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Showing Protein Aldehyde oxidase 2 (HMDBP14041)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP14041
Secondary Accession Numbers None
Name Aldehyde oxidase 2
Synonyms
  1. Aldehyde oxidase homolog 3
  2. Azaheterocycle hydroxylase 2
Gene Name AOX2
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal.
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
drug metabolic process
Cellular Component
cytosol
Molecular Function
electron carrier activity
protein homodimerization activity
flavin adenine dinucleotide binding
iron ion binding
FAD binding
aldehyde oxidase activity
2 iron, 2 sulfur cluster binding
molybdopterin cofactor binding
geranial:oxygen oxidoreductase activity
heptaldehyde:oxygen oxidoreductase activity
retinal oxidase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues Not Available
Molecular Weight 144922.87
Theoretical pI Not Available
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID H9TB19
UniProtKB/Swiss-Prot Entry Name AOXB_CAVPO
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Kurosaki M, Bolis M, Fratelli M, Barzago MM, Pattini L, Perretta G, Terao M, Garattini E: Structure and evolution of vertebrate aldehyde oxidases: from gene duplication to gene suppression. Cell Mol Life Sci. 2013 May;70(10):1807-30. doi: 10.1007/s00018-012-1229-5. Epub 2012 Dec 21. [PubMed:23263164 ]
  2. Lindblad-Toh K, Garber M, Zuk O, Lin MF, Parker BJ, Washietl S, Kheradpour P, Ernst J, Jordan G, Mauceli E, Ward LD, Lowe CB, Holloway AK, Clamp M, Gnerre S, Alfoldi J, Beal K, Chang J, Clawson H, Cuff J, Di Palma F, Fitzgerald S, Flicek P, Guttman M, Hubisz MJ, Jaffe DB, Jungreis I, Kent WJ, Kostka D, Lara M, Martins AL, Massingham T, Moltke I, Raney BJ, Rasmussen MD, Robinson J, Stark A, Vilella AJ, Wen J, Xie X, Zody MC, Baldwin J, Bloom T, Chin CW, Heiman D, Nicol R, Nusbaum C, Young S, Wilkinson J, Worley KC, Kovar CL, Muzny DM, Gibbs RA, Cree A, Dihn HH, Fowler G, Jhangiani S, Joshi V, Lee S, Lewis LR, Nazareth LV, Okwuonu G, Santibanez J, Warren WC, Mardis ER, Weinstock GM, Wilson RK, Delehaunty K, Dooling D, Fronik C, Fulton L, Fulton B, Graves T, Minx P, Sodergren E, Birney E, Margulies EH, Herrero J, Green ED, Haussler D, Siepel A, Goldman N, Pollard KS, Pedersen JS, Lander ES, Kellis M: A high-resolution map of human evolutionary constraint using 29 mammals. Nature. 2011 Oct 12;478(7370):476-82. doi: 10.1038/nature10530. [PubMed:21993624 ]