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Q96GA7 (SDSL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine dehydratase-like
Alternative name(s):
L-serine deaminase
L-serine dehydratase/L-threonine deaminase
L-threonine dehydratase
Short name=TDH
EC=4.3.1.19
Serine dehydratase 2
Short name=SDH 2
EC=4.3.1.17
Gene names
Name:SDSL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has low serine dehydratase and threonine dehydratase activity.

Catalytic activity

L-serine = pyruvate + NH3. Ref.5

L-threonine = 2-oxobutanoate + NH3. Ref.5

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer Probable. Ref.5

Sequence similarities

Belongs to the serine/threonine dehydratase family.

Biophysicochemical properties

Kinetic parameters:

KM=30 mM for serine

KM=7 mM for threonine

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Serine dehydratase-like
PRO_0000264624

Amino acid modifications

Modified residue11N-acetylmethionine Ref.4
Modified residue481N6-(pyridoxal phosphate)lysine

Experimental info

Mutagenesis721G → A: Strongly increased enzyme activity towards threonine. Ref.5
Mutagenesis3091C → A: Loss of enzyme activity. Ref.5

Secondary structure

................................................... 329
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96GA7 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: CEAD30E570A43B7E

FASTA32934,674
        10         20         30         40         50         60 
MDGPVAEHAK QEPFHVVTPL LESWALSQVA GMPVFLKCEN VQPSGSFKIR GIGHFCQEMA 

        70         80         90        100        110        120 
KKGCRHLVCS SGGNAGIAAA YAARKLGIPA TIVLPESTSL QVVQRLQGEG AEVQLTGKVW 

       130        140        150        160        170        180 
DEANLRAQEL AKRDGWENVP PFDHPLIWKG HASLVQELKA VLRTPPGALV LAVGGGGLLA 

       190        200        210        220        230        240 
GVVAGLLEVG WQHVPIIAME THGAHCFNAA ITAGKLVTLP DITSVAKSLG AKTVAARALE 

       250        260        270        280        290        300 
CMQVCKIHSE VVEDTEAVSA VQQLLDDERM LVEPACGAAL AAIYSGLLRR LQAEGCLPPS 

       310        320 
LTSVVVIVCG GNNINSRELQ ALKTHLGQV 

« Hide

References

« Hide 'large scale' references
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF134473 mRNA. Translation: AAP97250.1.
BC009849 mRNA. Translation: AAH09849.1.
BC091479 mRNA. Translation: AAH91479.1.
CCDSCCDS9170.1.
RefSeqNP_612441.1. NM_138432.2.
XP_005253887.1. XM_005253830.2.
XP_005253888.1. XM_005253831.2.
UniGeneHs.337594.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RKBX-ray2.80A/B/C/D/E11-328[»]
ProteinModelPortalQ96GA7.
SMRQ96GA7. Positions 11-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125255. 3 interactions.
IntActQ96GA7. 2 interactions.
MINTMINT-1456379.
STRING9606.ENSP00000341117.

Chemistry

DrugBankDB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteQ96GA7.

Polymorphism databases

DMDM74731799.

Proteomic databases

MaxQBQ96GA7.
PaxDbQ96GA7.
PRIDEQ96GA7.

Protocols and materials databases

DNASU113675.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345635; ENSP00000341117; ENSG00000139410.
ENST00000403593; ENSP00000385790; ENSG00000139410.
GeneID113675.
KEGGhsa:113675.
UCSCuc001tvi.3. human.

Organism-specific databases

CTD113675.
GeneCardsGC12P113860.
HGNCHGNC:30404. SDSL.
HPAHPA005740.
neXtProtNX_Q96GA7.
PharmGKBPA134862016.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1171.
HOGENOMHOG000046976.
HOVERGENHBG017784.
InParanoidQ96GA7.
KOK17989.
OMAETHGAHC.
OrthoDBEOG7VDXQ1.
PhylomeDBQ96GA7.
TreeFamTF329014.

Enzyme and pathway databases

BioCycMetaCyc:HS06616-MONOMER.
SABIO-RKQ96GA7.

Gene expression databases

ArrayExpressQ96GA7.
BgeeQ96GA7.
CleanExHS_SDSL.
GenevestigatorQ96GA7.

Family and domain databases

InterProIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMSSF53686. SSF53686. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSDSL. human.
EvolutionaryTraceQ96GA7.
GenomeRNAi113675.
NextBio78888.
PROQ96GA7.

Entry information

Entry nameSDSL_HUMAN
AccessionPrimary (citable) accession number: Q96GA7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 12

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