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Q99K67 (AASS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-aminoadipic semialdehyde synthase, mitochondrial
Alternative name(s):
LKR/SDH

Including the following 2 domains:

  1. Lysine ketoglutarate reductase
    Short name=LKR
    Short name=LOR
    EC=1.5.1.8
  2. Saccharopine dehydrogenase
    Short name=SDH
    EC=1.5.1.9
Gene names
Name:Aass
Synonyms:Lorsdh
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length926 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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 + (S)-2-amino-6-oxohexanoate + 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Mitochondrion
Chain33 – 926894Alpha-aminoadipic semialdehyde synthase, mitochondrial
PRO_0000001053

Regions

Region33 – 455423Lysine-ketoglutarate reductase
Region477 – 926450Saccharopine dehydrogenase

Amino acid modifications

Modified residue481N6-acetyllysine Ref.4
Modified residue521N6-acetyllysine Ref.4
Modified residue561N6-acetyllysine Ref.4
Modified residue931N6-acetyllysine; alternate Ref.4
Modified residue931N6-succinyllysine; alternate Ref.3
Modified residue1281N6-acetyllysine Ref.4
Modified residue1381N6-acetyllysine; alternate Ref.4
Modified residue1381N6-succinyllysine; alternate Ref.3
Modified residue2741N6-succinyllysine Ref.3
Modified residue2861N6-acetyllysine; alternate Ref.4
Modified residue2861N6-succinyllysine; alternate Ref.3
Modified residue3331N6-succinyllysine Ref.3
Modified residue4581N6-acetyllysine; alternate Ref.4
Modified residue4581N6-succinyllysine; alternate Ref.3
Modified residue5231N6-acetyllysine; alternate Ref.4
Modified residue5231N6-succinyllysine; alternate Ref.3
Modified residue5351N6-acetyllysine; alternate Ref.4
Modified residue5351N6-succinyllysine; alternate Ref.3
Modified residue5841N6-acetyllysine; alternate Ref.4
Modified residue5841N6-succinyllysine; alternate Ref.3
Modified residue7071N6-acetyllysine Ref.4
Modified residue7321N6-succinyllysine Ref.3
Modified residue7391N6-acetyllysine Ref.4
Modified residue7611N6-acetyllysine; alternate Ref.4
Modified residue7611N6-succinyllysine; alternate Ref.3
Modified residue7781N6-acetyllysine Ref.4
Modified residue7801N6-acetyllysine Ref.4

Experimental info

Sequence conflict1981V → I in CAA12114. Ref.1
Sequence conflict8511L → A in CAA12114. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99K67 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 5B4369C51F7D1D53

FASTA926102,975
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor.
[3]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-93; LYS-138; LYS-274; LYS-286; LYS-333; LYS-458; LYS-523; LYS-535; LYS-584; LYS-732 AND LYS-761, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[4]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-52; LYS-56; LYS-93; LYS-128; LYS-138; LYS-286; LYS-458; LYS-523; LYS-535; LYS-584; LYS-707; LYS-739; LYS-761; LYS-778 AND LYS-780, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ224761 mRNA. Translation: CAA12114.1.
BC005420 mRNA. Translation: AAH05420.1.
CCDSCCDS19937.1.
RefSeqNP_038958.2. NM_013930.4.
UniGeneMm.18651.

3D structure databases

ProteinModelPortalQ99K67.
SMRQ99K67. Positions 30-424, 481-912.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ99K67. 2 interactions.
MINTMINT-1840773.

PTM databases

PhosphoSiteQ99K67.

2D gel databases

REPRODUCTION-2DPAGEQ99K67.

Proteomic databases

MaxQBQ99K67.
PaxDbQ99K67.
PRIDEQ99K67.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031707; ENSMUSP00000031707; ENSMUSG00000029695.
GeneID30956.
KEGGmmu:30956.
UCSCuc009bbc.2. mouse.

Organism-specific databases

CTD10157.
MGIMGI:1353573. Aass.

Phylogenomic databases

eggNOGCOG1748.
GeneTreeENSGT00390000013249.
HOGENOMHOG000252920.
HOVERGENHBG048688.
InParanoidQ99K67.
KOK14157.
OMAILKQEIR.
OrthoDBEOG7F7W7Z.
PhylomeDBQ99K67.
TreeFamTF105728.

Enzyme and pathway databases

UniPathwayUPA00868; UER00835.
UPA00868; UER00836.

Gene expression databases

ArrayExpressQ99K67.
BgeeQ99K67.
CleanExMM_AASS.
GenevestigatorQ99K67.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
IPR016040. NAD(P)-bd_dom.
IPR005097. Saccharopine_DH/HSpermid_syn.
[Graphical view]
PfamPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
PF03435. Saccharop_dh. 1 hit.
[Graphical view]
SMARTSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio307440.
PROQ99K67.
SOURCESearch...

Entry information

Entry nameAASS_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot