CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-026079
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aldehyde oxidase 1 
Protein Synonyms/Alias
  
Gene Name
 Aox3 
Gene Synonyms/Alias
 Aoh1 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
849GRHPLLGKYRVGFMNacetylation[1]
986SSYYSRKKAVDEFNQacetylation[1]
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
  
Sequence Annotation
  
Keyword
 2Fe-2S; Iron; Iron-sulfur; Metal-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1334 AA 
Protein Sequence
MSRSKESDEL IFFVNGKKVI ERNADPEVNL LFYLRKIIQL TGTKYGCGGG DCGACTVMIS 60
RYNPISKKIS HFSAAACLVP ICSLHGAAVT TVEGIGSTKT RIHPVQERIA KGHGTQCGFC 120
TPGMVMSIYT LLRNHPEPST EQIMETLGGN LCRCTGYRPI VESARSFSPN SACCPMNEKW 180
KCCLDEGKNE PERKNSVCTK LYEKEEFQPL DPTQELIFPP ELMRMAEDSP NTVLTFRGER 240
TTWIAPGTLN DLLELKMEYP SAPLVIGNTC LGLDMKFKDV SYPIIISPAR ILELFVVTNT 300
NEGLTLGAGL SLTQVKNILS DVVSRLPKER TQTYRALLKH LRTLAGQQIR NVASLGGHII 360
SRLPTSDLNP IFGVGNCKLN VASTEGTQQI PLNDHFLAGV PEAILKPEQV LISVFVPLSR 420
KWEFVSAFRQ APRQQNAFAI VNAGMRVAFK EDTNTITDLS ILYGGIGATV VSAKSCQQLI 480
GRCWDEEMLD DAGRMIREEV SLLTAAPGGM VEYRKTLAIS FLFKFYLDVL KQLKRRNPHR 540
CPDISQKLLQ VLEDFPLTMP HGTQSFKDVD SQQPLQDQSG RPIMHQSGIK HATGEAVFCD 600
DMSVLAGELF LAVVTSSKPH ARIISLDASE ALASPGVVDV ITAQDVPGDN GREEESLYAQ 660
DEVICVGQIV CAVAADSYAR AKQATKKVKI VYEDMEPMIV TVQDALQHES FIGPEKKLEQ 720
GNVQLAFQSA DQILEGEVHL GGQEHFYMET QSVRVIPKGE DMEMDIYVSS QDAAFTQEMV 780
ARTLGIPKNR ITCHVKRVGG GFGGKTSKPG LLASVAAVAA QKTGRPIRFI LERGDDMLIT 840
GGRHPLLGKY RVGFMNNGKI KAADIQLYIN GGCTPDDSEL VIEYALLKLE NAYKIPNLRV 900
RGRVCKTNLP SNTAFRGFGF PQGAFVTGTW VSAVAAKCHL PPEKVRELNM YKTIDRTIHK 960
QEFDPTNLIK CWETCMENSS YYSRKKAVDE FNQQSFWKKR GIAIIPMKFS VGFPKTFYHQ 1020
AAALVQIYTD GSVLVAHGGV ELGQGINTKM IQVASRELKI PMSYIHLDEM NTMTVPNTIT 1080
TGGSTGADVN GRAVQNACQI LMKRLEPIIS QNPNGDWEEW INEAFIQSIS LSATGYFRGY 1140
QADMDWEKGE GDIYPYFVFG AACSEVEIDC LTGAHKNIRT DIVMDGSFSI NPAVDIGQIE 1200
GAFVQGLGLY TLEELKYSPE GVLYTRGPHQ YKIASVSDIP EEFHVSLLTP TQNPKAIYSS 1260
KGLGEAGMFL GSSVFFAIAA AVAAARKERG LPLILAINSP ATAEVIRMAC EDQFTNLVPK 1320
TDSKCCKPWS IPVA 1334 
Gene Ontology
 GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro. 
Interpro
 IPR002888; 2Fe-2S-bd.
 IPR001041; 2Fe-2S_ferredoxin-type.
 IPR006058; 2Fe2S_fd_BS.
 IPR000674; Ald_Oxase/Xan_DH_a/b.
 IPR016208; Ald_Oxase/xanthine_DH.
 IPR014313; Aldehyde_oxidase.
 IPR008274; AldOxase/xan_DH_Mopterin-bd.
 IPR012675; Beta-grasp_dom.
 IPR005107; CO_DH_flav_C.
 IPR016169; CO_DH_flavot_FAD-bd_sub2.
 IPR016166; FAD-bd_2.
 IPR016167; FAD-bd_2_sub1.
 IPR002346; Mopterin_DH_FAD-bd. 
Pfam
 PF01315; Ald_Xan_dh_C
 PF02738; Ald_Xan_dh_C2
 PF03450; CO_deh_flav_C
 PF00941; FAD_binding_5
 PF00111; Fer2
 PF01799; Fer2_2 
SMART
 SM01008; Ald_Xan_dh_C
 SM01092; CO_deh_flav_C 
PROSITE
 PS00197; 2FE2S_FER_1
 PS51085; 2FE2S_FER_2
 PS51387; FAD_PCMH 
PRINTS