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

Saccharopine dehydrogenase [NADP(+), L-glutamate-forming]

Gene

LYS9

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH.

Pathway:iL-lysine biosynthesis via AAA pathway

This protein is involved in step 2 of the subpathway that synthesizes L-lysine from L-alpha-aminoadipate (fungal route).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. L-aminoadipate-semialdehyde dehydrogenase (LYS2)
  2. Saccharopine dehydrogenase [NADP(+), L-glutamate-forming] (LYS9)
  3. Saccharopine dehydrogenase [NAD(+), L-lysine-forming] (LYS1)
This subpathway is part of the pathway L-lysine biosynthesis via AAA pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-lysine from L-alpha-aminoadipate (fungal route), the pathway L-lysine biosynthesis via AAA pathway and in Amino-acid biosynthesis.

GO - Molecular functioni

  • saccharopine dehydrogenase (NADP+, L-glutamate-forming) activity Source: SGD

GO - Biological processi

  • lysine biosynthetic process via aminoadipic acid Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Lysine biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-363.
ReactomeiREACT_347776. Lysine catabolism.
UniPathwayiUPA00033; UER00033.

Names & Taxonomyi

Protein namesi
Recommended name:
Saccharopine dehydrogenase [NADP(+), L-glutamate-forming] (EC:1.5.1.10)
Alternative name(s):
Saccharopine reductase
Gene namesi
Name:LYS9
Synonyms:LYS13
Ordered Locus Names:YNR050C
ORF Names:N3461
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNR050c.
EuPathDBiFungiDB:YNR050C.
SGDiS000005333. LYS9.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446Saccharopine dehydrogenase [NADP(+), L-glutamate-forming]PRO_0000212839Add
BLAST

Proteomic databases

MaxQBiP38999.
PaxDbiP38999.
PeptideAtlasiP38999.

Interactioni

Subunit structurei

Interacts with TRM112.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself1EBI-10294,EBI-10294

Protein-protein interaction databases

BioGridi35875. 16 interactions.
DIPiDIP-776N.
IntActiP38999. 9 interactions.
MINTiMINT-425978.

Structurei

Secondary structure

1
446
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi14 – 229Combined sources
Beta strandi27 – 359Combined sources
Helixi36 – 438Combined sources
Turni44 – 474Combined sources
Beta strandi49 – 524Combined sources
Helixi58 – 669Combined sources
Beta strandi68 – 736Combined sources
Helixi77 – 793Combined sources
Helixi80 – 9011Combined sources
Beta strandi93 – 964Combined sources
Helixi102 – 11413Combined sources
Beta strandi117 – 1193Combined sources
Turni124 – 1263Combined sources
Helixi128 – 14215Combined sources
Beta strandi146 – 15813Combined sources
Helixi160 – 1623Combined sources
Beta strandi171 – 1733Combined sources
Helixi176 – 1805Combined sources
Helixi181 – 1833Combined sources
Beta strandi186 – 1905Combined sources
Beta strandi193 – 1975Combined sources
Turni199 – 2013Combined sources
Helixi202 – 2054Combined sources
Beta strandi217 – 2215Combined sources
Helixi228 – 2314Combined sources
Beta strandi238 – 24710Combined sources
Helixi250 – 25910Combined sources
Turni260 – 2634Combined sources
Helixi269 – 2713Combined sources
Helixi277 – 2859Combined sources
Beta strandi288 – 2914Combined sources
Helixi292 – 3009Combined sources
Helixi308 – 32013Combined sources
Turni321 – 3244Combined sources
Helixi335 – 34612Combined sources
Beta strandi355 – 36612Combined sources
Beta strandi372 – 38211Combined sources
Helixi390 – 40718Combined sources
Beta strandi414 – 4174Combined sources
Helixi422 – 43615Combined sources
Beta strandi441 – 4444Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AXQX-ray1.70A1-446[»]
ProteinModelPortaliP38999.
SMRiP38999. Positions 2-446.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38999.

Family & Domainsi

Sequence similaritiesi

Belongs to the saccharopine dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1748.
GeneTreeiENSGT00390000013249.
HOGENOMiHOG000023158.
InParanoidiP38999.
KOiK00293.
OMAiDMIVMYH.
OrthoDBiEOG7FJH8S.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR005097. Saccharopine_DH/HSpermid_syn.
[Graphical view]
PfamiPF03435. Saccharop_dh. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38999-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKNVLLLGS GFVAQPVIDT LAANDDINVT VACRTLANAQ ALAKPSGSKA
60 70 80 90 100
ISLDVTDDSA LDKVLADNDV VISLIPYTFH PNVVKSAIRT KTDVVTSSYI
110 120 130 140 150
SPALRELEPE IVKAGITVMN EIGLDPGIDH LYAVKTIDEV HRAGGKLKSF
160 170 180 190 200
LSYCGGLPAP EDSDNPLGYK FSWSSRGVLL ALRNSAKYWK DGKIETVSSE
210 220 230 240 250
DLMATAKPYF IYPGYAFVCY PNRDSTLFKD LYHIPEAETV IRGTLRYQGF
260 270 280 290 300
PEFVKALVDM GMLKDDANEI FSKPIAWNEA LKQYLGAKST SKEDLIASID
310 320 330 340 350
SKATWKDDED RERILSGFAW LGLFSDAKIT PRGNALDTLC ARLEELMQYE
360 370 380 390 400
DNERDMVVLQ HKFGIEWADG TTETRTSTLV DYGKVGGYSS MAATVGYPVA
410 420 430 440
IATKFVLDGT IKGPGLLAPY SPEINDPIMK ELKDKYGIYL KEKTVA
Length:446
Mass (Da):48,918
Last modified:February 1, 1995 - v1
Checksum:i1EC4CE1CE3BCD916
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti393 – 3931A → T in AAT93229 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77363 Genomic DNA. Translation: CAA54552.1.
Z71665 Genomic DNA. Translation: CAA96331.1.
AY693210 Genomic DNA. Translation: AAT93229.1.
BK006947 Genomic DNA. Translation: DAA10591.1.
PIRiS41937.
RefSeqiNP_014448.1. NM_001183227.1.

Genome annotation databases

EnsemblFungiiYNR050C; YNR050C; YNR050C.
GeneIDi855786.
KEGGisce:YNR050C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77363 Genomic DNA. Translation: CAA54552.1.
Z71665 Genomic DNA. Translation: CAA96331.1.
AY693210 Genomic DNA. Translation: AAT93229.1.
BK006947 Genomic DNA. Translation: DAA10591.1.
PIRiS41937.
RefSeqiNP_014448.1. NM_001183227.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AXQX-ray1.70A1-446[»]
ProteinModelPortaliP38999.
SMRiP38999. Positions 2-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35875. 16 interactions.
DIPiDIP-776N.
IntActiP38999. 9 interactions.
MINTiMINT-425978.

Proteomic databases

MaxQBiP38999.
PaxDbiP38999.
PeptideAtlasiP38999.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNR050C; YNR050C; YNR050C.
GeneIDi855786.
KEGGisce:YNR050C.

Organism-specific databases

CYGDiYNR050c.
EuPathDBiFungiDB:YNR050C.
SGDiS000005333. LYS9.

Phylogenomic databases

eggNOGiCOG1748.
GeneTreeiENSGT00390000013249.
HOGENOMiHOG000023158.
InParanoidiP38999.
KOiK00293.
OMAiDMIVMYH.
OrthoDBiEOG7FJH8S.

Enzyme and pathway databases

UniPathwayiUPA00033; UER00033.
BioCyciYEAST:MONOMER3O-363.
ReactomeiREACT_347776. Lysine catabolism.

Miscellaneous databases

EvolutionaryTraceiP38999.
NextBioi980265.
PROiP38999.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR005097. Saccharopine_DH/HSpermid_syn.
[Graphical view]
PfamiPF03435. Saccharop_dh. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Feller A.
    Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 1278B.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
    Norbeck J., Blomberg A.
    FEMS Microbiol. Lett. 137:1-8(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 314-324.
    Strain: ATCC 38531 / Y41.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Trm11p and Trm112p are both required for the formation of 2-methylguanosine at position 10 in yeast tRNA."
    Purushothaman S.K., Bujnicki J.M., Grosjean H., Lapeyre B.
    Mol. Cell. Biol. 25:4359-4370(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRM112.

Entry informationi

Entry nameiLYS9_YEAST
AccessioniPrimary (citable) accession number: P38999
Secondary accession number(s): D6W1M5, E9P930
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 22, 2015
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 57500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.