Reviewed, UniProtKB/Swiss-Prot P09367 (SDHL_RAT)

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

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	363 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. L-threonine = 2-oxobutanoate + NH3.
Cofactor	Pyridoxal phosphate.
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Induction	By glucocorticoids and glucagon.
Sequence similarities	Belongs to the serine/threonine dehydratase family.

Ontologies

Keywords
Biological process	Gluconeogenesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	Pyridoxal phosphate
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro gluconeogenesis Traceable author statement. Source: RGD response to amino acid stimulus Inferred from expression pattern. Source: RGD response to cobalamin Inferred from expression pattern. Source: RGD
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-serine ammonia-lyase activity Traceable author statement. Source: RGD L-threonine ammonia-lyase activity Inferred from electronic annotation. Source: EC protein dimerization activity Inferred from direct assay. Source: RGD pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P09367-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P09367-2)

The sequence of this isoform differs from the canonical sequence as follows:
     65-100: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5 Ref.6

Chain

2 – 363

362

L-serine dehydratase/L-threonine deaminase

PRO_0000185596

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Modified residue

41

1

N6-(pyridoxal phosphate)lysine

Natural variations

Alternative sequence

65 – 100

36

Missing in isoform 2.

VSP_024798

Experimental info

Sequence conflict

12

1

P → T AA sequence Ref.5

Sequence conflict

16

1

S → T in AAA42123. Ref.1

Sequence conflict

164

1

P → Q in AAA42123. Ref.1

Sequence conflict

276

1

P → T AA sequence Ref.5

Sequence conflict

325

1

G → A in CAA68721. Ref.3

Secondary structure

1

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363

Helix Strand Turn

Details...

Beta strand

13 – 15

3

Helix

17 – 23

7

Beta strand

27 – 30

4

Helix

32 – 34

3

Helix

42 – 54

13

Beta strand

59 – 62

4

Helix

103 – 114

12

Beta strand

119 – 123

5

Helix

129 – 136

8

Turn

137 – 139

3

Beta strand

141 – 144

4

Helix

149 – 162

14

Beta strand

166 – 168

3

Turn

171 – 173

3

Helix

175 – 181

7

Helix

183 – 191

9

Beta strand

199 – 202

4

Helix

207 – 219

13

Beta strand

226 – 231

6

Beta strand

243 – 245

3

Helix

251 – 259

9

Helix

264 – 274

11

Beta strand

277 – 282

6

Helix

284 – 298

15

Helix

304 – 314

11

Helix

317 – 323

7

Beta strand

324 – 327

4

Beta strand

334 – 337

4

Helix

346 – 355

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C94FFF2EB9C6E33C	FASTA	363	38,433
	10 20 30 40 50 60 MAAQESLHVK TPLRDSMALS KVAGTSVFLK MDSSQPSGSF KIRGIGHLCK MKAKQGCKHF 70 80 90 100 110 120 VCSSVVQIWG SRMRGRSHSG DEQPHVRSQA LLPDTPSPLT AGNAGMATAY AARRLGLPAT 130 140 150 160 170 180 IVVPSTTPAL TIERLKNEGA TVEVVGEMLD EAIQLAKALE KNNPGWVYIS PFDDPLIWEG 190 200 210 220 230 240 HTSLVKELKE TLSAKPGAIV LSVGGGGLLC GVVQGLREVG WEDVPIIAME TFGAHSFHAA 250 260 270 280 290 300 VKEGKLVTLP KITSVAKALG VNTVGAQTLK LFYEHPIFSE VISDQEAVTA IEKFVDDEKI 310 320 330 340 350 360 LVEPACGAAL AAVYSGVVCR LQAEGRLQTP LASLVVIVCG GSNISLAQLQ ALKAQLGLNE LLK
	Isoform 2. Checksum: 525C043E62BDF388	FASTA	327	34,454
	10 20 30 40 50 60 MAAQESLHVK TPLRDSMALS KVAGTSVFLK MDSSQPSGSF KIRGIGHLCK MKAKQGCKHF 70 80 90 100 110 120 VCSSAGNAGM ATAYAARRLG LPATIVVPST TPALTIERLK NEGATVEVVG EMLDEAIQLA 130 140 150 160 170 180 KALEKNNPGW VYISPFDDPL IWEGHTSLVK ELKETLSAKP GAIVLSVGGG GLLCGVVQGL 190 200 210 220 230 240 REVGWEDVPI IAMETFGAHS FHAAVKEGKL VTLPKITSVA KALGVNTVGA QTLKLFYEHP 250 260 270 280 290 300 IFSEVISDQE AVTAIEKFVD DEKILVEPAC GAALAAVYSG VVCRLQAEGR LQTPLASLVV 310 320 IVCGGSNISL AQLQALKAQL GLNELLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and nucleotide sequence of the cDNA for rat liver serine dehydratase mRNA and structures of the 5' and 3' flanking regions of the serine dehydratase gene." Ogawa H., Miller D.A., Dunn T., Su Y., Burcham J.M., Peraino C., Fujioka M., Babcock K., Pitot H.C. Proc. Natl. Acad. Sci. U.S.A. 85:5809-5813(1988) [PubMed: 3413060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Sequence of the rat serine dehydratase gene." Ogawa H., Su Y., Dunn T., Miller D.A., Matsuda Y., Fujioka M., Pitot H.C. Nucleic Acids Res. 16:10921-10923(1988) [PubMed: 3205731] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Primary structure of rat liver serine dehydratase deduced from the cDNA sequence." Noda C., Ito K., Nakamura T., Ichihara A. FEBS Lett. 234:331-335(1988) [PubMed: 3391277] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Liver.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Liver.
[5]	"Primary structure of rat liver L-threonine deaminase." Leoncini R., Henschen A., Krieglstein K., Calvete J.J., Pagani R., Marinello E. Ital. J. Biochem. 39:228-234(1990) [PubMed: 2228554] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-363 (ISOFORM 2). Strain: Wistar. Tissue: Liver.
[6]	"The peptide sequences near the bound pyridoxal phosphate are conserved in serine dehydratase from rat liver, and threonine dehydratases from yeast and Escherichia coli." Ogawa H., Konishi K., Fujioka M. Biochim. Biophys. Acta 996:139-141(1989) [PubMed: 2660911] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5 AND 31-50. Tissue: Liver.
[7]	"Amino acid sequence around the pyridoxal 5'-phosphate binding site of rat liver L-threonine deaminase." Leoncini R., Henschen A., Krieglstein K., Calvete J.J., Pagani R., Marinello E. Ital. J. Biochem. 39:235-241(1990) [PubMed: 2228555] [Abstract] Cited for: PYRIDOXAL PHOSPHATE AT LYS-41.
[8]	"Properties of rat liver L-threonine deaminase." Pagani R., Leoncini R., Pizzichini M., Vannoni D., Tabucci A., Marinello E. Enzyme Protein 48:90-97(1995) [PubMed: 7581747] [Abstract] Cited for: CHARACTERIZATION. Tissue: Liver.
[9]	"Crystal structure of serine dehydratase from rat liver." Yamada T., Komoto J., Takata Y., Ogawa H., Pitot H.C., Takusagawa F. Biochemistry 42:12854-12865(2003) [PubMed: 14596599] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J03863 mRNA. Translation: AAA42123.1.
X13119 Genomic DNA. Translation: CAA31511.1.
Y00752 mRNA. Translation: CAA68721.1.
BC088110 mRNA. Translation: AAH88110.1.

IPI

IPI00193769.
IPI00231470.

PIR

DWRTT. S01009.
S01973.

RefSeq

NP_446414.3.

UniGene

Rn.9918

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PWE	X-ray	2.80	A/B/C/D/E/F	1-363	[»]
1PWH	X-ray	2.60	A/B/C/D	1-363	[»]
1RSQ	model	-	A	9-363	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P09367.

Proteomic databases

PRIDE

P09367.

Genome annotation databases

Ensembl

ENSRNOT00000001875; ENSRNOP00000001875; ENSRNOG00000001388; Rattus norvegicus. [Genome view]
ENSRNOT00000001876; ENSRNOP00000001876; ENSRNOG00000001388; Rattus norvegicus. [Genome view]

GeneID

25044.

KEGG

rno:25044.

UCSC

BC088110. rat.

Organism-specific databases

CTD

25044.

RGD

67376. Sds.

Phylogenomic databases

HOVERGEN

P09367.

Enzyme and pathway databases

BRENDA

4.3.1.17. 248.
4.3.1.19. 248.

Gene expression databases

ArrayExpress

P09367.

Genevestigator

P09367.

GermOnline

ENSRNOG00000001388. Rattus norvegicus.

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

NextBio

605215.

Entry information

Entry name

SDHL_RAT

Accession

Primary (citable) accession number: P09367
Secondary accession number(s): Q5M8C4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)