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P09367

- SDHL_RAT

UniProt

P09367 - SDHL_RAT

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Protein
L-serine dehydratase/L-threonine deaminase
Gene
Sds
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Pyridoxal phosphate.

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. cellular amino acid metabolic process Source: InterPro
  2. gluconeogenesis Source: RGD
  3. response to amino acid Source: RGD
  4. response to cobalamin Source: RGD
  5. response to nutrient levels Source: RGD
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: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 363362L-serine dehydratase/L-threonine deaminase
PRO_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

GenevestigatoriP09367.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001876.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

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. Trp_syn_b_sub_like_PLP_eny_SF.
[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. Align

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

MAAQESLHVK TPLRDSMALS KVAGTSVFLK MDSSQPSGSF KIRGIGHLCK    50
MKAKQGCKHF VCSSVVQIWG SRMRGRSHSG DEQPHVRSQA LLPDTPSPLT 100
AGNAGMATAY AARRLGLPAT IVVPSTTPAL TIERLKNEGA TVEVVGEMLD 150
EAIQLAKALE KNNPGWVYIS PFDDPLIWEG HTSLVKELKE TLSAKPGAIV 200
LSVGGGGLLC GVVQGLREVG WEDVPIIAME TFGAHSFHAA VKEGKLVTLP 250
KITSVAKALG VNTVGAQTLK LFYEHPIFSE VISDQEAVTA IEKFVDDEKI 300
LVEPACGAAL AAVYSGVVCR LQAEGRLQTP LASLVVIVCG GSNISLAQLQ 350
ALKAQLGLNE LLK 363
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei65 – 10036Missing in isoform 2.
VSP_024798Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121P → T AA sequence 1 Publication
Sequence conflicti16 – 161S → T in AAA42123. 1 Publication
Sequence conflicti164 – 1641P → Q in AAA42123. 1 Publication
Sequence conflicti276 – 2761P → T AA sequence 1 Publication
Sequence conflicti325 – 3251G → A in CAA68721. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
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:
EMBL
GenBank
DDBJ
Links Updated
J03863 mRNA. Translation: AAA42123.1 .
X13119 Genomic DNA. Translation: CAA31511.1 .
Y00752 mRNA. Translation: CAA68721.1 .
BC088110 mRNA. Translation: AAH88110.1 .
PIRi S01009. DWRTT.
S01973.
RefSeqi NP_446414.3. NM_053962.3. [P09367-2 ]
UniGenei Rn.9918.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PWE X-ray 2.80 A/B/C/D/E/F 1-363 [» ]
1PWH X-ray 2.60 A/B/C/D 1-363 [» ]
1RSQ model - A 9-363 [» ]
ProteinModelPortali P09367.
SMRi P09367. Positions 1-363.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000001876.

Chemistry

ChEMBLi CHEMBL1075240.

Proteomic databases

PaxDbi P09367.
PRIDEi P09367.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000001875 ; ENSRNOP00000001875 ; ENSRNOG00000001388 . [P09367-2 ]
GeneIDi 25044.
KEGGi rno:25044.

Organism-specific databases

CTDi 10993.
RGDi 67376. Sds.

Phylogenomic databases

eggNOGi COG1171.
GeneTreei ENSGT00550000074775.
HOGENOMi HOG000046976.
HOVERGENi HBG017784.
InParanoidi P09367.
KOi K17989.
PhylomeDBi P09367.

Enzyme and pathway databases

UniPathwayi UPA00138 .
BRENDAi 4.3.1.17. 5301.
SABIO-RK P09367.

Miscellaneous databases

EvolutionaryTracei P09367.
NextBioi 605215.
PROi P09367.

Gene expression databases

Genevestigatori P09367.

Family and domain databases

InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
[Graphical view ]
SUPFAMi SSF53686. SSF53686. 2 hits.
PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 134 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

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