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P09367 (SDHL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 134. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-serine dehydratase/L-threonine deaminase

Short name=SDH
EC=4.3.1.17
Alternative name(s):
L-serine deaminase
L-threonine dehydratase
Short name=TDH
EC=4.3.1.19
Gene names
Name:Sds
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length363 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-serine = pyruvate + NH3.

L-threonine = 2-oxobutanoate + NH3.

Cofactor

Pyridoxal phosphate.

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Induction

By glucocorticoids and glucagon.

Sequence similarities

Belongs to the serine/threonine dehydratase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P09367-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P09367-2)

The sequence of this isoform differs from the canonical sequence as follows:
     65-100: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6
Chain2 – 363362L-serine dehydratase/L-threonine deaminase
PRO_0000185596

Amino acid modifications

Modified residue21N-acetylalanine Ref.6
Modified residue411N6-(pyridoxal phosphate)lysine

Natural variations

Alternative sequence65 – 10036Missing in isoform 2.
VSP_024798

Experimental info

Sequence conflict121P → T AA sequence Ref.5
Sequence conflict161S → T in AAA42123. Ref.1
Sequence conflict1641P → Q in AAA42123. Ref.1
Sequence conflict2761P → T AA sequence Ref.5
Sequence conflict3251G → A in CAA68721. Ref.3

Secondary structure

........................................................ 363
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C94FFF2EB9C6E33C

FASTA36338,433
        10         20         30         40         50         60 
MAAQESLHVK TPLRDSMALS KVAGTSVFLK MDSSQPSGSF KIRGIGHLCK MKAKQGCKHF 

        70         80         90        100        110        120 
VCSSVVQIWG SRMRGRSHSG DEQPHVRSQA LLPDTPSPLT AGNAGMATAY AARRLGLPAT 

       130        140        150        160        170        180 
IVVPSTTPAL TIERLKNEGA TVEVVGEMLD EAIQLAKALE KNNPGWVYIS PFDDPLIWEG 

       190        200        210        220        230        240 
HTSLVKELKE TLSAKPGAIV LSVGGGGLLC GVVQGLREVG WEDVPIIAME TFGAHSFHAA 

       250        260        270        280        290        300 
VKEGKLVTLP KITSVAKALG VNTVGAQTLK LFYEHPIFSE VISDQEAVTA IEKFVDDEKI 

       310        320        330        340        350        360 
LVEPACGAAL AAVYSGVVCR LQAEGRLQTP LASLVVIVCG GSNISLAQLQ ALKAQLGLNE 


LLK 

« Hide

Isoform 2 [UniParc].

Checksum: 525C043E62BDF388
Show »

FASTA32734,454

References

« Hide 'large scale' references
[1]"Isolation and nucleotide sequence of the cDNA for rat liver serine dehydratase mRNA and structures of the 5' and 3' flanking regions of the serine dehydratase gene."
Ogawa H., Miller D.A., Dunn T., Su Y., Burcham J.M., Peraino C., Fujioka M., Babcock K., Pitot H.C.
Proc. Natl. Acad. Sci. U.S.A. 85:5809-5813(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Sequence of the rat serine dehydratase gene."
Ogawa H., Su Y., Dunn T., Miller D.A., Matsuda Y., Fujioka M., Pitot H.C.
Nucleic Acids Res. 16:10921-10923(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Primary structure of rat liver serine dehydratase deduced from the cDNA sequence."
Noda C., Ito K., Nakamura T., Ichihara A.
FEBS Lett. 234:331-335(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Liver.
[4]"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] (ISOFORM 2).
Tissue: Liver.
[5]"Primary structure of rat liver L-threonine deaminase."
Leoncini R., Henschen A., Krieglstein K., Calvete J.J., Pagani R., Marinello E.
Ital. J. Biochem. 39:228-234(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-363 (ISOFORM 2).
Strain: Wistar.
Tissue: Liver.
[6]"The peptide sequences near the bound pyridoxal phosphate are conserved in serine dehydratase from rat liver, and threonine dehydratases from yeast and Escherichia coli."
Ogawa H., Konishi K., Fujioka M.
Biochim. Biophys. Acta 996:139-141(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-5 AND 31-50, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PYRIDOXAL PHOSPHATE AT LYS-41.
Tissue: Liver.
[7]"Amino acid sequence around the pyridoxal 5'-phosphate binding site of rat liver L-threonine deaminase."
Leoncini R., Henschen A., Krieglstein K., Calvete J.J., Pagani R., Marinello E.
Ital. J. Biochem. 39:235-241(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PYRIDOXAL PHOSPHATE AT LYS-41.
[8]"Properties of rat liver L-threonine deaminase."
Pagani R., Leoncini R., Pizzichini M., Vannoni D., Tabucci A., Marinello E.
Enzyme Protein 48:90-97(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Liver.
[9]"Crystal structure of serine dehydratase from rat liver."
Yamada T., Komoto J., Takata Y., Ogawa H., Pitot H.C., Takusagawa F.
Biochemistry 42:12854-12865(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03863 mRNA. Translation: AAA42123.1.
X13119 Genomic DNA. Translation: CAA31511.1.
Y00752 mRNA. Translation: CAA68721.1.
BC088110 mRNA. Translation: AAH88110.1.
PIRDWRTT. S01009.
S01973.
RefSeqNP_446414.3. NM_053962.3. [P09367-2]
UniGeneRn.9918.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PWEX-ray2.80A/B/C/D/E/F1-363[»]
1PWHX-ray2.60A/B/C/D1-363[»]
1RSQmodel-A9-363[»]
ProteinModelPortalP09367.
SMRP09367. Positions 1-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000001876.

Chemistry

ChEMBLCHEMBL1075240.

Proteomic databases

PaxDbP09367.
PRIDEP09367.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001875; ENSRNOP00000001875; ENSRNOG00000001388. [P09367-2]
GeneID25044.
KEGGrno:25044.

Organism-specific databases

CTD10993.
RGD67376. Sds.

Phylogenomic databases

eggNOGCOG1171.
GeneTreeENSGT00550000074775.
HOGENOMHOG000046976.
HOVERGENHBG017784.
InParanoidP09367.
KOK17989.
PhylomeDBP09367.

Enzyme and pathway databases

BRENDA4.3.1.17. 5301.
SABIO-RKP09367.
UniPathwayUPA00138.

Gene expression databases

GenevestigatorP09367.

Family and domain databases

InterProIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMSSF53686. SSF53686. 2 hits.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09367.
NextBio605215.
PROP09367.

Entry information

Entry nameSDHL_RAT
AccessionPrimary (citable) accession number: P09367
Secondary accession number(s): Q5M8C4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways