CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039025
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
233ELVEAKFKYPGAPIVacetylation[1]
486AGSAPGGKVEFKRTLacetylation[1]
936QIDNTHYKQEFSAKTacetylation[1]
966ERKTAVGKFNAENSWacetylation[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; Complete proteome; Iron; Iron-sulfur; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1309 AA 
Protein Sequence
MLLPYLRKNL RLTGTKYGCG GGGCGACTVM ISRYNPSTKS IRHHPVNACL TPICSLYGTA 60
VTTVEGIGNT RTRLHPVQER IAKCHGTQCG FCTPGMVMSM YALLRNHPEP SLDQLTDALG 120
GNLCRCTGYR PIIDACKTFC RASGCCESKE NGVCCLDQGI NGSAEFQEGD ETSPELFSEK 180
EFQPLDPTQE LIFPPELMRI AEKQPPKTRV FYSNRMTWIS PVTLEELVEA KFKYPGAPIV 240
MGYTSVGPEV KFKGVFHPII ISPDRIEELS IINQTGDGLT LGAGLSLDQV KDILTDVVQK 300
LPEETTQTYR ALLKHLRTLA GSQIRNMASL GGHIVSRHLD SDLNPLLAVG NCTLNLLSKD 360
GKRQIPLSEQ FLRKCPDSDL KPQEVLVSVN IPFPLSWEFV SAFRQAQRQQ NALAIVNSGM 420
RVLFREGGGV IKELSILYGG VGPTTIGAKN SCQKLIGRPW NEEMLDTACR LVLDEVTLAG 480
SAPGGKVEFK RTLIISFLFK FYLEVLQGLK REDPGHYPSL TNNYESALED LHSKHHWRTL 540
THQNVDSMQL PQDPIGRPIM HLSGIKHATG EAIYCDDMPA VDRELFLTFV TSSRAHAKIV 600
SIDLSEALSL PGVVDIITAD HLQDTTTFGT ETLLATDKVH CVGQLVCAVI ADSETRAKQA 660
AKHVKVVYRD LEPLILTIEE AIQHKSFFES ERKLECGNVD EAFKIADQIL EGEIHIGGQE 720
HFYMETQSML VVPKGEDGEI DIYVSTQFPK HIQDIVAATL KLSVNKVMCH VRRVGGAFGG 780
KVGKTSIMAA ITAFAASKHG RAVRCTLERG EDMLITGGRH PYLGKYKVGF MRDGRIVALD 840
VEHYCNGGSS LDESLWVIEM GLLKMDNAYK FPNLRCRGWA CRTNLPSNTA LRGFGFPQAG 900
LVTEACVTEV AIRCGLSPEQ VRTINMYKQI DNTHYKQEFS AKTLFECWRE CMAKCSYSER 960
KTAVGKFNAE NSWKKRGMAV IPLKFPVGVG SVAMGQAAAL VHIYLDGSAL VSHGGIEMGQ 1020
GVHTKMIQVV SRELKMPMSS VHLRGTSTET VPNTNASGGS VVADLNGLAV KDACQTLLKR 1080
LEPIISKNPQ GTWKDWAQTA FDQSVSLSAV GYFRGYESNI NWEKGEGHPF EYFVYGAACS 1140
EVEIDCLTGD HKNIRTDIVM DVGHSINPAL DIGQVEGAFI QGMGLYTIEE LSYSPQGILY 1200
SRGPNQYKIP AICDIPTEMH ISFLPPSEHS NTLYSSKGLG ESGVFLGCSV FFAIHDAVRA 1260
ARQERGISGP WKLTSPLTPE KIRMACEDKF TKMIPRDEPG SYVPWNIPV 1309 
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:0043546; F:molybdopterin cofactor 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.
 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