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P20132

- SDHL_HUMAN

UniProt

P20132 - SDHL_HUMAN

Protein

L-serine dehydratase/L-threonine deaminase

Gene

SDS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.

    Kineticsi

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

    Pathwayi

    GO - Molecular functioni

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

    GO - Biological processi

    1. gluconeogenesis Source: UniProtKB-UniPathway
    2. L-serine catabolic process Source: UniProtKB
    3. pyruvate biosynthetic process Source: UniProtKB
    4. response to amino acid Source: Ensembl
    5. response to cobalamin Source: Ensembl

    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: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:10691. SDS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. mitochondrion Source: HPA

    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.

    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

    ArrayExpressiP20132.
    BgeeiP20132.
    CleanExiHS_SDS.
    GenevestigatoriP20132.

    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 – 164
    Helixi17 – 237
    Beta strandi25 – 317
    Helixi32 – 343
    Helixi36 – 383
    Helixi41 – 5414
    Beta strandi59 – 624
    Helixi67 – 7913
    Beta strandi83 – 886
    Helixi93 – 1019
    Beta strandi105 – 1095
    Helixi115 – 12612
    Beta strandi130 – 1334
    Helixi139 – 1457
    Helixi147 – 1559
    Beta strandi161 – 1666
    Beta strandi168 – 1703
    Helixi171 – 18212
    Beta strandi190 – 1956
    Helixi200 – 2078
    Helixi221 – 2233
    Helixi230 – 2367
    Beta strandi241 – 2466
    Helixi248 – 26215
    Helixi268 – 27811
    Helixi281 – 2877
    Beta strandi297 – 3026
    Helixi310 – 31910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000046976.
    HOVERGENiHBG017784.
    InParanoidiP20132.
    KOiK17989.
    OMAiGWIYVPP.
    OrthoDBiEOG7VDXQ1.
    PhylomeDBiP20132.
    TreeFamiTF329014.

    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. 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

    MMSGEPLHVK TPIRDSMALS KMAGTSVYLK MDSAQPSGSF KIRGIGHFCK    50
    RWAKQGCAHF VCSSAGNAGM AAAYAARQLG VPATIVVPST TPALTIERLK 100
    NEGATVKVVG ELLDEAFELA KALAKNNPGW VYIPPFDDPL IWEGHASIVK 150
    ELKETLWEKP GAIALSVGGG GLLCGVVQGL QEVGWGDVPV IAMETFGAHS 200
    FHAATTAGKL VSLPKITSVA KALGVKTVGA QALKLFQEHP IFSEVISDQE 250
    AVAAIEKFVD DEKILVEPAC GAALAAVYSH VIQKLQLEGN LRTPLPSLVV 300
    IVCGGSNISL AQLRALKEQL GMTNRLPK 328
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi229462819.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05037 mRNA. Translation: AAA36604.1 .
    AK292760 mRNA. Translation: BAF85449.1 .
    CH471054 Genomic DNA. Translation: EAW98054.1 .
    CCDSi CCDS9169.1.
    PIRi A34232. DWHUT.
    RefSeqi NP_006834.2. NM_006843.2.
    UniGenei Hs.439023.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P5J X-ray 2.50 A 1-328 [» ]
    4H27 X-ray 1.30 A 1-328 [» ]
    ProteinModelPortali P20132.
    SMRi P20132. Positions 4-322.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000257549.

    Chemistry

    DrugBanki DB00133. L-Serine.
    DB00114. Pyridoxal Phosphate.

    PTM databases

    PhosphoSitei P20132.

    Polymorphism databases

    DMDMi 229462819.

    Proteomic databases

    PaxDbi P20132.
    PRIDEi P20132.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257549 ; ENSP00000257549 ; ENSG00000135094 .
    GeneIDi 10993.
    KEGGi hsa:10993.
    UCSCi uc001tvg.3. human.

    Organism-specific databases

    CTDi 10993.
    GeneCardsi GC12M113830.
    HGNCi HGNC:10691. SDS.
    HPAi HPA039230.
    MIMi 182128. gene.
    neXtProti NX_P20132.
    PharmGKBi PA35616.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1171.
    HOGENOMi HOG000046976.
    HOVERGENi HBG017784.
    InParanoidi P20132.
    KOi K17989.
    OMAi GWIYVPP.
    OrthoDBi EOG7VDXQ1.
    PhylomeDBi P20132.
    TreeFami TF329014.

    Enzyme and pathway databases

    UniPathwayi UPA00138 .
    BioCyci MetaCyc:HS05952-MONOMER.
    BRENDAi 4.3.1.17. 2681.
    SABIO-RK P20132.

    Miscellaneous databases

    ChiTaRSi SDS. human.
    EvolutionaryTracei P20132.
    GenomeRNAii 10993.
    NextBioi 41775.
    PROi P20132.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20132.
    Bgeei P20132.
    CleanExi HS_SDS.
    Genevestigatori P20132.

    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. 1 hit.
    PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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: October 1, 2014
    This is version 138 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