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Q9UDR5 (AASS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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-ketoglutarate 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 By similarity.

Subcellular location

Mitochondrion By similarity.

Tissue specificity

Expressed in all 16 tissues examined with highest expression in the liver.

Induction

Induced by starvation By similarity.

Involvement in disease

Hyperlysinemia, 1 (HYPLYS1) [MIM:238700]: An autosomal recessive metabolic condition with variable clinical features. Some patients present with non-specific seizures, hypotonia, or mildly delayed psychomotor development, and increased serum lysine and pipecolic acid on laboratory analysis. However, about half of the probands are reported to be asymptomatic, and hyperlysinemia is generally considered to be a benign metabolic variant.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1

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 By similarity
Chain33 – 926894Alpha-aminoadipic semialdehyde synthase, mitochondrial
PRO_0000001052

Regions

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

Amino acid modifications

Modified residue481N6-acetyllysine By similarity
Modified residue561N6-acetyllysine By similarity
Modified residue931N6-acetyllysine; alternate By similarity
Modified residue931N6-succinyllysine; alternate By similarity
Modified residue1281N6-acetyllysine By similarity
Modified residue1381N6-acetyllysine; alternate By similarity
Modified residue1381N6-succinyllysine; alternate By similarity
Modified residue2741N6-succinyllysine By similarity
Modified residue2861N6-acetyllysine; alternate By similarity
Modified residue2861N6-succinyllysine; alternate By similarity
Modified residue3331N6-succinyllysine By similarity
Modified residue4581N6-acetyllysine; alternate By similarity
Modified residue4581N6-succinyllysine; alternate By similarity
Modified residue5231N6-acetyllysine; alternate By similarity
Modified residue5231N6-succinyllysine; alternate By similarity
Modified residue5351N6-acetyllysine; alternate By similarity
Modified residue5351N6-succinyllysine; alternate By similarity
Modified residue5841N6-acetyllysine; alternate By similarity
Modified residue5841N6-succinyllysine; alternate By similarity
Modified residue7071N6-acetyllysine By similarity
Modified residue7321N6-succinyllysine By similarity
Modified residue7391N6-acetyllysine By similarity
Modified residue7611N6-acetyllysine; alternate By similarity
Modified residue7611N6-succinyllysine; alternate By similarity
Modified residue7801N6-acetyllysine By similarity

Experimental info

Sequence conflict5891S → C in CAA07619. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9UDR5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CB4194014351A18D

FASTA926102,132
        10         20         30         40         50         60 
MLQVHRTGLG RLGVSLSKGL HHKAVLAVRR EDVNAWERRA PLAPKHIKGI TNLGYKVLIQ 

        70         80         90        100        110        120 
PSNRRAIHDK DYVKAGGILQ EDISEACLIL GVKRPPEEKL MSRKTYAFFS HTIKAQEANM 

       130        140        150        160        170        180 
GLLDEILKQE IRLIDYEKMV DHRGVRVVAF GQWAGVAGMI NILHGMGLRL LALGHHTPFM 

       190        200        210        220        230        240 
HIGMAHNYRN SSQAVQAVRD AGYEISLGLM PKSIGPLTFV FTGTGNVSKG AQAIFNELPC 

       250        260        270        280        290        300 
EYVEPHELKE VSQTGDLRKV YGTVLSRHHH LVRKTDAVYD PAEYDKHPER YISRFNTDIA 

       310        320        330        340        350        360 
PYTTCLINGI YWEQNTPRLL TRQDAQSLLA PGKFSPAGVE GCPALPHKLV AICDISADTG 

       370        380        390        400        410        420 
GSIEFMTECT TIEHPFCMYD ADQHIIHDSV EGSGILMCSI DNLPAQLPIE ATECFGDMLY 

       430        440        450        460        470        480 
PYVEEMILSD ATQPLESQNF SPVVRDAVIT SNGTLPDKYK YIQTLRESRE RAQSLSMGTR 

       490        500        510        520        530        540 
RKVLVLGSGY ISEPVLEYLS RDGNIEITVG SDMKNQIEQL GKKYNINPVS MDICKQEEKL 

       550        560        570        580        590        600 
GFLVAKQDLV ISLLPYVLHP LVAKACITNK VNMVTASYIT PALKELEKSV EDAGITIIGE 

       610        620        630        640        650        660 
LGLDPGLDHM LAMETIDKAK EVGATIESYI SYCGGLPAPE HSNNPLRYKF SWSPVGVLMN 

       670        680        690        700        710        720 
VMQSATYLLD GKVVNVAGGI SFLDAVTSMD FFPGLNLEGY PNRDSTKYAE IYGISSAHTL 

       730        740        750        760        770        780 
LRGTLRYKGY MKALNGFVKL GLINREALPA FRPEANPLTW KQLLCDLVGI SPSSEHDVLK 

       790        800        810        820        830        840 
EAVLKKLGGD NTQLEAAEWL GLLGDEQVPQ AESILDALSK HLVMKLSYGP EEKDMIVMRD 

       850        860        870        880        890        900 
SFGIRHPSGH LEHKTIDLVA YGDINGFSAM AKTVGLPTAM AAKMLLDGEI GAKGLMGPFS 

       910        920 
KEIYGPILER IKAEGIIYTT QSTIKP 

« Hide

References

« Hide 'large scale' references
[1]"Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia."
Sacksteder K.A., Biery B.J., Morrell J.C., Goodman B.K., Geisbrecht B.V., Cox R.P., Gould S.J., Geraghty M.T.
Am. J. Hum. Genet. 66:1736-1743(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INVOLVEMENT IN HYPLYS1.
[2]"Cloning and expression analysis of the LKR/SDH gene in human tissues."
Papes F., Kemper E.L., Cord-Neto G., Langone F., Arruda P.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF229180 mRNA. Translation: AAF44328.1.
AJ007714 mRNA. Translation: CAA07619.2.
AC006020 Genomic DNA. Translation: AAF03526.1.
CCDSCCDS5783.1.
RefSeqNP_005754.2. NM_005763.3.
UniGeneHs.156738.

3D structure databases

ProteinModelPortalQ9UDR5.
SMRQ9UDR5. Positions 30-424, 481-924.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115459. 5 interactions.
IntActQ9UDR5. 2 interactions.
MINTMINT-2820994.
STRING9606.ENSP00000377040.

Chemistry

DrugBankDB00142. L-Glutamic Acid.
DB00157. NADH.

PTM databases

PhosphoSiteQ9UDR5.

Polymorphism databases

DMDM46396032.

Proteomic databases

MaxQBQ9UDR5.
PaxDbQ9UDR5.
PeptideAtlasQ9UDR5.
PRIDEQ9UDR5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000393376; ENSP00000377040; ENSG00000008311.
ENST00000417368; ENSP00000403768; ENSG00000008311.
GeneID10157.
KEGGhsa:10157.
UCSCuc003vka.3. human.

Organism-specific databases

CTD10157.
GeneCardsGC07M121713.
HGNCHGNC:17366. AASS.
HPAHPA020637.
HPA020728.
HPA020734.
MIM238700. phenotype.
605113. gene.
neXtProtNX_Q9UDR5.
Orphanet2203. Hyperlysinemia.
3124. Saccharopinuria.
PharmGKBPA24369.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1748.
HOGENOMHOG000252920.
HOVERGENHBG048688.
InParanoidQ9UDR5.
KOK14157.
OMAILKQEIR.
OrthoDBEOG7F7W7Z.
PhylomeDBQ9UDR5.
TreeFamTF105728.

Enzyme and pathway databases

BioCycMetaCyc:HS00244-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ9UDR5.
UniPathwayUPA00868; UER00835.
UPA00868; UER00836.

Gene expression databases

ArrayExpressQ9UDR5.
BgeeQ9UDR5.
CleanExHS_AASS.
GenevestigatorQ9UDR5.

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

ChiTaRSAASS. human.
GeneWikiAASS.
GenomeRNAi10157.
NextBio38452.
PROQ9UDR5.
SOURCESearch...

Entry information

Entry nameAASS_HUMAN
AccessionPrimary (citable) accession number: Q9UDR5
Secondary accession number(s): O95462
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM