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Reviewed, UniProtKB/Swiss-Prot Q9UDR5 (AASS_HUMAN)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
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 + 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 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

Defects in AASS are the cause of hyperlysinemia [MIM:238700]. Hyperlysinemia is an autosomal recessive condition characterized by hyperlysinemia lysinuria and variable saccharopinuria.

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

Experimental info

Sequence conflict5891S → C in CAA07619. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9UDR5-1 [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: 10775527] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[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: 12853948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Web resources

Cross-references

Sequence databases

AF229180 mRNA. Translation: AAF44328.1.
AJ007714 mRNA. Translation: CAA07619.2.
AC006020 Genomic DNA. Translation: AAF03526.1.
IPIIPI00033217.
RefSeqNP_005754.2.
UniGeneHs.156738

3D structure databases

ModBaseSearch...

Proteomic databases

PeptideAtlasQ9UDR5.
PRIDEQ9UDR5.

Genome annotation databases

EnsemblENSG00000008311. Homo sapiens. [Contig view]
GeneID10157.
KEGGhsa:10157.

Organism-specific databases

GeneCardsGC07M121503.
HGNCHGNC:17366. AASS.
MIM238700. phenotype.
605113. gene.
Orphanet2203. Hyperlysinemia.
3124. Saccharopinuria.
PharmGKBPA24369.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9UDR5.
HOVERGENQ9UDR5.
OMAQ9UDR5. DNPLRYK.

Enzyme and pathway databases

BioCycMetaCyc:MON-12249.
BRENDA1.5.1.8. 247.
1.5.1.9. 247.
ReactomeREACT_13. Metabolism of amino acids.

Gene expression databases

ArrayExpressQ9UDR5.
BgeeQ9UDR5.
CleanExHS_AASS.
GermOnlineENSG00000008311. Homo sapiens.

Family and domain databases

InterProIPR007698. Ala_DH/PNT_C.
IPR008142. Ala_DH/PNT_CS1.
IPR008143. Ala_DH/PNT_CS2.
IPR007886. Ala_DH/PNT_N.
IPR005097. Saccharopine_DH.
[Graphical view]
PfamPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
PF03435. Saccharop_dh. 1 hit.
[Graphical view]
PROSITEPS00836. ALADH_PNT_1. False negative.
PS00837. ALADH_PNT_2. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00142. L-Glutamic Acid.
DB00157. NADH.
NextBio38452.
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: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 7

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

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents