Reviewed, UniProtKB/Swiss-Prot P20132 (SDHL_HUMAN)

Names and origin

Protein names

Recommended name:
    L-serine dehydratase/L-threonine deaminase
    EC=4.3.1.17
Alternative name(s):
    L-serine deaminase
    SDH
    L-threonine dehydratase
    EC=4.3.1.19
    TDH

Gene names

Name:	SDS
Synonyms:	SDH

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	328 AA.
Sequence status	Complete.
Protein existence	Evidence 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 KM=31 mM for threonine

Ontologies

Keywords
Biological process	Gluconeogenesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	L-serine catabolic process Ref.4 Inferred from direct assay. Source: UniProtKB gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW pyruvate biosynthetic process Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-serine ammonia-lyase activity Ref.4 Inferred from direct assay. Source: UniProtKB L-threonine ammonia-lyase activity Inferred from electronic annotation. Source: EC protein homodimerization activity Inferred from direct assay. Source: UniProtKB pyridoxal phosphate binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 328

328

L-serine dehydratase/L-threonine deaminase

PRO_0000185594

Amino acid modifications

Modified residue

41

1

N6-(pyridoxal phosphate)lysine

Experimental info

Mutagenesis

303

1

C → A: Loss of enzyme activity. Ref.4

Sequence conflict

89

1

S → G in AAA36604. Ref.1

Sequence conflict

106

1

V → C in AAA36604. Ref.1

Sequence conflict

183

1

V → C in AAA36604. Ref.1

Sequence conflict

230

1

A → S in AAA36604. Ref.1

Sequence conflict

270

1

C → W in AAA36604. Ref.1

Secondary structure

1

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328

Helix Strand Turn

Details...

Beta strand

13 – 16

4

Helix

17 – 23

7

Beta strand

27 – 30

4

Helix

32 – 34

3

Helix

36 – 38

3

Helix

42 – 54

13

Beta strand

59 – 62

4

Helix

67 – 79

13

Beta strand

83 – 87

5

Helix

93 – 101

9

Beta strand

105 – 108

4

Helix

113 – 126

14

Beta strand

130 – 132

3

Helix

139 – 145

7

Helix

147 – 155

9

Beta strand

161 – 166

6

Beta strand

168 – 170

3

Helix

171 – 182

12

Beta strand

190 – 195

6

Helix

200 – 207

8

Helix

221 – 223

3

Helix

230 – 238

9

Beta strand

241 – 246

6

Helix

248 – 261

14

Helix

268 – 278

11

Helix

281 – 287

7

Beta strand

298 – 301

4

Helix

310 – 320

11

Sequences

	Sequence		Length	Mass (Da)
	P20132-1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: F6E9AB01D6308C83	FASTA	328	34,625
	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

References

	« Hide 'large scale' referencesShow '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: 2674117] [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: 14702039] [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. , 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: 18342636] [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: 14646100] [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.

IPI

IPI00022201.

PIR

DWHUT. A34232.

RefSeq

NP_006834.2.

UniGene

Hs.439023

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P5J	X-ray	2.50	A	1-328	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P20132.

Genome annotation databases

Ensembl

ENST00000257549; ENSP00000257549; ENSG00000135094; Homo sapiens. [Genome view]

GeneID

10993.

KEGG

hsa:10993.

Organism-specific databases

CTD

10993.

GeneCards

GC12M112292.

HGNC

HGNC:10691. SDS.

MIM

182128. gene.

PharmGKB

PA35616.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17195.

HOGENOM

HBG714501.

HOVERGEN

P20132.

InParanoid

P20132.

OMA

ETFGAHS.

OrthoDB

EOG96HJWP.

PhylomeDB

P20132.

Enzyme and pathway databases

BRENDA

4.3.1.17. 247.

Gene expression databases

ArrayExpress

P20132.

Bgee

P20132.

CleanEx

HS_SDS.

Genevestigator

P20132.

GermOnline

ENSG00000135094. Homo sapiens.

Family and domain databases

InterPro

IPR001926. PyrdxlP-dep_enz_bsu.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
[Graphical view]

Pfam

PF00291. PALP. 1 hit.
[Graphical view]

PROSITE

PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00133. L-Serine.
DB00114. Pyridoxal Phosphate.

SOURCE

Search...

Entry information

Entry name

SDHL_HUMAN

Accession

Primary (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:	January 19, 2010
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.