Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

L-serine dehydratase/L-threonine deaminase

Gene

Sds

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-serine = pyruvate + NH3.
L-threonine = 2-oxobutanoate + NH3.

Cofactori

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

GO - Molecular functioni

  • L-serine ammonia-lyase activity Source: RGD
  • L-threonine ammonia-lyase activity Source: UniProtKB-EC
  • protein dimerization activity Source: RGD
  • pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  • cellular amino acid metabolic process Source: InterPro
  • gluconeogenesis Source: RGD
  • response to amino acid Source: RGD
  • response to cobalamin Source: RGD
  • response to nutrient levels Source: RGD

Keywordsi

Molecular functionLyase
Biological processGluconeogenesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BRENDAi4.3.1.17 5301
ReactomeiR-RNO-8849175 Threonine catabolism
SABIO-RKP09367
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi67376 Sds

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075240

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001855962 – 363L-serine dehydratase/L-threonine deaminaseAdd BLAST362

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei41N6-(pyridoxal phosphate)lysine1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP09367
PRIDEiP09367

PTM databases

iPTMnetiP09367

Expressioni

Inductioni

By glucocorticoids and glucagon.

Gene expression databases

BgeeiENSRNOG00000001388
ExpressionAtlasiP09367 baseline and differential
GenevisibleiP09367 RN

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • protein dimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001876

Structurei

Secondary structure

1363
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 15Combined sources3
Helixi17 – 23Combined sources7
Beta strandi27 – 30Combined sources4
Helixi32 – 34Combined sources3
Helixi42 – 54Combined sources13
Beta strandi59 – 63Combined sources5
Helixi103 – 114Combined sources12
Beta strandi119 – 123Combined sources5
Helixi129 – 137Combined sources9
Beta strandi141 – 144Combined sources4
Helixi149 – 161Combined sources13
Beta strandi166 – 169Combined sources4
Turni171 – 173Combined sources3
Helixi175 – 191Combined sources17
Beta strandi199 – 202Combined sources4
Beta strandi204 – 206Combined sources3
Helixi207 – 219Combined sources13
Beta strandi226 – 231Combined sources6
Helixi236 – 243Combined sources8
Helixi257 – 259Combined sources3
Helixi266 – 272Combined sources7
Turni273 – 276Combined sources4
Beta strandi277 – 282Combined sources6
Helixi284 – 298Combined sources15
Helixi304 – 314Combined sources11
Helixi317 – 323Combined sources7
Beta strandi324 – 327Combined sources4
Beta strandi334 – 337Combined sources4
Helixi346 – 355Combined sources10
Turni356 – 359Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PWEX-ray2.80A/B/C/D/E/F1-363[»]
1PWHX-ray2.60A/B/C/D1-363[»]
1RSQmodel-A9-363[»]
ProteinModelPortaliP09367
SMRiP09367
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09367

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1250 Eukaryota
COG1171 LUCA
GeneTreeiENSGT00550000074775
HOGENOMiHOG000046976
HOVERGENiHBG017784
InParanoidiP09367
KOiK17989
PhylomeDBiP09367

Family and domain databases

InterProiView protein in InterPro
IPR001926 PLP-dep
IPR000634 Ser/Thr_deHydtase_PyrdxlP-BS
IPR036052 Trypto_synt_PLP_dependent
PfamiView protein in Pfam
PF00291 PALP, 1 hit
SUPFAMiSSF53686 SSF53686, 2 hits
PROSITEiView protein in PROSITE
PS00165 DEHYDRATASE_SER_THR, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P09367-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAQESLHVK TPLRDSMALS KVAGTSVFLK MDSSQPSGSF KIRGIGHLCK
60 70 80 90 100
MKAKQGCKHF VCSSVVQIWG SRMRGRSHSG DEQPHVRSQA LLPDTPSPLT
110 120 130 140 150
AGNAGMATAY AARRLGLPAT IVVPSTTPAL TIERLKNEGA TVEVVGEMLD
160 170 180 190 200
EAIQLAKALE KNNPGWVYIS PFDDPLIWEG HTSLVKELKE TLSAKPGAIV
210 220 230 240 250
LSVGGGGLLC GVVQGLREVG WEDVPIIAME TFGAHSFHAA VKEGKLVTLP
260 270 280 290 300
KITSVAKALG VNTVGAQTLK LFYEHPIFSE VISDQEAVTA IEKFVDDEKI
310 320 330 340 350
LVEPACGAAL AAVYSGVVCR LQAEGRLQTP LASLVVIVCG GSNISLAQLQ
360
ALKAQLGLNE LLK
Length:363
Mass (Da):38,433
Last modified:January 23, 2007 - v3
Checksum:iC94FFF2EB9C6E33C
GO
Isoform 2 (identifier: P09367-2) [UniParc]FASTAAdd to basket

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

Show »
Length:327
Mass (Da):34,454
Checksum:i525C043E62BDF388
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12P → T AA sequence (PubMed:2228554).Curated1
Sequence conflicti16S → T in AAA42123 (PubMed:3413060).Curated1
Sequence conflicti164P → Q in AAA42123 (PubMed:3413060).Curated1
Sequence conflicti276P → T AA sequence (PubMed:2228554).Curated1
Sequence conflicti325G → A in CAA68721 (PubMed:3391277).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_02479865 – 100Missing in isoform 2. 2 PublicationsAdd BLAST36

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03863 mRNA Translation: AAA42123.1
X13119 Genomic DNA Translation: CAA31511.1
Y00752 mRNA Translation: CAA68721.1
BC088110 mRNA Translation: AAH88110.1
PIRiS01009 DWRTT
S01973
RefSeqiNP_446414.3, NM_053962.3 [P09367-2]
UniGeneiRn.9918

Genome annotation databases

EnsembliENSRNOT00000001875; ENSRNOP00000001875; ENSRNOG00000001388 [P09367-2]
GeneIDi25044
KEGGirno:25044

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiSDHL_RAT
AccessioniPrimary (citable) accession number: P09367
Secondary accession number(s): Q5M8C4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 156 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health