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P09367

- SDHL_RAT

UniProt

P09367 - SDHL_RAT

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
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    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

    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 – 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.
    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. 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

    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:
    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

    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: October 1, 2014
    This is version 135 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