P20132 (SDHL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	328 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 Ref.4 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 Reference proteome
Gene Ontology (GO)
Biological_process	L-serine catabolic process Inferred from direct assay PubMed 15689518Ref.4. Source: UniProtKB gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-UniPathway pyruvate biosynthetic process Inferred from direct assay PubMed 15689518. Source: UniProtKB response to amino acid stimulus Inferred from electronic annotation. Source: Compara response to cobalamin Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrion Inferred from direct assay. Source: HPA
Molecular_function	L-serine ammonia-lyase activity Inferred from direct assay PubMed 15689518Ref.4. Source: UniProtKB L-threonine ammonia-lyase activity Inferred from electronic annotation. Source: EC protein homodimerization activity Inferred from direct assay PubMed 15689518. Source: UniProtKB pyridoxal phosphate binding Inferred from direct assay PubMed 15689518. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 328

327

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

25 – 31

7

Helix

32 – 34

3

Helix

36 – 38

3

Helix

41 – 54

14

Beta strand

59 – 62

4

Helix

67 – 79

13

Beta strand

83 – 88

6

Helix

93 – 101

9

Beta strand

105 – 109

5

Helix

115 – 126

12

Beta strand

130 – 133

4

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 – 236

7

Beta strand

241 – 246

6

Helix

248 – 262

15

Helix

268 – 278

11

Helix

281 – 287

7

Beta strand

297 – 302

6

Helix

310 – 319

10

Sequences

	Sequence		Length	Mass (Da)
	P20132 [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] [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]	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] [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.

IPI

IPI00022201.

PIR

DWHUT. A34232.

RefSeq

NP_006834.2. NM_006843.2.

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	[»]
4H27	X-ray	1.30	A	1-328	[»]

ProteinModelPortal

P20132.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000257549.

PTM databases

PhosphoSite

P20132.

Polymorphism databases

DMDM

229462819.

Proteomic databases

PaxDb

P20132.

PRIDE

P20132.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000257549; ENSP00000257549; ENSG00000135094.

GeneID

10993.

KEGG

hsa:10993.

UCSC

uc001tvg.3. human.

Organism-specific databases

CTD

10993.

GeneCards

GC12M113830.

HGNC

HGNC:10691. SDS.

HPA

HPA039230.

MIM

182128. gene.

neXtProt

NX_P20132.

PharmGKB

PA35616.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1171.

HOGENOM

HOG000046976.

HOVERGEN

HBG017784.

InParanoid

P20132.

KO

K01752.

OMA

WVYISPF.

OrthoDB

EOG4PZJ79.

PhylomeDB

P20132.

Enzyme and pathway databases

BRENDA

4.3.1.17. 2681.

SABIO-RK

P20132.

UniPathway

UPA00138.

Gene expression databases

ArrayExpress

P20132.

Bgee

P20132.

CleanEx

HS_SDS.

Genevestigator

P20132.

GermOnline

ENSG00000135094. Homo sapiens.

Family and domain databases

InterPro

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

Pfam

PF00291. PALP. 1 hit.
[Graphical view]

SUPFAM

SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.

PROSITE

PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SDS. human.

DrugBank

DB00133. L-Serine.
DB00114. Pyridoxal Phosphate.

EvolutionaryTrace

P20132.

GenomeRNAi

10993.

NextBio

41775.

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:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.