Tag | Content |
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CPLM ID | CPLM-024403 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Alpha-aminoadipic semialdehyde synthase, mitochondrial |
Protein Synonyms/Alias | LKR/SDH; Lysine ketoglutarate reductase; LKR; LOR; Saccharopine dehydrogenase; SDH |
Gene Name | Aass |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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45 | RRAPLAPKHIKGITK | acetylation | [1] | 48 | PLAPKHIKGITKLGY | acetylation | [1] | 52 | KHIKGITKLGYKVLI | acetylation | [1] | 70 | NRRAIHDKEYVRAGG | acetylation | [1] | 138 | IRLIDYEKMVDHRGS | acetylation | [1] | 286 | YDPVEYEKYPERYIS | acetylation | [1] | 523 | QMQQLSKKYDINTVN | acetylation | [1] | 535 | TVNVTVGKQEDKLQS | acetylation | [1] | 584 | SYITPAMKELEKSVD | acetylation | [1] | 707 | YPNRDSTKYAEIYGI | acetylation | [1] | 732 | LRYKGYSKALNGFVK | acetylation | [1] | 780 | SSSCEKLKEVVFTKL | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | 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 (By similarity). |
Sequence Annotation | REGION 33 455 Lysine-ketoglutarate reductase (By REGION 477 926 Saccharopine dehydrogenase (By |
Keyword | Complete proteome; Mitochondrion; Multifunctional enzyme; NAD; NADP; Oxidoreductase; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 926 AA |
Protein Sequence | MLRAQRLRLA RLRACVSRGL HHKPVMALRR EDVNAWERRA PLAPKHIKGI TKLGYKVLIQ 60 PSNRRAIHDK EYVRAGGILQ EDITEACLIL GVKRPPEEKL MSKKTYAFFS HTIKAQEANM 120 SLLDEVLKQE IRLIDYEKMV DHRGSRIVAF GHWAGVAGMI NILHGMGLRL LALGHHTPFM 180 HLGMAHNYRN SSQAVQAVRD AGYEISLGLM PKSIGPLTFV FTGTGNVSKG AQEVFNELPC 240 EYVEPHELKE VSKTGDLRKV YGTVLSRHHH LVRKTDGVYD PVEYEKYPER YISRFNADIA 300 PYTTCLINGI YWEQNTPRLL TRQDAQSLLV PVKSSVVPVE GCPELPHKLV AICDISADTG 360 GSIDFMTECT TIERPFCMYD ADQHIIHDSV EGSGILMCSI DNLPAQLPIE ATEYFGDMLY 420 PYVEEMLLSD ASQPLESQNF SPVVRDAVIT SNGLLTDKYK YIQKLRESRE RIQFLSMSTK 480 KKVLVLGSGY VSGPVLEYLS RGNNIEITLG SDMTNQMQQL SKKYDINTVN VTVGKQEDKL 540 QSLVESQDLV ISLLPYVLHP VVAKACIDSK VNMVTASYIT PAMKELEKSV DDAGITVIGE 600 LGLDPGLDHM LAMETIDKAK DLGATIESYV SYCGGLPAPE HSDNPLRYKF SWSPVGVLMN 660 IMQPASYLLN GKVVNVTGGV SFLNSVTPMD YFPGLNLEGY PNRDSTKYAE IYGISSAHTL 720 LRGTLRYKGY SKALNGFVKL GLINRETYPA LRPEANPLTW KQLLCDLVGI SRSSSCEKLK 780 EVVFTKLGGD STQLEAAEWL GLLGDEQVPQ AESIVDAFSK HLVSKLSYGP EEKDMIVMRD 840 SFGIRHPSGH LENKTIDLVV YGDFNGFSAM AKTVGLPTAM AAKMLLDGEI ETKGLMGPFS 900 KEIYGPILER IKAEGIVFNT QSTIKL 926 |
Gene Ontology | GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IEA:EC. GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:EC. GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway. |
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