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Protein

L-serine dehydratase/L-threonine deaminase

Gene

Sds

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-serine = pyruvate + NH3.
L-threonine = 2-oxobutanoate + NH3.

Cofactori

Pathwayi

GO - Molecular functioni

  1. L-serine ammonia-lyase activity Source: RGD
  2. L-threonine ammonia-lyase activity Source: GO_Central
  3. protein dimerization activity Source: RGD
  4. pyridoxal phosphate binding Source: GO_Central

GO - Biological processi

  1. gluconeogenesis Source: RGD
  2. L-serine catabolic process Source: GO_Central
  3. response to amino acid Source: RGD
  4. response to cobalamin Source: RGD
  5. response to nutrient levels Source: RGD
  6. threonine catabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Gluconeogenesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi4.3.1.17. 5301.
SABIO-RKP09367.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
L-serine dehydratase/L-threonine deaminase (EC:4.3.1.17)
Short name:
SDH
Alternative name(s):
L-serine deaminase
L-threonine dehydratase (EC:4.3.1.19)
Short name:
TDH
Gene namesi
Name:Sds
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 12

Organism-specific databases

RGDi67376. Sds.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 363362L-serine dehydratase/L-threonine deaminasePRO_0000185596Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei41 – 411N6-(pyridoxal phosphate)lysine

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP09367.
PRIDEiP09367.

Expressioni

Inductioni

By glucocorticoids and glucagon.

Gene expression databases

ExpressionAtlasiP09367. baseline and differential.
GenevestigatoriP09367.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001876.

Structurei

Secondary structure

1
363
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 153Combined sources
Helixi17 – 237Combined sources
Beta strandi27 – 304Combined sources
Helixi32 – 343Combined sources
Helixi42 – 5413Combined sources
Beta strandi59 – 635Combined sources
Helixi103 – 11412Combined sources
Beta strandi119 – 1235Combined sources
Helixi129 – 1379Combined sources
Beta strandi141 – 1444Combined sources
Helixi149 – 16113Combined sources
Beta strandi166 – 1694Combined sources
Turni171 – 1733Combined sources
Helixi175 – 19117Combined sources
Beta strandi199 – 2024Combined sources
Beta strandi204 – 2063Combined sources
Helixi207 – 21913Combined sources
Beta strandi226 – 2316Combined sources
Helixi236 – 2438Combined sources
Helixi257 – 2593Combined sources
Helixi266 – 2727Combined sources
Turni273 – 2764Combined sources
Beta strandi277 – 2826Combined sources
Helixi284 – 29815Combined sources
Helixi304 – 31411Combined sources
Helixi317 – 3237Combined sources
Beta strandi324 – 3274Combined sources
Beta strandi334 – 3374Combined sources
Helixi346 – 35510Combined sources
Turni356 – 3594Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PWEX-ray2.80A/B/C/D/E/F1-363[»]
1PWHX-ray2.60A/B/C/D1-363[»]
1RSQmodel-A9-363[»]
ProteinModelPortaliP09367.
SMRiP09367. Positions 1-363.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09367.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1171.
GeneTreeiENSGT00550000074775.
HOGENOMiHOG000046976.
HOVERGENiHBG017784.
InParanoidiP09367.
KOiK17989.
PhylomeDBiP09367.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 2 hits.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P09367-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAQESLHVK TPLRDSMALS KVAGTSVFLK MDSSQPSGSF KIRGIGHLCK
60 70 80 90 100
MKAKQGCKHF VCSSVVQIWG SRMRGRSHSG DEQPHVRSQA LLPDTPSPLT
110 120 130 140 150
AGNAGMATAY AARRLGLPAT IVVPSTTPAL TIERLKNEGA TVEVVGEMLD
160 170 180 190 200
EAIQLAKALE KNNPGWVYIS PFDDPLIWEG HTSLVKELKE TLSAKPGAIV
210 220 230 240 250
LSVGGGGLLC GVVQGLREVG WEDVPIIAME TFGAHSFHAA VKEGKLVTLP
260 270 280 290 300
KITSVAKALG VNTVGAQTLK LFYEHPIFSE VISDQEAVTA IEKFVDDEKI
310 320 330 340 350
LVEPACGAAL AAVYSGVVCR LQAEGRLQTP LASLVVIVCG GSNISLAQLQ
360
ALKAQLGLNE LLK
Length:363
Mass (Da):38,433
Last modified:January 23, 2007 - v3
Checksum:iC94FFF2EB9C6E33C
GO
Isoform 2 (identifier: P09367-2) [UniParc]FASTAAdd to basket

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

Show »
Length:327
Mass (Da):34,454
Checksum:i525C043E62BDF388
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121P → T AA sequence (PubMed:2228554).Curated
Sequence conflicti16 – 161S → T in AAA42123 (PubMed:3413060).Curated
Sequence conflicti164 – 1641P → Q in AAA42123 (PubMed:3413060).Curated
Sequence conflicti276 – 2761P → T AA sequence (PubMed:2228554).Curated
Sequence conflicti325 – 3251G → A in CAA68721 (PubMed:3391277).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei65 – 10036Missing in isoform 2. 2 PublicationsVSP_024798Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03863 mRNA. Translation: AAA42123.1.
X13119 Genomic DNA. Translation: CAA31511.1.
Y00752 mRNA. Translation: CAA68721.1.
BC088110 mRNA. Translation: AAH88110.1.
PIRiS01009. DWRTT.
S01973.
RefSeqiNP_446414.3. NM_053962.3. [P09367-2]
XP_008767435.1. XM_008769213.1. [P09367-2]
UniGeneiRn.9918.

Genome annotation databases

EnsembliENSRNOT00000001875; ENSRNOP00000001875; ENSRNOG00000001388. [P09367-2]
GeneIDi25044.
KEGGirno:25044.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03863 mRNA. Translation: AAA42123.1.
X13119 Genomic DNA. Translation: CAA31511.1.
Y00752 mRNA. Translation: CAA68721.1.
BC088110 mRNA. Translation: AAH88110.1.
PIRiS01009. DWRTT.
S01973.
RefSeqiNP_446414.3. NM_053962.3. [P09367-2]
XP_008767435.1. XM_008769213.1. [P09367-2]
UniGeneiRn.9918.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PWEX-ray2.80A/B/C/D/E/F1-363[»]
1PWHX-ray2.60A/B/C/D1-363[»]
1RSQmodel-A9-363[»]
ProteinModelPortaliP09367.
SMRiP09367. Positions 1-363.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001876.

Chemistry

ChEMBLiCHEMBL1075240.

Proteomic databases

PaxDbiP09367.
PRIDEiP09367.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001875; ENSRNOP00000001875; ENSRNOG00000001388. [P09367-2]
GeneIDi25044.
KEGGirno:25044.

Organism-specific databases

CTDi10993.
RGDi67376. Sds.

Phylogenomic databases

eggNOGiCOG1171.
GeneTreeiENSGT00550000074775.
HOGENOMiHOG000046976.
HOVERGENiHBG017784.
InParanoidiP09367.
KOiK17989.
PhylomeDBiP09367.

Enzyme and pathway databases

UniPathwayiUPA00138.
BRENDAi4.3.1.17. 5301.
SABIO-RKP09367.

Miscellaneous databases

EvolutionaryTraceiP09367.
NextBioi605215.
PROiP09367.

Gene expression databases

ExpressionAtlasiP09367. baseline and differential.
GenevestigatoriP09367.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 2 hits.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Entry informationi

Entry nameiSDHL_RAT
AccessioniPrimary (citable) accession number: P09367
Secondary accession number(s): Q5M8C4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.