P38997 (LYS1_YARLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Saccharopine dehydrogenase [NAD(+), L-lysine-forming]
Short name=SDH
EC=1.5.1.7

Alternative name(s):
Lysine--2-oxoglutarate reductase

Gene names

Name:	LYS5
Ordered Locus Names:	YALI0B15444g

Organism

Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) [Reference proteome]

Taxonomic identifier

284591 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia › Yarrowia lipolytica

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH.
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 3/3.
Sequence similarities	Belongs to the AlaDH/PNT family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Lysine biosynthesis
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lysine biosynthetic process via aminoadipic acid Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	saccharopine dehydrogenase (NAD+, L-lysine-forming) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 369	369	Saccharopine dehydrogenase [NAD(+), L-lysine-forming]		PRO_0000199015
Sites
	Active site	205	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P38997 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: B1B749FA008B8A36	FASTA	369	40,612
	10 20 30 40 50 60 MTAPVKLHLR AETKPLEHRS ALTPTTTRKL LDAGFEVFVE KSPLRIFDDQ EFVDVGATLV 70 80 90 100 110 120 EEGSWVSAPE DRMIIGLKEL PEESFPLSHE HIQFAHCYKD QGGWKDVLSR FPAGNGTLYD 130 140 150 160 170 180 LEFLEDDNGR RVAAFGFHAG FAGAAIGVET WAFQQTHPDS ENLPGVSAYP NETELVDKIK 190 200 210 220 230 240 KDLAAAVEKG SKLPTVLVIG ALGRCGSGAI DLARKVGIPE ENIIRWDMNE TKKGGPFQEI 250 260 270 280 290 300 ADADIFINCI YLSQPIPPFI NYDLLNKETR KLSVIVDVSA DTTNPHNPVP VYTIATTFDH 310 320 330 340 350 360 PTVPVETTAG PKLSVCSIDH LPSLLPREAS EAFSEALLPS LLQLPQRDTA PVWTRAKALF DKHVLRIGE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Overlapping reading frames at the LYS5 locus in the yeast Yarrowia lipolytica." Xuan J.-W., Fournier P., Declerck N., Chasles M., Gaillardin C. Mol. Cell. Biol. 10:4795-4806(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 20460 / W29 / CBS 7504 / IFP29.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M34929 Genomic DNA. Translation: AAA35248.1. CR382128 Genomic DNA. Translation: CAG83182.1.
PIR	A36467.
RefSeq	XP_500931.1. XM_500931.1.
3D structure databases
ProteinModelPortal	P38997.
SMR	P38997. Positions 3-367.
ModBase	Search...
Protein-protein interaction databases
STRING	4952.P38997.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2907616.
KEGG	yli:YALI0B15444g.
Phylogenomic databases
eggNOG	NOG79735.
HOGENOM	HOG000143704.
KO	K00290.
OMA	QFAHCYK.
OrthoDB	EOG408RHS.
Enzyme and pathway databases
UniPathway	UPA00033; UER00034.
Family and domain databases
InterPro	IPR007886. AlaDH/PNT_N. IPR007698. AlaDH/PNT_NAD(H)-bd. IPR027281. Lys1. [Graphical view]
PANTHER	PTHR11133:SF4. PTHR11133:SF4. 1 hit.
Pfam	PF01262. AlaDh_PNT_C. 1 hit. PF05222. AlaDh_PNT_N. 1 hit. [Graphical view]
PIRSF	PIRSF018250. Saccharopine_DH_Lys. 1 hit.
SMART	SM01002. AlaDh_PNT_C. 1 hit. SM01003. AlaDh_PNT_N. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LYS1_YARLI

Accession

Primary (citable) accession number: P38997

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program