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P20132

- SDHL_HUMAN

UniProt

P20132 - SDHL_HUMAN

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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

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

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
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: Chromosome 12

Organism-specific databases

HGNCiHGNC:10691. SDS.

Subcellular locationi

GO - Cellular componenti

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

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.
GenevestigatoriP20132.

Organism-specific databases

HPAiHPA039230.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi116189. 1 interaction.
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.
OMAiGWIYVPP.
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.

Polymorphism databases

DMDMi229462819.

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 .
CCDSi CCDS9169.1.
PIRi A34232. DWHUT.
RefSeqi NP_006834.2. NM_006843.2.
UniGenei Hs.439023.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

BioGridi 116189. 1 interaction.
STRINGi 9606.ENSP00000257549.

Chemistry

DrugBanki DB00133. L-Serine.

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.
GeneTreei ENSGT00550000074775.
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

Bgeei P20132.
CleanExi HS_SDS.
ExpressionAtlasi P20132. baseline and differential.
Genevestigatori P20132.

Family and domain databases

InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. TrpB-like_PLP-dep.
[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

« 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. "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: November 26, 2014
This is version 140 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