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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

    Keywordsi

    Molecular functionLyase
    LigandPyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06616-MONOMER.
    BRENDAi4.3.1.17. 2681.
    SABIO-RKiQ96GA7.

    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
    Proteomesi
    • UP000005640 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:30404. SDSL.

    Subcellular locationi

    GO - Cellular componenti

    • extracellular exosome Source: UniProtKB
    • mitochondrion Source: Ensembl

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi72G → A: Strongly increased enzyme activity towards threonine. 1 Publication1
    Mutagenesisi309C → A: Loss of enzyme activity. 1 Publication1

    Organism-specific databases

    DisGeNETi113675.
    OpenTargetsiENSG00000139410.
    PharmGKBiPA134862016.

    Chemistry databases

    DrugBankiDB00114. Pyridoxal Phosphate.

    Polymorphism and mutation databases

    BioMutaiSDSL.
    DMDMi74731799.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002646241 – 329Serine dehydratase-likeAdd BLAST329

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei1N-acetylmethionineCombined sources1
    Modified residuei48N6-(pyridoxal phosphate)lysine1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiQ96GA7.
    MaxQBiQ96GA7.
    PaxDbiQ96GA7.
    PeptideAtlasiQ96GA7.
    PRIDEiQ96GA7.

    PTM databases

    iPTMnetiQ96GA7.
    PhosphoSitePlusiQ96GA7.

    Expressioni

    Gene expression databases

    BgeeiENSG00000139410.
    CleanExiHS_SDSL.
    ExpressionAtlasiQ96GA7. baseline and differential.
    GenevisibleiQ96GA7. HS.

    Organism-specific databases

    HPAiHPA005740.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-744440,EBI-744440

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi125255. 2 interactors.
    IntActiQ96GA7. 2 interactors.
    MINTiMINT-1456379.
    STRINGi9606.ENSP00000341117.

    Structurei

    Secondary structure

    1329
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi20 – 23Combined sources4
    Helixi24 – 30Combined sources7
    Beta strandi34 – 38Combined sources5
    Helixi39 – 41Combined sources3
    Helixi49 – 61Combined sources13
    Beta strandi66 – 69Combined sources4
    Helixi74 – 85Combined sources12
    Beta strandi90 – 94Combined sources5
    Helixi100 – 108Combined sources9
    Beta strandi112 – 115Combined sources4
    Helixi120 – 132Combined sources13
    Beta strandi136 – 138Combined sources3
    Helixi145 – 161Combined sources17
    Beta strandi162 – 164Combined sources3
    Beta strandi167 – 172Combined sources6
    Beta strandi174 – 176Combined sources3
    Helixi177 – 189Combined sources13
    Beta strandi196 – 201Combined sources6
    Helixi206 – 213Combined sources8
    Helixi227 – 229Combined sources3
    Helixi236 – 244Combined sources9
    Beta strandi247 – 252Combined sources6
    Helixi254 – 268Combined sources15
    Helixi274 – 284Combined sources11
    Helixi287 – 293Combined sources7
    Beta strandi304 – 308Combined sources5
    Helixi316 – 325Combined sources10

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ96GA7.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1250. Eukaryota.
    COG1171. LUCA.
    GeneTreeiENSGT00550000074775.
    HOGENOMiHOG000046976.
    HOVERGENiHBG017784.
    InParanoidiQ96GA7.
    KOiK17989.
    OMAiGCRHLVC.
    OrthoDBiEOG091G0FCF.
    PhylomeDBiQ96GA7.
    TreeFamiTF329014.

    Family and domain databases

    InterProiView protein in InterPro
    IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR001926. TrpB-like_PLP-dep.
    PfamiView protein in Pfam
    PF00291. PALP. 1 hit.
    SUPFAMiSSF53686. SSF53686. 1 hit.
    PROSITEiView protein in PROSITE
    PS00165. DEHYDRATASE_SER_THR. 1 hit.

    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_001291922.1. NM_001304993.1.
    NP_612441.1. NM_138432.3.
    XP_005253888.1. XM_005253831.4.
    XP_011536148.1. XM_011537846.2.
    UniGeneiHs.337594.

    Genome annotation databases

    EnsembliENST00000345635; ENSP00000341117; ENSG00000139410.
    ENST00000403593; ENSP00000385790; ENSG00000139410.
    GeneIDi113675.
    KEGGihsa:113675.
    UCSCiuc009zwh.4. human.

    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 one 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.

    Entry informationi

    Entry nameiSDSL_HUMAN
    AccessioniPrimary (citable) accession number: Q96GA7
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: December 1, 2001
    Last modified: June 7, 2017
    This is version 122 of the entry and version 1 of the sequence. See 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