Reviewed, UniProtKB/Swiss-Prot Q870G1 (LYS1_EMENI)

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:	lysA
ORF Names:	AN2873-A

Organism

Emericella nidulans (Aspergillus nidulans)

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 (fungi route): step 3/3.
Subunit structure	Monomer By similarity.
Sequence similarities	Belongs to the AlaDH/PNT family.
Sequence caution	The sequence AAL23682.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAA63444.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene AN2873 has been split into 2 genes: lysA and ubp16.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Lysine biosynthesis
Ligand	NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	lysine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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 – 375	375	Saccharopine dehydrogenase [NAD+, L-lysine-forming]		PRO_0000199012
Sites
	Active site	205	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q870G1-1 [UniParc]. Last modified May 26, 2009. Version 2. Checksum: 02C6DFBEFFCB54C4	FASTA	375	41,098
	10 20 30 40 50 60 MGSNKIWLRA ETKPAEARSA LTPTTCKALI DAGYEVTVER STQRIFDDDE FAKVGAPLVE 70 80 90 100 110 120 EGSWVKDAPK DAYILGLKEL PEDDFPLEHV HISFAHCYKE QAGWEKVLSR WPRGGGVLLD 130 140 150 160 170 180 LEFLTDDAGR RVAAFGFSAG YAGAALAVKN WAWQLTHPEG EPLAGEKPYA NQDLLIQSVK 190 200 210 220 230 240 ESLQAGQKQS GKSPKILVIG ALGRCGKGAV QLAKDVGIPE SDIIQWDMEE TKKGGPFKEI 250 260 270 280 290 300 VEDADIFVNC IYLSSKIPHF VNVESLSTPS RRLSVICDVS ADTTNPNNPI PVYNITTTFD 310 320 330 340 350 360 KPTVPVTLPN GTQGTPLSVI SIDHLPSLLP RESSEMFSEA LMPSLLQLKD RENARVWKQA 370 EDLFNQKVAT LPQTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Impact of the cross-pathway control on the regulation of lysine and penicillin biosynthesis in Aspergillus nidulans." Busch S., Bode H.B., Brakhage A.A., Braus G.H. Curr. Genet. 42:209-219(2003) [PubMed: 12589472] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY057447 Genomic DNA. Translation: AAL23682.1. Sequence problems. AACD01000051 Genomic DNA. Translation: EAA63444.1. Sequence problems.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.5.1.7. 3859.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

LYS1_EMENI

Accession

Primary (citable) accession number: Q870G1
Secondary accession number(s): Q5B9A7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	May 26, 2009
Last modified:	June 16, 2009
This is version 27 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)