ID AASS_MOUSE Reviewed; 926 AA.
AC Q99K67; Q9Z1I9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 01-MAY-2013, entry version 95.
DE RecName: Full=Alpha-aminoadipic semialdehyde synthase, mitochondrial;
DE AltName: Full=LKR/SDH;
DE Includes:
DE RecName: Full=Lysine ketoglutarate reductase;
DE Short=LKR;
DE Short=LOR;
DE EC=1.5.1.8;
DE Includes:
DE RecName: Full=Saccharopine dehydrogenase;
DE Short=SDH;
DE EC=1.5.1.9;
DE Flags: Precursor;
GN Name=Aass; Synonyms=Lorsdh;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J X CBA/J; TISSUE=Liver;
RX PubMed=10567240; DOI=10.1042/0264-6021:3440555;
RA Papes F., Kemper E.L., Cord-Neto G., Langone F., Arruda P.;
RT "Lysine degradation through the saccharopine pathway in mammals:
RT involvement of both bifunctional and monofunctional lysine-degrading
RT enzymes in mouse.";
RL Biochem. J. 344:555-563(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the first two steps
CC in lysine degradation. The N-terminal and the C-terminal contain
CC lysine-oxoglutarate reductase and saccharopine dehydrogenase
CC activity, respectively.
CC -!- CATALYTIC ACTIVITY: N(6)-(L-1,3-dicarboxypropyl)-L-lysine +
CC NADP(+) + H(2)O = L-lysine + 2-oxoglutarate + NADPH.
CC -!- CATALYTIC ACTIVITY: N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD(+)
CC + H(2)O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via
CC saccharopine pathway; glutaryl-CoA from L-lysine: step 1/6.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via
CC saccharopine pathway; glutaryl-CoA from L-lysine: step 2/6.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- TISSUE SPECIFICITY: Both enzymes are highly expressed in kidney
CC and liver, very low expression is seen in heart, brain, spleen,
CC lung, skeletal muscle and testis. SDH was detected only in
CC cortical regions of the kidney.
CC -!- INDUCTION: Induced by starvation.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT
CC family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine
CC dehydrogenase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ224761; CAA12114.1; -; mRNA.
DR EMBL; BC005420; AAH05420.1; -; mRNA.
DR IPI; IPI00387491; -.
DR RefSeq; NP_038958.2; NM_013930.4.
DR UniGene; Mm.18651; -.
DR ProteinModelPortal; Q99K67; -.
DR SMR; Q99K67; 30-424, 481-912.
DR PhosphoSite; Q99K67; -.
DR REPRODUCTION-2DPAGE; Q99K67; -.
DR PaxDb; Q99K67; -.
DR PRIDE; Q99K67; -.
DR Ensembl; ENSMUST00000031707; ENSMUSP00000031707; ENSMUSG00000029695.
DR GeneID; 30956; -.
DR KEGG; mmu:30956; -.
DR CTD; 10157; -.
DR MGI; MGI:1353573; Aass.
DR eggNOG; COG1748; -.
DR GeneTree; ENSGT00390000013249; -.
DR HOGENOM; HOG000252920; -.
DR HOVERGEN; HBG048688; -.
DR InParanoid; Q99K67; -.
DR KO; K14157; -.
DR OMA; WKELLCD; -.
DR OrthoDB; EOG4PZJ5Z; -.
DR UniPathway; UPA00868; UER00835.
DR UniPathway; UPA00868; UER00836.
DR NextBio; 307440; -.
DR ArrayExpress; Q99K67; -.
DR Bgee; Q99K67; -.
DR CleanEx; MM_AASS; -.
DR Genevestigator; Q99K67; -.
DR GermOnline; ENSMUSG00000029695; Mus musculus.
DR GO; GO:0005739; C:mitochondrion; TAS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IDA:UniProtKB.
DR GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:EC.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:UniProtKB.
DR GO; GO:0019477; P:L-lysine catabolic process; IDA:MGI.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR005097; Saccharopine_DH/HSpermid_syn.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF03435; Saccharop_dh; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR PROSITE; PS00836; ALADH_PNT_1; FALSE_NEG.
DR PROSITE; PS00837; ALADH_PNT_2; FALSE_NEG.
PE 2: Evidence at transcript level;
KW Complete proteome; Mitochondrion; Multifunctional enzyme; NAD; NADP;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1 32 Mitochondrion.
FT CHAIN 33 926 Alpha-aminoadipic semialdehyde synthase,
FT mitochondrial.
FT /FTId=PRO_0000001053.
FT REGION 33 455 Lysine-ketoglutarate reductase.
FT REGION 477 926 Saccharopine dehydrogenase.
FT CONFLICT 198 198 V -> I (in Ref. 1; CAA12114).
FT CONFLICT 851 851 L -> A (in Ref. 1; CAA12114).
SQ SEQUENCE 926 AA; 102975 MW; 5B4369C51F7D1D53 CRC64;
MLRAQRPRLA RLRACLSRGL HHKPVMALRR EDVNAWERRA PLAPKHIKGI TKLGYKVLIQ
PSNRRAIHDK EYVRAGGILQ EDITEACLIL GVKRPPEEKL MSKKTYAFFS HTIKAQEANM
NLLDEVLKQE IRLIDYEKMV DHRGSRIVAF GQWAGVAGMI NILHGMGLRL LALGHHTPFM
HLGMAHNYRN SSQAVQAVRD AGYEISLGLM PKSIGPLTFV FTGTGNVSKG AQEVFNELPC
EYVEPHELRE VSKTGDLRKV YGTVLSRHHH LVRKTDGVYD PVEYEKYPER YTSRFNTDIA
PYTTCLINGI YWEQNTPRLL TRQDAQSLLV PVKSSVVPVE GCPELPHKLV AICDISADTG
GSIDFMTECT TIERPFCMYD ADQQIIHDSV EGSGILMCSI DNLPAQLPIE ATEYFGDMLY
PYVEEMLLSD ASQPLESQNF SPVVRDAVIT SNGLLTDKYK YIQKLRESRE RIQFLSMSTK
KKVLVLGSGY VSGPVLEYLS RDNNIEITLG SDMTNQMQQL SKKYNINPVS LTVGKQEAKL
QSLVESQDLV ISLLPYVLHP VVAKACIESR VNMVTASYIT PAMKELEKSV DDAGITVIGE
LGLDPGLDHM LAMETIDTAK ELGATVESYV SYCGGLPAPE HSDNPLRYKF SWSPVGVLMN
IMQPASYLLN GKVVNVTGGV SFLNSVTPMD YFPGLNLEGY PNRDSIKYAE IYGISSAHTL
LRGTLRYKGY SKALNGFVKL GLINREAYPA LRPEANPLTW KQLLCDLVGI SRSSPCEKLK
EVVFTKLGGD NTQLEAAEWL GLLGDEQVPQ AESIVDAFSK HLVSKLSYGP EEKDMIVMRD
SFGIRHPSGH LENKTIDLVV YGDFNGFSAM AKTVGLPTAM AAKMLLDGEI EAKGLMGPFT
KEIYGPILER IKAEGIVFNT QSTIKL
//
