Edgar A.J.
    BMC Biochem. 3:19-19(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJImported.
    Tissue: LiverImported.
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported.
    Tissue: EmbryoImported.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported.
    Tissue: EmbryoImported.

Entry informationi

Entry nameiTDH_MOUSE
AccessioniPrimary (citable) accession number: Q8K3F7
Secondary accession number(s): Q6PD91, Q9JLU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.