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P20132 (SDHL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
L-serine dehydratase/L-threonine deaminase

Short name=SDH
EC=4.3.1.17
Alternative name(s):
L-serine deaminase
L-threonine dehydratase
Short name=TDH
EC=4.3.1.19
Gene names
Name:SDS
Synonyms:SDH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-serine = pyruvate + NH3. Ref.4

L-threonine = 2-oxobutanoate + NH3. Ref.4

Cofactor

Pyridoxal phosphate.

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the serine/threonine dehydratase family.

Biophysicochemical properties

Kinetic parameters:

KM=23 mM for serine Ref.4

KM=31 mM for threonine

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 328327L-serine dehydratase/L-threonine deaminase
PRO_0000185594

Amino acid modifications

Modified residue411N6-(pyridoxal phosphate)lysine

Experimental info

Mutagenesis3031C → A: Loss of enzyme activity. Ref.4
Sequence conflict891S → G in AAA36604. Ref.1
Sequence conflict1061V → C in AAA36604. Ref.1
Sequence conflict1831V → C in AAA36604. Ref.1
Sequence conflict2301A → S in AAA36604. Ref.1
Sequence conflict2701C → W in AAA36604. Ref.1

Secondary structure

...................................................... 328
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20132 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: F6E9AB01D6308C83

FASTA32834,625
        10         20         30         40         50         60 
MMSGEPLHVK TPIRDSMALS KMAGTSVYLK MDSAQPSGSF KIRGIGHFCK RWAKQGCAHF 

        70         80         90        100        110        120 
VCSSAGNAGM AAAYAARQLG VPATIVVPST TPALTIERLK NEGATVKVVG ELLDEAFELA 

       130        140        150        160        170        180 
KALAKNNPGW VYIPPFDDPL IWEGHASIVK ELKETLWEKP GAIALSVGGG GLLCGVVQGL 

       190        200        210        220        230        240 
QEVGWGDVPV IAMETFGAHS FHAATTAGKL VSLPKITSVA KALGVKTVGA QALKLFQEHP 

       250        260        270        280        290        300 
IFSEVISDQE AVAAIEKFVD DEKILVEPAC GAALAAVYSH VIQKLQLEGN LRTPLPSLVV 

       310        320 
IVCGGSNISL AQLRALKEQL GMTNRLPK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05037 mRNA. Translation: AAA36604.1.
AK292760 mRNA. Translation: BAF85449.1.
CH471054 Genomic DNA. Translation: EAW98054.1.
PIRDWHUT. A34232.
RefSeqNP_006834.2. NM_006843.2.
UniGeneHs.439023.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P5JX-ray2.50A1-328[»]
4H27X-ray1.30A1-328[»]
ProteinModelPortalP20132.
SMRP20132. Positions 4-322.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000257549.

Chemistry

DrugBankDB00133. L-Serine.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteP20132.

Polymorphism databases

DMDM229462819.

Proteomic databases

PaxDbP20132.
PRIDEP20132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257549; ENSP00000257549; ENSG00000135094.
GeneID10993.
KEGGhsa:10993.
UCSCuc001tvg.3. human.

Organism-specific databases

CTD10993.
GeneCardsGC12M113830.
HGNCHGNC:10691. SDS.
HPAHPA039230.
MIM182128. gene.
neXtProtNX_P20132.
PharmGKBPA35616.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1171.
HOGENOMHOG000046976.
HOVERGENHBG017784.
InParanoidP20132.
KOK17989.
OMAGWIYVPP.
OrthoDBEOG7VDXQ1.
PhylomeDBP20132.
TreeFamTF329014.

Enzyme and pathway databases

BioCycMetaCyc:HS05952-MONOMER.
BRENDA4.3.1.17. 2681.
SABIO-RKP20132.
UniPathwayUPA00138.

Gene expression databases

ArrayExpressP20132.
BgeeP20132.
CleanExHS_SDS.
GenevestigatorP20132.

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

ChiTaRSSDS. human.
EvolutionaryTraceP20132.
GenomeRNAi10993.
NextBio41775.
PROP20132.
SOURCESearch...

Entry information

Entry nameSDHL_HUMAN
AccessionPrimary (citable) accession number: P20132
Secondary accession number(s): A8K9P5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 135 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

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