[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Sigma 1278B; Feller A.; Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169870 [NCBI, ExPASy, EBI, Israel, Japan] Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."; Nature 387:84-87(1997).
[3]	PROTEIN SEQUENCE OF 2-9; 36-65; 132-149; 193-204; 216-225 AND 313-327, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY. Bienvenut W.V., Peters C.; Submitted (JUN-2005) to UniProtKB.
[4]	PROTEIN SEQUENCE OF 2-3, CLEAVAGE OF INITIATOR METHIONINE, SUBUNIT, AND ENZYME REGULATION. PubMed=418069 [NCBI, ExPASy, EBI, Israel, Japan] Ogawa H., Fujioka M.; "Purification and characterization of saccharopine dehydrogenase from baker's yeast."; J. Biol. Chem. 253:3666-3670(1978).
[5]	PROTEIN SEQUENCE OF 203-212. DOI=10.1016/0005-2795(80)90024-0; PubMed=6769500 [NCBI, ExPASy, EBI, Israel, Japan] Ogawa H., Hase T., Fujioka M.; "Amino acid sequence of a peptide containing an essential cysteine residue of yeast saccharopine dehydrogenase (L-lysine-forming)."; Biochim. Biophys. Acta 623:225-228(1980).
[6]	BIOPHYSICOCHEMICAL PROPERTIES. PubMed=4287986 [NCBI, ExPASy, EBI, Israel, Japan] Saunders P.P., Broquist H.P.; "Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. IV. Saccharopine dehydrogenase."; J. Biol. Chem. 241:3435-3440(1966).
[7]	BIOPHYSICOCHEMICAL PROPERTIES. PubMed=4318475 [NCBI, ExPASy, EBI, Israel, Japan] Fujioka M., Nakatani Y.; "A kinetic study of saccharopine dehydrogenase reaction."; Eur. J. Biochem. 16:180-186(1970).
[8]	ACTIVE SITE. PubMed=378997 [NCBI, ExPASy, EBI, Israel, Japan] Ogawa H., Okamoto M., Fujioka M.; "Chemical modification of the active site sulfhydryl group of saccharopine dehydrogenase (L-lysine-forming)."; J. Biol. Chem. 254:7030-7035(1979).
[9]	ENZYME REGULATION. PubMed=6985909 [NCBI, ExPASy, EBI, Israel, Japan] Fujioka M., Takata Y., Ogawa H., Okamoto M.; "The inactivation of saccharopine dehydrogenase (L-lysine-forming) by diethyl pyrocarbonate."; J. Biol. Chem. 255:937-942(1980).
[10]	ENZYME REGULATION. PubMed=6771291 [NCBI, ExPASy, EBI, Israel, Japan] Ogawa H., Fujioka M.; "The reaction of pyridoxal 5'-phosphate with an essential lysine residue of saccharopine dehydrogenase (L-lysine-forming)."; J. Biol. Chem. 255:7420-7425(1980).
[11]	INDUCTION. PubMed=3123231 [NCBI, ExPASy, EBI, Israel, Japan] Ramos F., Dubois E., Pierard A.; "Control of enzyme synthesis in the lysine biosynthetic pathway of Saccharomyces cerevisiae. Evidence for a regulatory role of gene LYS14."; Eur. J. Biochem. 171:171-176(1988).
[12]	SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan] Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.; "Global analysis of protein localization in budding yeast."; Nature 425:686-691(2003).
[13]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).

Comments

FUNCTION: Catalyzes the NAD(+)-dependent cleavage of saccharopine to L-lysine and 2-oxoglutarate.
CATALYTIC ACTIVITY: N⁶-(L-1,3-dicarboxypropyl)-L-lysine + NAD⁺ + H₂O = L-lysine + 2-oxoglutarate + NADH.
ENZYME REGULATION: Inhibited by p-chloromercuribenzoate and iodoacetate by modification of the active site cysteine residue. Inhibited by diethyl pyrocarbonate by modification of histidine residues. Inhibited by pyridoxal 5'-phsophate by modification of an essential lysine residue.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=0.089 mM for NADH;
	K_M=0.1 mM for NAD⁺;
	K_M=1.67 mM for saccharopine;
	K_M=0.55 mM for 2-oxoglutarate;
	K_M=2.0 mM for L-lysine;
pH dependence:	Optimum pH is 10 for the forward reaction, and 6.5-7 for the reverse reaction;

PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungi route): step 3/3 .
SUBUNIT: Monomer.
INTERACTION:
P53112:PEX14; NbExp=1; IntAct=EBI-10264, EBI-13212;
P33203:PRP40; NbExp=1; IntAct=EBI-10264, EBI-701;
P39940:RSP5; NbExp=1; IntAct=EBI-10264, EBI-16219;
P40318:SSM4; NbExp=1; IntAct=EBI-10264, EBI-18208;
SUBCELLULAR LOCATION: Cytoplasm.
INDUCTION: Induced by alpha-aminoadipate semialdehyde in a LYS14-dependent manner. Repressed by lysine.
MISCELLANEOUS: Present with 111934 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the AlaDH/PNT family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X77362; CAA54551.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z38061; CAA86194.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S48496; S48496.

RefSeq

NP_012300.1; -.

3D structure databases

PDB

2Q99; X-ray; 1.64 A; A=1-373.	[ExPASy / RCSB / EBI]
2QRJ; X-ray; 1.60 A; A=1-373.	[ExPASy / RCSB / EBI]
2QRK; X-ray; 1.75 A; A=1-373.	[ExPASy / RCSB / EBI]
2QRL; X-ray; 1.60 A; A=1-373.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2Q99; -.
2QRJ; -.
2QRK; -.
2QRL; -.

ModBase

P38998.

Protein-protein interaction databases

DIP

DIP:5291N; -.

IntAct

P38998; -.

Organism-specific databases

YIR034c; -.

S000001473; LYS1.

Gene expression databases

GermOnline

YIR034C; Saccharomyces cerevisiae.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004754;	Molecular function: saccharopine dehydrogenase (NAD+, L-lysine-forming) activity (inferred from electronic annotation from EC).
GO:0019878;	Biological process: lysine biosynthetic process via aminoadipic acid (traceable author statement from SGD).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR007698; Ala_DHase/PNT_C.
IPR007886; Ala_DHase/PNT_N.
Graphical view of domain structure.

Pfam

PF01262; AlaDh_PNT_C; 1.
PF05222; AlaDh_PNT_N; 1.
Pfam graphical view of domain structure.

ProtoNet

P38998.

Proteomic databases

PeptideAtlas

P38998; -.

Genome annotation databases

Ensembl

YIR034C; Saccharomyces cerevisiae. [Contig view]

854852; -.

Z47047_GR; YIR034C.

sce:YIR034C; -.

fig|4932.3.peg.1844; -.

Phylogenomic databases

HOGENOM

P38998; -.

Other

LinkHub

P38998; -.

NextBio

977755; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Amino-acid biosynthesis; Complete proteome; Cytoplasm; Direct protein sequencing; Lysine biosynthesis; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 373`	`372`	`Saccharopine dehydrogenase [NAD+, L-lysine-forming].`	`PRO_0000199016`
`ACT_SITE`	`205 205`
`MOD_RES`	`2 2`		`N-acetylalanine; partial.`
`CONFLICT`	`209 209`		`A -> AL (in Ref. 5; AA sequence).`
`CONFLICT`	`309 309`		`A -> V (in Ref. 1; CAA54551).`
`STRAND`	`5 8`	`4`
`HELIX`	`23 31`	`9`
`STRAND`	`35 39`	`5`
`STRAND`	`44 46`	`3`
`HELIX`	`48 53`	`6`
`STRAND`	`57 59`	`3`
`HELIX`	`63 66`	`4`
`STRAND`	`71 74`	`4`
`STRAND`	`89 93`	`5`
`HELIX`	`104 114`	`11`
`STRAND`	`117 120`	`4`
`HELIX`	`121 123`	`3`
`HELIX`	`136 156`	`21`
`HELIX`	`172 188`	`17`
`STRAND`	`196 200`	`5`
`HELIX`	`204 216`	`13`
`HELIX`	`220 222`	`3`
`STRAND`	`223 226`	`4`
`HELIX`	`228 231`	`4`
`HELIX`	`239 242`	`4`
`STRAND`	`243 248`	`6`
`HELIX`	`262 265`	`4`
`STRAND`	`274 277`	`4`
`STRAND`	`308 311`	`4`
`STRAND`	`314 316`	`3`
`HELIX`	`321 324`	`4`
`HELIX`	`326 341`	`16`
`HELIX`	`342 346`	`5`
`TURN`	`347 349`	`3`
`HELIX`	`351 364`	`14`
`HELIX`	`370 372`	`3`

Sequence information

Length: 373 AA [This is the length of the unprocessed precursor]

Molecular weight: 41465 Da [This is the MW of the unprocessed precursor]

CRC64: 7E3A810876C1DC41 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVTLHLRA ETKPLEARAA LTPTTVKKLI AKGFKIYVED SPQSTFNINE YRQAGAIIVP 

        70         80         90        100        110        120 
AGSWKTAPRD RIIIGLKEMP ETDTFPLVHE HIQFAHCYKD QAGWQNVLMR FIKGHGTLYD 

       130        140        150        160        170        180 
LEFLENDQGR RVAAFGFYAG FAGAALGVRD WAFKQTHSDD EDLPAVSPYP NEKALVKDVT 

       190        200        210        220        230        240 
KDYKEALATG ARKPTVLIIG ALGRCGSGAI DLLHKVGIPD ANILKWDIKE TSRGGPFDEI 

       250        260        270        280        290        300 
PQADIFINCI YLSKPIAPFT NMEKLNNPNR RLRTVVDVSA DTTNPHNPIP IYTVATVFNK 

       310        320        330        340        350        360 
PTVLVPTTAG PKLSVISIDH LPSLLPREAS EFFSHDLLPS LELLPQRKTA PVWVRAKKLF 

       370 
DRHCARVKRS SRL

P38998 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools