Reviewed, UniProtKB/Swiss-Prot P80456 (ADO_RABIT)

Names and origin

Protein names

Recommended name:
    Aldehyde oxidase
    EC=1.2.3.1
Alternative name(s):
    Retinal oxidase

Gene names

Name:	AOX1
Synonyms:	AO

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	1334 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	An aldehyde + H(2)O + O(2) = a carboxylic acid + H(2)O(2).
Cofactor	Binds 2 2Fe-2S clusters. FAD. Molybdopterin.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Tissue specificity	Very high expression in liver and lung. High expression in kidney, pancreas, brain stem and spinal cord. Moderate expression in heart, testis, eye, cerebral cortex and cerebellum. Low expression in stomach and muscle.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the xanthine dehydrogenase family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding PCMH-type domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FAD binding Inferred from electronic annotation. Source: InterPro NAD binding Inferred from electronic annotation. Source: InterPro aldehyde oxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1334	1334	Aldehyde oxidase		PRO_0000166107
Regions
	Domain	5 – 92	88	2Fe-2S ferredoxin-type
	Domain	236 – 421	186	FAD-binding PCMH-type
Sites
	Metal binding	44	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	49	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	52	1	Iron-sulfur (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P80456-1 [UniParc]. Last modified May 15, 2002. Version 2. Checksum: 0747A0569C2C062A	FASTA	1,334	147,138
	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

References

[1]

"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." Huang D.-Y., Furukawa A., Ichikawa Y. Arch. Biochem. Biophys. 364:264-272(1999) [PubMed: 10190983] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 857-884; 891-943 AND 1272-1293. Strain: Japanese white. Tissue: Liver.

[2]

"Properties of rabbit liver aldehyde oxidase and the relationship of the enzyme to xanthine oxidase and dehydrogenase." Turner N.A., Doyle W.A., Ventom A.M., Bray R.C. Eur. J. Biochem. 232:646-657(1995) [PubMed: 7556219] [Abstract] Cited for: PROTEIN SEQUENCE OF 203-231 AND 574-597. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB009345 mRNA. Translation: BAA81726.1.
RefSeq	NP_001075459.1.
UniGene	Ocu.2359
3D structure databases
HSSP	HSSP built from PDB template 1FO4 based on UniProtKB P80457.
ModBase	Search...
Genome annotation databases
GeneID	100008601.
Phylogenomic databases
HOVERGEN	P80456.
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]
Gene3D	G3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 2 hits. G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit. G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit. G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit. G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF01315. Ald_Xan_dh_C. 1 hit. PF02738. Ald_Xan_dh_C2. 1 hit. PF03450. CO_deh_flav_C. 1 hit. PF00941. FAD_binding_5. 1 hit. PF00111. Fer2. 1 hit. PF01799. Fer2_2. 1 hit. [Graphical view]
PIRSF	PIRSF000127. Xanthine_DH. 1 hit.
ProDom	PD186071. 2Fe-2S_bind. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR02969. mam_aldehyde_ox. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. PS00559. MOLYBDOPTERIN_EUK. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADO_RABIT

Accession

Primary (citable) accession number: P80456
Secondary accession number(s): Q9XTA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	May 15, 2002
Last modified:	November 25, 2008
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)