Reviewed, UniProtKB/Swiss-Prot P48034 (ADO_BOVIN)

Names and origin

Protein names

Recommended name:
    Aldehyde oxidase
    EC=1.2.3.1

Gene names

Name:	AOX1
Synonyms:	AO

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	1339 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	Expressed at high levels in liver, lung and spleen.
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 – 1339	1339	Aldehyde oxidase		PRO_0000166103
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
Experimental info
	Sequence conflict	5	1	S → A in AAI05266. Ref.2
	Sequence conflict	185	1	M → I in AAI05266. Ref.2
	Sequence conflict	804	1	V → I in AAI05266. Ref.2
	Sequence conflict	1060	1	V → A in AAI05266. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P48034-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 3CA7FF9D2B06F655	FASTA	1,339	147,611
	10 20 30 40 50 60 MEGGSELLFY VNGRKVTEKN VDPETMLLPY LRKKLRLTGT KYGCGGGGCG ACTVMISRYN 70 80 90 100 110 120 PITKKIRHYP ANACLTPICS LYGAAVTTVE GIGSTKTRIH PVQERIAKCH GTQCGFCTPG 130 140 150 160 170 180 MVMSLYTLLR NHPEPTLTQL NDALGGNLCR CTGYRPIINA CKTFCKTSGC CQSKENGVCC 190 200 210 220 230 240 LDQGMNGLPE FEEGNETSLK LFSEEEFLPL DPTQELIFPP ELMTMAEKKT QKTRIFGSDR 250 260 270 280 290 300 MTWISPVTLK ELLEAKVKYP QAPVVMGNTS VGPDMKFKGI FHPVIISPDR IEELSVVNYT 310 320 330 340 350 360 DNGLTLGAAV SLAEVKDILA NVTRKLPEEK TQMYHALLKH LETLAGPQIR NMASLGGHIV 370 380 390 400 410 420 SRHPDSDLNP LLAVGNCTLN LLSKEGRRQI PLNEQFLRKC PSADLKPEEI LISVNIPYSR 430 440 450 460 470 480 KWEFVSAFRQ AQRQQNALAI VNSGMRVCFG KGDGIIRELS IAYGGVGPTT ILANNSCQKL 490 500 510 520 530 540 IGRPWNEEML DAACRLILDE VSLPGSAPGG RVEFKRTLIV SFLFKFYLEV SQILKGMDLV 550 560 570 580 590 600 HYPSLASKYE SALEDLHSRH YWSTLKYQNA DLKQLSQDPI GHPIMHLSGI KHATGEAIYC 610 620 630 640 650 660 DDMPVVDREL FLTFVTSSRA HAKIVSIDVS AALSLPGVVD ILTGEHLPGI NTTFGFLTDA 670 680 690 700 710 720 DQLLSTDEVS CVGQLVCAVI ADSEVQARRA AQQVKIVYQD LEPVILTIEE AIQNKSFFEP 730 740 750 760 770 780 ERKLEYGNVD EAFKMVDQIL EGEIHMGGQE HFYMETQSML VVPKGEDREI DVYVSAQFPK 790 800 810 820 830 840 YIQDITASVL KVSANKVMCH VKRVGGAFGG KVTKTGVLAA ITAFAANKHG RPVRCILERG 850 860 870 880 890 900 EDILITGGRH PYLGKYKAGF MNDGRILALD MEHYNNAGAF LDESLFVIEM GLLKLENAYK 910 920 930 940 950 960 FPNLRCRGWA CRTNLPSNTA LRGFGFPQAG LITEACITEV AAKCGLPPEK VRMINMYKEI 970 980 990 1000 1010 1020 DQTPYKQEIN TKNLTQCWKE CMATSSYTLR KAAVEKFNSE NYWKKKGLAM VPLKYPIGLG 1030 1040 1050 1060 1070 1080 SVAAGQAAAL VHIYLDGSVL VTHGGIEMGQ GVHTKMIQVV SRELRMPLSS IHLRGTSTET 1090 1100 1110 1120 1130 1140 IPNTNPSGGS VVADLNGLAV KDACQTLLKR LKPIISKNPK GTWKDWAQAA FNESISLSAT 1150 1160 1170 1180 1190 1200 GYFRGYESNI NWETGEGHPF EYFVYGAACS EVEIDCLTGA HKNIRTDIVM DVGYSINPAL 1210 1220 1230 1240 1250 1260 DVGQIEGAFI QGMGLYTIEE LNYSPQGVLY TRGPNQYKIP AICDIPMELH ISFLPPSENS 1270 1280 1290 1300 1310 1320 NTLYSSKGLG ESGIFLGCSV FFAIHDAIRA ARQERGLPGP LRLNSPLTPE KIRMACEDKF 1330 TKMIPRDEPG SYVPWSVPI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification, cDNA cloning, and tissue distribution of bovine liver aldehyde oxidase." Calzi M.L., Raviolo C., Ghibaudi E., de Gioia L., Salmona M., Cazzaniga G., Kurosaki M., Terao M., Garattini E. J. Biol. Chem. 270:31037-31045(1995) [PubMed: 8537361] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-48; 187-218 AND 538-573. Tissue: Liver.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Uterus.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X87251 mRNA. Translation: CAA60701.1. BC105265 mRNA. Translation: AAI05266.1.
PIR	S46980.
RefSeq	NP_788841.1.
UniGene	Bt.45005
3D structure databases
HSSP	HSSP built from PDB template 1FO4 based on UniProtKB P80457.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000009725. Bos taurus. [Contig view]
GeneID	338074.
KEGG	bta:338074.
Phylogenomic databases
HOVERGEN	P48034.
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_BOVIN

Accession

Primary (citable) accession number: P48034
Secondary accession number(s): Q3MHE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)