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Protein

L-serine dehydratase/L-threonine deaminase

Gene

SDS

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

Functioni

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=23 mM for serine1 Publication
  2. KM=31 mM for threonine1 Publication

    Pathway:igluconeogenesis

    This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

    GO - Molecular functioni

    • L-serine ammonia-lyase activity Source: UniProtKB
    • L-threonine ammonia-lyase activity Source: GO_Central
    • protein homodimerization activity Source: UniProtKB
    • pyridoxal phosphate binding Source: UniProtKB

    GO - Biological processi

    • gluconeogenesis Source: UniProtKB-UniPathway
    • L-serine catabolic process Source: UniProtKB
    • pyruvate biosynthetic process Source: UniProtKB
    • 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

    BioCyciMetaCyc:HS05952-MONOMER.
    BRENDAi4.3.1.17. 2681.
    SABIO-RKP20132.
    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
    Synonyms:SDH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:10691. SDS.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi303 – 3031C → A: Loss of enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA35616.

    Chemistry

    DrugBankiDB00133. L-Serine.

    Polymorphism and mutation databases

    BioMutaiSDS.
    DMDMi229462819.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 328327L-serine dehydratase/L-threonine deaminasePRO_0000185594Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei41 – 411N6-(pyridoxal phosphate)lysine

    Proteomic databases

    PaxDbiP20132.
    PRIDEiP20132.

    PTM databases

    PhosphoSiteiP20132.

    Expressioni

    Gene expression databases

    BgeeiP20132.
    CleanExiHS_SDS.
    ExpressionAtlasiP20132. baseline and differential.
    GenevisibleiP20132. HS.

    Organism-specific databases

    HPAiHPA039230.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi9606.ENSP00000257549.

    Structurei

    Secondary structure

    1
    328
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 164Combined sources
    Helixi17 – 237Combined sources
    Beta strandi25 – 317Combined sources
    Helixi32 – 343Combined sources
    Helixi36 – 383Combined sources
    Helixi41 – 5414Combined sources
    Beta strandi59 – 624Combined sources
    Helixi67 – 7913Combined sources
    Beta strandi83 – 886Combined sources
    Helixi93 – 1019Combined sources
    Beta strandi105 – 1095Combined sources
    Helixi115 – 12612Combined sources
    Beta strandi130 – 1334Combined sources
    Helixi139 – 1457Combined sources
    Helixi147 – 1559Combined sources
    Beta strandi161 – 1666Combined sources
    Beta strandi168 – 1703Combined sources
    Helixi171 – 18212Combined sources
    Beta strandi190 – 1956Combined sources
    Helixi200 – 2078Combined sources
    Helixi221 – 2233Combined sources
    Helixi230 – 2367Combined sources
    Beta strandi241 – 2466Combined sources
    Helixi248 – 26215Combined sources
    Helixi268 – 27811Combined sources
    Helixi281 – 2877Combined sources
    Beta strandi297 – 3026Combined sources
    Helixi310 – 31910Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P5JX-ray2.50A1-328[»]
    4H27X-ray1.30A1-328[»]
    ProteinModelPortaliP20132.
    SMRiP20132. Positions 4-322.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20132.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1171.
    GeneTreeiENSGT00550000074775.
    HOGENOMiHOG000046976.
    HOVERGENiHBG017784.
    InParanoidiP20132.
    KOiK17989.
    OMAiYVHPFDH.
    OrthoDBiEOG7VDXQ1.
    PhylomeDBiP20132.
    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.

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

    P20132-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MMSGEPLHVK TPIRDSMALS KMAGTSVYLK MDSAQPSGSF KIRGIGHFCK
    60 70 80 90 100
    RWAKQGCAHF VCSSAGNAGM AAAYAARQLG VPATIVVPST TPALTIERLK
    110 120 130 140 150
    NEGATVKVVG ELLDEAFELA KALAKNNPGW VYIPPFDDPL IWEGHASIVK
    160 170 180 190 200
    ELKETLWEKP GAIALSVGGG GLLCGVVQGL QEVGWGDVPV IAMETFGAHS
    210 220 230 240 250
    FHAATTAGKL VSLPKITSVA KALGVKTVGA QALKLFQEHP IFSEVISDQE
    260 270 280 290 300
    AVAAIEKFVD DEKILVEPAC GAALAAVYSH VIQKLQLEGN LRTPLPSLVV
    310 320
    IVCGGSNISL AQLRALKEQL GMTNRLPK
    Length:328
    Mass (Da):34,625
    Last modified:May 5, 2009 - v2
    Checksum:iF6E9AB01D6308C83
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti89 – 891S → G in AAA36604 (PubMed:2674117).Curated
    Sequence conflicti106 – 1061V → C in AAA36604 (PubMed:2674117).Curated
    Sequence conflicti183 – 1831V → C in AAA36604 (PubMed:2674117).Curated
    Sequence conflicti230 – 2301A → S in AAA36604 (PubMed:2674117).Curated
    Sequence conflicti270 – 2701C → W in AAA36604 (PubMed:2674117).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05037 mRNA. Translation: AAA36604.1.
    AK292760 mRNA. Translation: BAF85449.1.
    CH471054 Genomic DNA. Translation: EAW98054.1.
    CCDSiCCDS9169.1.
    PIRiA34232. DWHUT.
    RefSeqiNP_006834.2. NM_006843.2.
    UniGeneiHs.439023.

    Genome annotation databases

    EnsembliENST00000257549; ENSP00000257549; ENSG00000135094.
    GeneIDi10993.
    KEGGihsa:10993.
    UCSCiuc001tvg.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05037 mRNA. Translation: AAA36604.1.
    AK292760 mRNA. Translation: BAF85449.1.
    CH471054 Genomic DNA. Translation: EAW98054.1.
    CCDSiCCDS9169.1.
    PIRiA34232. DWHUT.
    RefSeqiNP_006834.2. NM_006843.2.
    UniGeneiHs.439023.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P5JX-ray2.50A1-328[»]
    4H27X-ray1.30A1-328[»]
    ProteinModelPortaliP20132.
    SMRiP20132. Positions 4-322.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9606.ENSP00000257549.

    Chemistry

    DrugBankiDB00133. L-Serine.

    PTM databases

    PhosphoSiteiP20132.

    Polymorphism and mutation databases

    BioMutaiSDS.
    DMDMi229462819.

    Proteomic databases

    PaxDbiP20132.
    PRIDEiP20132.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000257549; ENSP00000257549; ENSG00000135094.
    GeneIDi10993.
    KEGGihsa:10993.
    UCSCiuc001tvg.3. human.

    Organism-specific databases

    CTDi10993.
    GeneCardsiGC12M113830.
    HGNCiHGNC:10691. SDS.
    HPAiHPA039230.
    MIMi182128. gene.
    neXtProtiNX_P20132.
    PharmGKBiPA35616.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1171.
    GeneTreeiENSGT00550000074775.
    HOGENOMiHOG000046976.
    HOVERGENiHBG017784.
    InParanoidiP20132.
    KOiK17989.
    OMAiYVHPFDH.
    OrthoDBiEOG7VDXQ1.
    PhylomeDBiP20132.
    TreeFamiTF329014.

    Enzyme and pathway databases

    UniPathwayiUPA00138.
    BioCyciMetaCyc:HS05952-MONOMER.
    BRENDAi4.3.1.17. 2681.
    SABIO-RKP20132.

    Miscellaneous databases

    ChiTaRSiSDS. human.
    EvolutionaryTraceiP20132.
    GenomeRNAii10993.
    NextBioi41775.
    PROiP20132.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP20132.
    CleanExiHS_SDS.
    ExpressionAtlasiP20132. baseline and differential.
    GenevisibleiP20132. 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. "Human liver serine dehydratase. cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources."
      Ogawa H., Gomi T., Konishi K., Date T., Nakashima H., Nose K., Matsuda Y., Peraino C., Pitot H.C., Fujioka M.
      J. Biol. Chem. 264:15818-15823(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-303, BIOPHYSICOCHEMICAL PROPERTIES.
    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. "Crystallization and preliminary crystallographic analysis of human serine dehydratase."
      Sun L., Li X., Dong Y., Yang M., Liu Y., Han X., Zhang X., Pang H., Rao Z.
      Acta Crystallogr. D 59:2297-2299(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE.

    Entry informationi

    Entry nameiSDHL_HUMAN
    AccessioniPrimary (citable) accession number: P20132
    Secondary accession number(s): A8K9P5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: May 5, 2009
    Last modified: July 22, 2015
    This is version 146 of the entry and version 2 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. 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.