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Protein

Serine dehydratase-like

Gene

SDSL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has low serine dehydratase and threonine dehydratase activity.

Catalytic activityi

L-serine = pyruvate + NH3.1 Publication
L-threonine = 2-oxobutanoate + NH3.1 Publication

Cofactori

Kineticsi

  1. KM=30 mM for serine
  2. KM=7 mM for threonine

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06616-MONOMER.
    BRENDAi4.3.1.17. 2681.
    SABIO-RKQ96GA7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine dehydratase-like
    Alternative name(s):
    L-serine deaminase
    L-serine dehydratase/L-threonine deaminase
    L-threonine dehydratase (EC:4.3.1.19)
    Short name:
    TDH
    Serine dehydratase 2 (EC:4.3.1.17)
    Short name:
    SDH 2
    Gene namesi
    Name:SDSL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:30404. SDSL.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: GO_Central
    • extracellular exosome Source: UniProtKB
    • mitochondrion Source: Ensembl
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi72 – 721G → A: Strongly increased enzyme activity towards threonine. 1 Publication
    Mutagenesisi309 – 3091C → A: Loss of enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134862016.

    Polymorphism and mutation databases

    BioMutaiSDSL.
    DMDMi74731799.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 329329Serine dehydratase-likePRO_0000264624Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei48 – 481N6-(pyridoxal phosphate)lysine

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ96GA7.
    PaxDbiQ96GA7.
    PRIDEiQ96GA7.

    PTM databases

    PhosphoSiteiQ96GA7.

    Expressioni

    Gene expression databases

    BgeeiQ96GA7.
    CleanExiHS_SDSL.
    ExpressionAtlasiQ96GA7. baseline and differential.
    GenevisibleiQ96GA7. HS.

    Organism-specific databases

    HPAiHPA005740.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi125255. 3 interactions.
    IntActiQ96GA7. 2 interactions.
    MINTiMINT-1456379.
    STRINGi9606.ENSP00000341117.

    Structurei

    Secondary structure

    1
    329
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi20 – 234Combined sources
    Helixi24 – 307Combined sources
    Beta strandi34 – 385Combined sources
    Helixi39 – 413Combined sources
    Helixi49 – 6113Combined sources
    Beta strandi66 – 694Combined sources
    Helixi74 – 8512Combined sources
    Beta strandi90 – 945Combined sources
    Helixi100 – 1089Combined sources
    Beta strandi112 – 1154Combined sources
    Helixi120 – 13213Combined sources
    Beta strandi136 – 1383Combined sources
    Helixi145 – 16117Combined sources
    Beta strandi162 – 1643Combined sources
    Beta strandi167 – 1726Combined sources
    Beta strandi174 – 1763Combined sources
    Helixi177 – 18913Combined sources
    Beta strandi196 – 2016Combined sources
    Helixi206 – 2138Combined sources
    Helixi227 – 2293Combined sources
    Helixi236 – 2449Combined sources
    Beta strandi247 – 2526Combined sources
    Helixi254 – 26815Combined sources
    Helixi274 – 28411Combined sources
    Helixi287 – 2937Combined sources
    Beta strandi304 – 3085Combined sources
    Helixi316 – 32510Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RKBX-ray2.80A/B/C/D/E11-328[»]
    ProteinModelPortaliQ96GA7.
    SMRiQ96GA7. Positions 11-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96GA7.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1171.
    GeneTreeiENSGT00550000074775.
    HOGENOMiHOG000046976.
    HOVERGENiHBG017784.
    InParanoidiQ96GA7.
    KOiK17989.
    OMAiGHFCQEM.
    OrthoDBiEOG7VDXQ1.
    PhylomeDBiQ96GA7.
    TreeFamiTF329014.

    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. 1 hit.
    PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q96GA7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDGPVAEHAK QEPFHVVTPL LESWALSQVA GMPVFLKCEN VQPSGSFKIR
    60 70 80 90 100
    GIGHFCQEMA KKGCRHLVCS SGGNAGIAAA YAARKLGIPA TIVLPESTSL
    110 120 130 140 150
    QVVQRLQGEG AEVQLTGKVW DEANLRAQEL AKRDGWENVP PFDHPLIWKG
    160 170 180 190 200
    HASLVQELKA VLRTPPGALV LAVGGGGLLA GVVAGLLEVG WQHVPIIAME
    210 220 230 240 250
    THGAHCFNAA ITAGKLVTLP DITSVAKSLG AKTVAARALE CMQVCKIHSE
    260 270 280 290 300
    VVEDTEAVSA VQQLLDDERM LVEPACGAAL AAIYSGLLRR LQAEGCLPPS
    310 320
    LTSVVVIVCG GNNINSRELQ ALKTHLGQV
    Length:329
    Mass (Da):34,674
    Last modified:December 1, 2001 - v1
    Checksum:iCEAD30E570A43B7E
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF134473 mRNA. Translation: AAP97250.1.
    BC009849 mRNA. Translation: AAH09849.1.
    BC091479 mRNA. Translation: AAH91479.1.
    CCDSiCCDS9170.1.
    RefSeqiNP_612441.1. NM_138432.3.
    XP_005253888.1. XM_005253831.3.
    UniGeneiHs.337594.

    Genome annotation databases

    EnsembliENST00000345635; ENSP00000341117; ENSG00000139410.
    ENST00000403593; ENSP00000385790; ENSG00000139410.
    GeneIDi113675.
    KEGGihsa:113675.
    UCSCiuc001tvi.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF134473 mRNA. Translation: AAP97250.1.
    BC009849 mRNA. Translation: AAH09849.1.
    BC091479 mRNA. Translation: AAH91479.1.
    CCDSiCCDS9170.1.
    RefSeqiNP_612441.1. NM_138432.3.
    XP_005253888.1. XM_005253831.3.
    UniGeneiHs.337594.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RKBX-ray2.80A/B/C/D/E11-328[»]
    ProteinModelPortaliQ96GA7.
    SMRiQ96GA7. Positions 11-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi125255. 3 interactions.
    IntActiQ96GA7. 2 interactions.
    MINTiMINT-1456379.
    STRINGi9606.ENSP00000341117.

    PTM databases

    PhosphoSiteiQ96GA7.

    Polymorphism and mutation databases

    BioMutaiSDSL.
    DMDMi74731799.

    Proteomic databases

    MaxQBiQ96GA7.
    PaxDbiQ96GA7.
    PRIDEiQ96GA7.

    Protocols and materials databases

    DNASUi113675.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000345635; ENSP00000341117; ENSG00000139410.
    ENST00000403593; ENSP00000385790; ENSG00000139410.
    GeneIDi113675.
    KEGGihsa:113675.
    UCSCiuc001tvi.3. human.

    Organism-specific databases

    CTDi113675.
    GeneCardsiGC12P113860.
    HGNCiHGNC:30404. SDSL.
    HPAiHPA005740.
    neXtProtiNX_Q96GA7.
    PharmGKBiPA134862016.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1171.
    GeneTreeiENSGT00550000074775.
    HOGENOMiHOG000046976.
    HOVERGENiHBG017784.
    InParanoidiQ96GA7.
    KOiK17989.
    OMAiGHFCQEM.
    OrthoDBiEOG7VDXQ1.
    PhylomeDBiQ96GA7.
    TreeFamiTF329014.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06616-MONOMER.
    BRENDAi4.3.1.17. 2681.
    SABIO-RKQ96GA7.

    Miscellaneous databases

    ChiTaRSiSDSL. human.
    EvolutionaryTraceiQ96GA7.
    GenomeRNAii113675.
    NextBioi78888.
    PROiQ96GA7.

    Gene expression databases

    BgeeiQ96GA7.
    CleanExiHS_SDSL.
    ExpressionAtlasiQ96GA7. baseline and differential.
    GenevisibleiQ96GA7. HS.

    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. 1 hit.
    PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning of a new human cDNA homologous to Homo sapiens serine dehydratase."
      Gong R.M., Yu L., Zhao S.Y.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
      Tissue: Lung and Placenta.
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    4. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: crystal structure and site-directed mutagenesis studies."
      Yamada T., Komoto J., Kasuya T., Takata Y., Ogawa H., Mori H., Takusagawa F.
      Biochim. Biophys. Acta 1780:809-818(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 11-328 IN COMPLEX WITH PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF GLY-72 AND CYS-309.

    Entry informationi

    Entry nameiSDSL_HUMAN
    AccessioniPrimary (citable) accession number: Q96GA7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: December 1, 2001
    Last modified: June 24, 2015
    This is version 106 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    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.