CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024068
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aldehyde oxidase 
Protein Synonyms/Alias
  
Gene Name
 Aox1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
420VNIPCSRKWEFVSAFacetylation[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
 DOMAIN 4 91 2Fe-2S ferredoxin-type.
 DOMAIN 235 420 FAD-binding PCMH-type.
 METAL 43 43 Iron-sulfur (2Fe-2S) (By similarity).
 METAL 48 48 Iron-sulfur (2Fe-2S) (By similarity).
 METAL 51 51 Iron-sulfur (2Fe-2S) (By similarity).  
Keyword
 2Fe-2S; Complete proteome; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1333 AA 
Protein Sequence
MDPPQLLFYV NGQKVVENNV DPEMMLLPYL RKNLRLTGTK YGCGGGGCGA CTVMISRYNP 60
STKSIRHHPV NACLTPICSL YGTAVTTVEG IGNTRTRLHP VQERIAKCHS TQCGFCTPGM 120
VMSMYALLRN HPEPSLDQLT DALGGNLCRC TGYRPIIDAC KTFCRASGCC ESKENGVCCL 180
DQGINGSAEF QEGDETSPEL FSEKEFQPLD PTQELIFPPE LMRIAEKQPP KTRVFYSNRM 240
TWISPVTLEE LVEAKFKYPG APIVMGYTSV GPEVKFKGVF HPIIISPDRI EELSIINQTG 300
DGLTLGAGLS LDQVKDILTD VVQKLPEETT QTYRALLKHL RTLAGSQIRN MASLGGHIVS 360
RHLDSDLNPL LAVGNCTLNL LSKDGKRQIP LSEQFLRKCP DSDLKPQEVL VSVNIPCSRK 420
WEFVSAFRQA QRQQNALAIV NSGMRVLFRE GGGVIKELSI LYGGVGPTTI GAKNSCQKLI 480
GRPWNEEMLD TACRLVLDEV TLAGSAPGGK VEFKRTLIIS FLFKFYLEVL QGLKREDPGH 540
YPSLTNNYES ALEDLHSKHH WRTLTHQNVD SMQLPQDPIG RPIMHLSGIK HATGEAIYCD 600
DMPAVDRELF LTFVTSSRAH AKIVSIDLSE ALSLPGVVDI ITADHLQDAT TFGTETLLAT 660
DKVHCVGQLV CAVIADSETR AKQAAKHVKV VYRDLEPLIL TIEEAIQHKS FFESERKLEC 720
GNVDEAFKIA DQILEGEIHI GGQEHFYMET QSMLVVPKGE DGEIDIYVST QFPKHIQDIV 780
AATLKLSVNK VMCHVRRVGG AFGGKVGKTS IMAAITAFAA SKHGRAVRCT LERGEDMLIT 840
GGRHPYLGKY KVGFMRDGRI VALDVEHYCN GGSSLDESLW VIEMGLLKMD NAYKFPNLRC 900
RGWACRTNLP SHTALRGFGF PQAGLVTEAC VTEVAIRCGL SPEQVRTINM YKQIDNTHYK 960
QEFSAKTLFE CWRECMAKCS YSERKTAVGK FNAENSWKKR GMAVIPLKFP VGVGSVAMGQ 1020
AAALVHIYLD GSALVSHGGI EMGQGVHTKM IQVVSRELKM PMSSVHLRGT STETVPNTNA 1080
SGGSVVADLN GLAVKDACQT LLKRLEPIIS KNPQGTWKDW AQTAFDQSVS LSAVGYFRGY 1140
ESNINWEKGE GHPFEYFVYG AACSEVEIDC LTGDHKNIRT DIVMDVGHSI NPALDIGQVE 1200
GAFIQGMGLY TIEELSYSPQ GILYSRGPNQ YKIPAICDIP TEMHISFLPP SEHSNTLYSS 1260
KGLGESGVFL GCSVFFAIHD AVRAARQERG ISGPWKLTSP LTPEKIRMAC EDKFTKMIPR 1320
DEPGSYVPWN IPV 1333 
Gene Ontology
 GO:0005829; C:cytosol; TAS:RGD.
 GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0004031; F:aldehyde oxidase activity; IDA:RGD.
 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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro.
 GO:0017144; P:drug metabolic process; TAS:RGD.
 GO:0006805; P:xenobiotic metabolic process; TAS:RGD. 
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.
 IPR022407; OxRdtase_Mopterin_BS. 
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
 PS00559; MOLYBDOPTERIN_EUK 
PRINTS