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UniProtKB/Swiss-Prot entry P80456

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ADO_RABIT
Primary accession number P80456
Secondary accession number Q9XTA9
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on May 15, 2002 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 63)
Name and origin of the protein
Protein name Aldehyde oxidase
Synonyms EC 1.2.3.1
Retinal oxidase
Gene name
Name: AOX1
Synonyms: AO
From
Oryctolagus cuniculus (Rabbit) [TaxID: 9986] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 857-884; 891-943 AND 1272-1293.
STRAIN=Japanese white;
TISSUE=Liver;
DOI=10.1006/abbi.1999.1129; PubMed=10190983 [NCBI, ExPASy, EBI, Israel, Japan]
Huang D.-Y., Furukawa A., Ichikawa Y.;
"Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli.";
Arch. Biochem. Biophys. 364:264-272(1999).
[2]
 PROTEIN SEQUENCE OF 203-231 AND 574-597.
TISSUE=Liver;
DOI=10.1111/j.1432-1033.1995.tb20856.x; PubMed=7556219 [NCBI, ExPASy, EBI, Israel, Japan]
Turner N.A., Doyle W.A., Ventom A.M., Bray R.C.;
"Properties of rabbit liver aldehyde oxidase and the relationship of the enzyme to xanthine oxidase and dehydrogenase.";
Eur. J. Biochem. 232:646-657(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB009345; BAA81726.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001075459.1; -.
UniGene Ocu.2359
3D structure databases
HSSP P80457; 1FO4. [HSSP ENTRY / PDB]
ModBase P80456.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0051537; Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004031; Molecular function: aldehyde oxidase activity (inferred from electronic annotation from EC).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0030151; Molecular function: molybdenum ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002888; 2Fe-2S_bd.
IPR006058; 2Fe2S_fd_BS.
IPR000674; Ald_Oxase/Xan_DHase_a/b.
IPR016208; Ald_Oxase/xanthine_DHase.
IPR014313; Aldehyde_oxidase.
IPR008274; AldOxase/xan_DHase_Mopterin-bd.
IPR012675; b-grasp_ferredoxin-like.
IPR005107; CO_DHase_flav_C.
IPR016169; CO_DHase_flavot_FAD-bd_sub2.
IPR016167; FAD-bd_2_sub1.
IPR001041; Ferredoxin.
IPR002346; Mopterin_DHase_FAD-bd.
IPR000572; OxRdtase_Mopterin-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.365.10; Ald_xan_DH_mo_bd; 2.
G3DSA:3.90.1170.50; Aldxan_DH_hamm; 1.
G3DSA:3.30.390.50; CO_DH_flav_C; 1.
G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1.
G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
G3DSA:3.10.20.30; Ferredoxin_fold; 1.
Pfam PF01315; Ald_Xan_dh_C; 1.
PF02738; Ald_Xan_dh_C2; 1.
PF03450; CO_deh_flav_C; 1.
PF00941; FAD_binding_5; 1.
PF00111; Fer2; 1.
PF01799; Fer2_2; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000127; Xanthine_DH; 1.
ProDom PD186071; 2Fe-2S_bind; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR02969; mam_aldehyde_ox; 1.
PROSITE PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS51387; FAD_PCMH; 1.
PS00559; MOLYBDOPTERIN_EUK; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P80456.
Genome annotation databases
GeneID 100008601; -.
Phylogenomic databases
HOVERGEN P80456; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   1334  1334     Aldehyde oxidase. PRO_0000166107
DOMAIN   5     92  88     2Fe-2S ferredoxin-type. 
DOMAIN   236    421  186     FAD-binding PCMH-type. 
METAL   44     44        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   49     49        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   52     52        Iron-sulfur (2Fe-2S) (By similarity). 
Sequence information
Length: 1334 AA [This is the length of the unprocessed precursor] Molecular weight: 147138 Da [This is the MW of the unprocessed precursor] CRC64: 0747A0569C2C062A [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MEPAPELLFY VNGRKVVEKQ VDPETMLLPY LRKKLRLTGT KYGCGGGGCG ACTVMISRYN 

        70         80         90        100        110        120 
RVTKKIRHYP VNACLTPICS LYGAAVTTVE GIGSTTTRLH PVQERIAKFH GTQCGFCTPG 

       130        140        150        160        170        180 
MVMSMYALLR NHPEPTLDQL ADALGGNLCR CTGYRPIIEA YKTFCKTSDC CQNKENGFCC 

       190        200        210        220        230        240 
LDQGINGLPE VEEENQTRPN LFSEEEYLPL DPTQELIFPP ELMTMAEKQP QRTRVFSGER 

       250        260        270        280        290        300 
MMWISPVTLK ALLEAKSTYP QAPVVMGNTS VGPGVKFKGI FHPVIISPDS IEELNVVSHT 

       310        320        330        340        350        360 
HSGLTLGAGL SLAQVKDILA DVVQKVPEEN AQTYRALLKH LGTLAGSQIR NMASLGGHII 

       370        380        390        400        410        420 
SRHLDSDLNP LLAVGNCTLN VLSKEGERQI PLDEQFLSRC PEADLKPQEI LASVHIPYSR 

       430        440        450        460        470        480 
KWEFVLAFRQ AQRKQNALAI VNSGMRVFFG EGDGIIRELA ISYGGVGPTI ICAKNSCQKL 

       490        500        510        520        530        540 
IGRSWNEEML DTACRLILDE VSLPGSAPGG KVEFKRTLII SFLFKFYLEV SQILKRMAPG 

       550        560        570        580        590        600 
LSPHLADKYE SALQDLHARY SWSTLKDQDV DARQLSQDPI GHPVMHLSGV KHATGEAIYL 

       610        620        630        640        650        660 
DDMPAVDQEL FMAFVTSPRA HAKIVSTDLL EALSLPGVVD IVTAEHLQDG NTFYTEKLLA 

       670        680        690        700        710        720 
ADEVLCVGQL VCAVIAESEV QAKQAAKQVK IVYEDLEPVI LSIEEAIEQK SFFEPERKLE 

       730        740        750        760        770        780 
YGNVDEAFKV VDQILEGEIH MGGQEHFYME TQSVLVVPKG EDQEMDVYAS TQFPKYIQDM 

       790        800        810        820        830        840 
VAAVLKLPVN KVMCHVKRVG GAFGGKVFKA SIMAAIAAFA ANKHGRAVRC ILERGEDMLI 

       850        860        870        880        890        900 
TGGRHPYLGK YKAGFMNDGR IVALDVEHYS NGGCSLDESL LVIEMGLLKM ENAYKFPNLR 

       910        920        930        940        950        960 
CRGWACRTNL PSNTAFRGFG FPQAGLITEC CITEVAAKCG LSPEKVRAIN FYKEIDQTPY 

       970        980        990       1000       1010       1020 
KQEINAKNLT QCWNECLAKS SYFQRKVAVE KFNAENYWKQ RGLAIIPFKY PRGLGSVAYG 

      1030       1040       1050       1060       1070       1080 
QAAALVHVYL DGSVLVTHGG IEMGQGVHTK MIQVVSRELK MPMSNVHLRG TSTETVPNTN 

      1090       1100       1110       1120       1130       1140 
ASGGSVVADL NGLAVKDACQ TLLKRLEPII NKNPQGTWKE WAQAAFDKSI SLSATGYFRG 

      1150       1160       1170       1180       1190       1200 
YDSNIDWDKG EGHPFEYFVY GAACSEVEID CLTGDHKTIR TDIVMDVGYS INPALDIGQV 

      1210       1220       1230       1240       1250       1260 
EGAFIQGMGL YTIEELHYSP QGILYSRGPN QYKIPAICDI PAELNVTFLP PSEKSNTLYS 

      1270       1280       1290       1300       1310       1320 
SKGLGESGVF MGCSVFFAIR EAVCAARQAR GLSAPWKLSS PLTPEKIRMA CEDKFTKMIP 

      1330 
RDKPGSYVPW NVPV
P80456 in FASTA format

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