Reviewed, UniProtKB/Swiss-Prot Q99K67 (AASS_MOUSE)

Names and origin

Protein names

Recommended name:
    Alpha-aminoadipic semialdehyde synthase, mitochondrial
Alternative name(s):
    LKR/SDH
Including the following 2 domains:
    1- Recommended name:
            Lysine ketoglutarate reductase
                Short name=LKR
                Short name=LOR
              EC=1.5.1.8
    2- Recommended name:
            Saccharopine dehydrogenase
                Short name=SDH
              EC=1.5.1.9

Gene names

Name:	Aass
Synonyms:	Lorsdh

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	926 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-oxoglutarate reductase and saccharopine dehydrogenase activity, respectively.
Catalytic activity	N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-lysine + 2-oxoglutarate + NADPH. N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + 2-aminoadipate 6-semialdehyde + NADH.
Pathway	Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 1/6. Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 2/6.
Subunit structure	Homodimer.
Subcellular location	Mitochondrion.
Tissue specificity	Both enzymes are highly expressed in kidney and liver, very low expression is seen in heart, brain, spleen, lung, skeletal muscle and testis. SDH was detected only in cortical regions of the kidney.
Induction	Induced by starvation.
Sequence similarities	In the N-terminal section; belongs to the AlaDH/PNT family. In the C-terminal section; belongs to the saccharopine dehydrogenase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	L-lysine catabolic process Ref.1 Inferred from direct assay. Source: MGI generation of precursor metabolites and energy Ref.1 Traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Ref.1 Traceable author statement. Source: UniProtKB
Molecular function	binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity Ref.1 Inferred from direct assay. Source: UniProtKB saccharopine dehydrogenase (NADP+, 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
	Transit peptide	1 – 32	32	Mitochondrion
	Chain	33 – 926	894	Alpha-aminoadipic semialdehyde synthase, mitochondrial		PRO_0000001053
Regions
	Region	33 – 455	423	Lysine-ketoglutarate reductase
	Region	477 – 926	450	Saccharopine dehydrogenase
Experimental info
	Sequence conflict	198	1	V → I in CAA12114. Ref.1
	Sequence conflict	851	1	L → A in CAA12114. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q99K67-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 5B4369C51F7D1D53	FASTA	926	102,975
	10 20 30 40 50 60 MLRAQRPRLA RLRACLSRGL HHKPVMALRR EDVNAWERRA PLAPKHIKGI TKLGYKVLIQ 70 80 90 100 110 120 PSNRRAIHDK EYVRAGGILQ EDITEACLIL GVKRPPEEKL MSKKTYAFFS HTIKAQEANM 130 140 150 160 170 180 NLLDEVLKQE IRLIDYEKMV DHRGSRIVAF GQWAGVAGMI NILHGMGLRL LALGHHTPFM 190 200 210 220 230 240 HLGMAHNYRN SSQAVQAVRD AGYEISLGLM PKSIGPLTFV FTGTGNVSKG AQEVFNELPC 250 260 270 280 290 300 EYVEPHELRE VSKTGDLRKV YGTVLSRHHH LVRKTDGVYD PVEYEKYPER YTSRFNTDIA 310 320 330 340 350 360 PYTTCLINGI YWEQNTPRLL TRQDAQSLLV PVKSSVVPVE GCPELPHKLV AICDISADTG 370 380 390 400 410 420 GSIDFMTECT TIERPFCMYD ADQQIIHDSV EGSGILMCSI DNLPAQLPIE ATEYFGDMLY 430 440 450 460 470 480 PYVEEMLLSD ASQPLESQNF SPVVRDAVIT SNGLLTDKYK YIQKLRESRE RIQFLSMSTK 490 500 510 520 530 540 KKVLVLGSGY VSGPVLEYLS RDNNIEITLG SDMTNQMQQL SKKYNINPVS LTVGKQEAKL 550 560 570 580 590 600 QSLVESQDLV ISLLPYVLHP VVAKACIESR VNMVTASYIT PAMKELEKSV DDAGITVIGE 610 620 630 640 650 660 LGLDPGLDHM LAMETIDTAK ELGATVESYV SYCGGLPAPE HSDNPLRYKF SWSPVGVLMN 670 680 690 700 710 720 IMQPASYLLN GKVVNVTGGV SFLNSVTPMD YFPGLNLEGY PNRDSIKYAE IYGISSAHTL 730 740 750 760 770 780 LRGTLRYKGY SKALNGFVKL GLINREAYPA LRPEANPLTW KQLLCDLVGI SRSSPCEKLK 790 800 810 820 830 840 EVVFTKLGGD NTQLEAAEWL GLLGDEQVPQ AESIVDAFSK HLVSKLSYGP EEKDMIVMRD 850 860 870 880 890 900 SFGIRHPSGH LENKTIDLVV YGDFNGFSAM AKTVGLPTAM AAKMLLDGEI EAKGLMGPFT 910 920 KEIYGPILER IKAEGIVFNT QSTIKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lysine degradation through the saccharopine pathway in mammals: involvement of both bifunctional and monofunctional lysine-degrading enzymes in mouse." Papes F., Kemper E.L., Cord-Neto G., Langone F., Arruda P. Biochem. J. 344:555-563(1999) [PubMed: 10567240] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J X CBA/J. Tissue: Liver.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary tumor.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ224761 mRNA. Translation: CAA12114.1. BC005420 mRNA. Translation: AAH05420.1.
IPI	IPI00387491.
RefSeq	NP_038958.2.
UniGene	Mm.18651
3D structure databases
ModBase	Search...
2-D gel databases
REPRODUCTION-2DPAGE	Q99K67.
Proteomic databases
PRIDE	Q99K67.
Genome annotation databases
Ensembl	ENSMUSG00000029695. Mus musculus. [Contig view]
GeneID	30956.
KEGG	mmu:30956.
Organism-specific databases
MGI	MGI:1353573. Aass.
Phylogenomic databases
HOGENOM	Q99K67.
HOVERGEN	Q99K67.
OMA	Q99K67. DNPLRYK.
Enzyme and pathway databases
BRENDA	1.5.1.8. 244. 1.5.1.9. 244.
Gene expression databases
ArrayExpress	Q99K67.
Bgee	Q99K67.
CleanEx	MM_AASS.
GermOnline	ENSMUSG00000029695. Mus musculus.
Family and domain databases
InterPro	IPR007698. Ala_DH/PNT_C. IPR008142. Ala_DH/PNT_CS1. IPR008143. Ala_DH/PNT_CS2. IPR007886. Ala_DH/PNT_N. IPR005097. Saccharopine_DH. [Graphical view]
Pfam	PF01262. AlaDh_PNT_C. 1 hit. PF05222. AlaDh_PNT_N. 1 hit. PF03435. Saccharop_dh. 1 hit. [Graphical view]
PROSITE	PS00836. ALADH_PNT_1. False negative. PS00837. ALADH_PNT_2. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	307440.
SOURCE	Search...

Entry information

Entry name

AASS_MOUSE

Accession

Primary (citable) accession number: Q99K67
Secondary accession number(s): Q9Z1I9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)