Reviewed, UniProtKB/Swiss-Prot Q09694 (LYS1_SCHPO)

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:	lys3
ORF Names:	SPAC227.18, SPAC2F7.01

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	368 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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 (fungi 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
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lysine biosynthetic process via aminoadipic acid Inferred from mutant phenotype. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro 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 – 368	368	Saccharopine dehydrogenase [NAD+, L-lysine-forming]		PRO_0000199014
Sites
	Active site	205	1	By similarity
Amino acid modifications
	Modified residue	85	1	Phosphoserine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q09694-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 789AB01DB171ED13	FASTA	368	41,393
	10 20 30 40 50 60 MVAPHLWLRA ETKPLEERSA LTPRTAKILA DAGFQITIER SSQRAFKDKE FERLGFPMVP 70 80 90 100 110 120 EGSWRHAPKD AYIIGLKELP ENDNSPLKHT HIQFAHCYKN QEGWREVLSR FPAGNGLLYD 130 140 150 160 170 180 LEFLQDDNGR RVAAFGYHAG FAGSAISCLV WAHQLLHPNK QFPAIRPFPN EKSLVRHVAR 190 200 210 220 230 240 QVRLALKKNN NQYPRILVIG ALGRCGTGAC DLASKIGIPF DNILRWDINE TKKGGPFTEI 250 260 270 280 290 300 TESDIFVNCI YLSMPIPKFC TVESLNVPNR KLRVVCDVSC DTTNPNNPIP IYNVNTTFDH 310 320 330 340 350 360 PTVEVKGVTT PPPLEVISID HLPTLLPRES SEAFSEALIP SLLALKDVDN APVWVRAKKL YETMVQKL

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAB61467.1.
PIR	S58145. T38549. T50174.
RefSeq	NP_592972.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2541500.
KEGG	spo:SPAC227.18.
NMPDR	fig|4896.1.peg.2942.
Organism-specific databases
GeneDB_Spombe	SPAC227.18.
Phylogenomic databases
OMA	Q09694. IGALGRC.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001980-MON.
BRENDA	1.5.1.7. 653.
Gene expression databases
ArrayExpress	Q09694.
Family and domain databases
InterPro	IPR007698. Ala_DH/PNT_C. IPR007886. Ala_DH/PNT_N. [Graphical view]
Pfam	PF01262. AlaDh_PNT_C. 1 hit. PF05222. AlaDh_PNT_N. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LYS1_SCHPO

Accession

Primary (citable) accession number: Q09694
Secondary accession number(s): Q9UTC1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	December 1, 2000
Last modified:	June 16, 2009
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)