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UniProtKB - Q8K3F7 (TDH_MOUSE)

>sp|Q8K3F7|TDH_MOUSE L-threonine 3-dehydrogenase, mitochondrial OS=Mus musculus OX=10090 GN=Tdh PE=1 SV=1
MLFLGMLKQVVNGTAQSKASSCRKLVLPLKFLGTSQHRIPADANFHSTSISEAEPPRVLI
TGGLGQLGVGLANLLRKRFGKDNVILSDIRKPPAHVFHSGPFVYANILDYKSLREIVVNH
RISWLFHYSALLSAVGEANVSLARDVNITGLHNVLDVAAEYNVRLFVPSTIGAFGPTSPR
NPAPDLCIQRPRTIYGVSKVHTELMGEYYYYRYGLDFRCLRYPGIISADSQPGGGTTDYA
VQIFHAAAKNGTFECNLEAGTRLPMMYISDCLRATLEVMEAPAERLSMRTYNISAMSFTP
EELAQALRKHAPDFQITYCVDPLRQAIAESWPMILDDSNARKDWGWKHDFDLPELVATML
NFHGVSTRVAQVN

Entry version 127 (25 May 2022)
Sequence version 1 (01 Oct 2002)
Previous versions | rss

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Protein

L-threonine 3-dehydrogenase, mitochondrial

Gene

Tdh

Organism

Mus musculus (Mouse)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalyzes the NAD⁺-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate, mediating L-threonine catabolism.

1 Publication

Catalytic activityⁱ

L-threonine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
NAD⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
(2S)-2-amino-3-oxobutanoate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
NADH
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.4
  "Structural insights on mouse L-threonine dehydrogenase: A regulatory role of Arg180 in catalysis."
  He C., Huang X., Liu Y., Li F., Yang Y., Tao H., Han C., Zhao C., Xiao Y., Shi Y.
  J. Struct. Biol. 192:510-518(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 47-373 OF WILD-TYPE AND VARIANT LYS-180 IN COMPLEX WITH NAD, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF SER-133; ARG-180; THR-237 AND MET-333.
EC:
1.1.1.103
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.4
  "Structural insights on mouse L-threonine dehydrogenase: A regulatory role of Arg180 in catalysis."
  He C., Huang X., Liu Y., Li F., Yang Y., Tao H., Han C., Zhao C., Xiao Y., Shi Y.
  J. Struct. Biol. 192:510-518(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 47-373 OF WILD-TYPE AND VARIANT LYS-180 IN COMPLEX WITH NAD, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF SER-133; ARG-180; THR-237 AND MET-333.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
L-threonine
zoom
+
NAD⁺
zoom
=
(2S)-2-amino-3-oxobutanoate
zoom
+
H⁺
+
NADH

Kineticsⁱ

Pathwayⁱ: L-threonine degradation via oxydo-reductase pathway

This protein is involved in step 1 of the subpathway that synthesizes glycine from L-threonine.1 Publication 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 key	Position(s)	DescriptionActions	Length
Active siteⁱ	195	Proton donor/acceptor1 Publication	1
Binding siteⁱ	195	NADCombined sources1 Publication	1
Binding siteⁱ	199	NADCombined sources1 Publication	1
Binding siteⁱ	225	NAD; via amide nitrogenCombined sources1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	62 – 67	NAD bindingCombined sources1 Publication	6
Nucleotide bindingⁱ	88 – 90	NAD bindingCombined sources1 Publication	3
Nucleotide bindingⁱ	106 – 107	NAD bindingCombined sources1 Publication	2

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Ligand	NAD

Enzyme and pathway databases

BRENDAⁱ	1.1.1.103, 3474
UniPathwayⁱ	UPA00046;UER00505

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: L-threonine 3-dehydrogenase, mitochondrialCurated (EC:1.1.1.1031 Publication)
Gene namesⁱ	Name:TdhImported
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 14

Organism-specific databases

MGIⁱ	MGI:1926231, Tdh
VEuPathDBⁱ	HostDB:ENSMUSG00000021953

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	133	S → A: Decreased L-threonine 3-dehydrogenase activity. 1 Publication	1
Mutagenesisⁱ	180	R → K: Decreased L-threonine 3-dehydrogenase activity. No effect on protein NAD(+)-binding. No gross effect on protein folding. No effect on protein stability. 1 Publication	1
Mutagenesisⁱ	237	T → A: Decreased L-threonine 3-dehydrogenase activity. 1 Publication	1
Mutagenesisⁱ	333	M → A: Decreased L-threonine 3-dehydrogenase activity. 1 Publication	1
Mutagenesisⁱ	333	M → E: Decreased L-threonine 3-dehydrogenase activity. Decreased affinity for L-threonine. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – ?	MitochondrionSequence analysis
ChainⁱPRO_0000298784	? – 373	L-threonine 3-dehydrogenase, mitochondrial

Proteomic databases

PaxDbⁱ	Q8K3F7
PeptideAtlas More...PeptideAtlasⁱ	Q8K3F7
PRIDEⁱ	Q8K3F7
ProteomicsDBⁱ	262738

PTM databases

iPTMnetⁱ	Q8K3F7
PhosphoSitePlusⁱ	Q8K3F7

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSMUSG00000021953, Expressed in yolk sac and 65 other tissues
ExpressionAtlasⁱ	Q8K3F7, baseline and differential
Genevisibleⁱ	Q8K3F7, MM

Interactionⁱ

Subunit structureⁱ

Homodimer.

1 Publication

GO - Molecular functionⁱ

identical protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- Ref.4
  "Structural insights on mouse L-threonine dehydrogenase: A regulatory role of Arg180 in catalysis."
  He C., Huang X., Liu Y., Li F., Yang Y., Tao H., Han C., Zhao C., Xiao Y., Shi Y.
  J. Struct. Biol. 192:510-518(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 47-373 OF WILD-TYPE AND VARIANT LYS-180 IN COMPLEX WITH NAD, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF SER-133; ARG-180; THR-237 AND MET-333.

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	208451, 4 interactors
STRINGⁱ	10090.ENSMUSP00000022522

Miscellaneous databases

RNActⁱ	Q8K3F7, protein

RNActⁱ

Q8K3F7, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	58 – 61	Combined sources	4
Turnⁱ	62 – 64	Combined sources	3
Helixⁱ	66 – 79	Combined sources	14
Helixⁱ	81 – 83	Combined sources	3
Beta strandⁱ	84 – 88	Combined sources	5
Helixⁱ	94 – 97	Combined sources	4
Beta strandⁱ	102 – 104	Combined sources	3
Helixⁱ	110 – 119	Combined sources	10
Beta strandⁱ	124 – 127	Combined sources	4
Helixⁱ	133 – 138	Combined sources	6
Helixⁱ	146 – 160	Combined sources	15
Beta strandⁱ	164 – 166	Combined sources	3
Helixⁱ	171 – 173	Combined sources	3
Beta strandⁱ	181 – 183	Combined sources	3
Beta strandⁱ	185 – 187	Combined sources	3
Helixⁱ	194 – 212	Combined sources	19
Beta strandⁱ	217 – 222	Combined sources	6
Beta strandⁱ	224 – 226	Combined sources	3
Helixⁱ	236 – 238	Combined sources	3
Helixⁱ	239 – 248	Combined sources	10
Beta strandⁱ	252 – 257	Combined sources	6
Beta strandⁱ	263 – 267	Combined sources	5
Helixⁱ	268 – 280	Combined sources	13
Helixⁱ	283 – 285	Combined sources	3
Beta strandⁱ	289 – 292	Combined sources	4
Beta strandⁱ	295 – 298	Combined sources	4
Helixⁱ	300 – 308	Combined sources	9
Beta strandⁱ	315 – 318	Combined sources	4
Helixⁱ	322 – 330	Combined sources	9
Helixⁱ	338 – 344	Combined sources	7
Helixⁱ	352 – 362	Combined sources	11

Show more details

3D structure databases

AlphaFoldDBⁱ	Q8K3F7
SMRⁱ	Q8K3F7
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the NAD(P)-dependent epimerase/dehydratase family.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG2774, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000014037
HOGENOMⁱ	CLU_007383_19_1_1
InParanoidⁱ	Q8K3F7
OMAⁱ	HWHASPR
Database of Orthologous Groups More...OrthoDBⁱ	1327602at2759
PhylomeDBⁱ	Q8K3F7
TreeFamⁱ	TF314544

Family and domain databases

InterProⁱ	View protein in InterPro IPR001509, Epimerase_deHydtase IPR036291, NAD(P)-bd_dom_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01370, Epimerase, 1 hit
SUPFAMⁱ	SSF51735, SSF51735, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

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

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show all Align All

Q8K3F7-1 [UniParc]FASTA Add 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

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

F6X7T7	F6X7T7_MOUSE	L-threonine 3-dehydrogenase, mitoch... L-threonine 3-dehydrogenase, mitochondrial	Tdh	219	Annotation score:
F6Y7H0	F6Y7H0_MOUSE	L-threonine 3-dehydrogenase, mitoch... L-threonine 3-dehydrogenase, mitochondrial	Tdh	191	Annotation score:
F7AJL7	F7AJL7_MOUSE	L-threonine 3-dehydrogenase, mitoch... L-threonine 3-dehydrogenase, mitochondrial	Tdh	169	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	82	D → N in AAH58860 (PubMed:15489334).Curated	1
Sequence conflictⁱ	214	G → V in AAF61395 (PubMed:12097150).Curated	1
Sequence conflictⁱ	232	P → R in AAF61395 (PubMed:12097150).Curated	1
Sequence conflictⁱ	318	Y → H in AAH58860 (PubMed:15489334).Curated	1
Sequence conflictⁱ	361	N → S in AAF61395 (PubMed:12097150).Curated	1

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS27202.1
NCBI Reference Sequences More...RefSeqⁱ	NP_067455.5, NM_021480.5

Genome annotation databases

Ensemblⁱ	ENSMUST00000022522; ENSMUSP00000022522; ENSMUSG00000021953
GeneIDⁱ	58865
KEGGⁱ	mmu:58865
UCSC genome browser More...UCSCⁱ	uc007uhs.1, mouse

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q8K3F7	L-threonine dehydrogenase		MUSSI		373	UniRef90_Q8K3F7
L-threonine 3-dehydrogenase, mitochondrial		MUSCR		373
+5

Protein	Similar proteins		Species	Score	Length	Source
Q8K3F7	L-threonine 3-dehydrogenase, mitochondrial		BOVIN		373	UniRef50_Q8K3F7
L-threonine dehydrogenase		MUSSI		373
L-threonine 3-dehydrogenase, mitochondrial		MUSCR		373
L-threonine 3-dehydrogenase, mitochondrial-like isoform X2		GEOSA		373
L-threonine 3-dehydrogenase, mitochondrial-like		Microcaecilia unicolor		373
+579

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
CCDSⁱ	CCDS27202.1
RefSeqⁱ	NP_067455.5, NM_021480.5

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4YR9	X-ray	2.80	A/B/C/D/E/F	47-373	[»]
	4YRA	X-ray	2.65	A/B/C/D/E/F/G/H/I/J/K/L	47-373	[»]
	4YRB	X-ray	3.25	A/B/C/D/E/F	47-373	[»]
AlphaFoldDBⁱ	Q8K3F7
SMRⁱ	Q8K3F7
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	208451, 4 interactors
STRINGⁱ	10090.ENSMUSP00000022522

PTM databases

iPTMnetⁱ	Q8K3F7
PhosphoSitePlusⁱ	Q8K3F7

Proteomic databases

PaxDbⁱ	Q8K3F7
PeptideAtlasⁱ	Q8K3F7
PRIDEⁱ	Q8K3F7
ProteomicsDBⁱ	262738

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	58865

DNASUⁱ

58865

Genome annotation databases

Ensemblⁱ	ENSMUST00000022522; ENSMUSP00000022522; ENSMUSG00000021953
GeneIDⁱ	58865
KEGGⁱ	mmu:58865
UCSCⁱ	uc007uhs.1, mouse

Organism-specific databases

CTDⁱ	157739
MGIⁱ	MGI:1926231, Tdh
VEuPathDBⁱ	HostDB:ENSMUSG00000021953

Phylogenomic databases

eggNOGⁱ	KOG2774, Eukaryota
GeneTreeⁱ	ENSGT00390000014037
HOGENOMⁱ	CLU_007383_19_1_1
InParanoidⁱ	Q8K3F7
OMAⁱ	HWHASPR
OrthoDBⁱ	1327602at2759
PhylomeDBⁱ	Q8K3F7
TreeFamⁱ	TF314544

Enzyme and pathway databases

UniPathwayⁱ	UPA00046;UER00505
BRENDAⁱ	1.1.1.103, 3474

Miscellaneous databases

BioGRID-ORCSⁱ	58865, 2 hits in 70 CRISPR screens
ChiTaRSⁱ	Tdh, mouse
Protein Ontology More...PROⁱ	PR:Q8K3F7
RNActⁱ	Q8K3F7, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000021953, Expressed in yolk sac and 65 other tissues
ExpressionAtlasⁱ	Q8K3F7, baseline and differential
Genevisibleⁱ	Q8K3F7, MM

Family and domain databases

InterProⁱ	View protein in InterPro IPR001509, Epimerase_deHydtase IPR036291, NAD(P)-bd_dom_sf
Pfamⁱ	View protein in Pfam PF01370, Epimerase, 1 hit
SUPFAMⁱ	SSF51735, SSF51735, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TDH_MOUSE
Accessionⁱ	Q8K3F7Primary (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:	May 25, 2022
	This is version 127 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q8K3F7 (TDH_MOUSE)

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L-threonine 3-dehydrogenase, mitochondrial

Tdh

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-threonine degradation via oxydo-reductase pathway

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Mitochondrion

Mitochondrion

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

Pathwayⁱ: L-threonine degradation via oxydo-reductase pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ