| Tag |
Content |
| dbPAF ID |
dbPAF-0052342 |
| Uniprot Accession |
G3X982; AOXC_MOUSE; B2RSI5; Q8VI15;
|
| Genbank Protein ID |
NP_076106.2;
|
| Genbank Nucleotide ID |
NM_023617.2;
|
| Protein Name |
Aldehyde oxidase 3 |
| Protein Synonyms/Alias |
Aldehyde oxidase homolog 1;Azaheterocycle hydroxylase 3; |
| Gene Name |
Aox3 |
| Gene Synonyms/Alias |
Aoh1; |
| Organism |
Mus musculus(Mouse) |
| NCBI Taxa ID |
10090 |
Functional Description
(View all) |
Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor.Functional Description
Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. |
Phosphorylation Sites
|
dbPAF PTMs: 2 |
Sequence
(Fasta) | MSPSKESDEL IFFVNGKKVT ERNADPEVNL LFYLRKVIRL TGTKYGCGGG DCGACTVMIS 60
RYDPISKRIS HFSATACLVP ICSLHGAAVT TVEGIGSTKT RIHPVQERIA KGHGTQCGFC 120
TPGMVMSIYT LLRNHPEPST EQIMETLGGN LCRCTGYRPI VESAKSFCPS STCCQMNGEG 180
KCCLDEEKNE PERKNSVCTK LYEKKEFQPL DPTQELIFPP ELMRMAEESQ NTVLTFRGER 240
TTWIAPGTLN DLLELKMKHP SAPLVIGNTY LGLHMKFTDV SYPIIISPAR ILELFVVTNT 300
KQGLTLGAGL SLTQVKNVLS DVVSRLPKEK TQIYCALLKQ LKTLAGQQIR NVASLGGHII 360
SRLPTSDLNP ILGIGNCILN VASTEGIQQI PLNDHFLAGV PDAILKPEQV LISVFVPRSS 420
KWEFVSAFRQ APRQQNAFAT VNAGMKVVFK EDTNTITDLG ILYGGIGATV ISADKSCRQL 480
IGRCWDEEML DDAGKMICEE VSLLMAAPGG MEEYRKTLAI SFLFMFYLDV LKQLKTRDPH 540
KYPDISQKLL HILEDFPLTM PYGMQSFQDV DFQQPLQDPI GRPIMHQSGI KHATGEAVFC 600
DDMSVLPGEL FLAVVTSSKS HAKIISLDAS EALASLGVVD VVTARDVPGD NGREEESLYA 660
QDEVICVGQI VCAVAADSYA HAQQAAKKVK IVYQDIEPMI VTVQDALQYE SFIGPERKLE 720
QGNVEEAFQC ADQILEGEVH LGGQEHFYME TQSVRVVPKG EDKEMDIYVS SQDAAFTQEM 780
VARTLGIPKN RINCHVKRVG GAFGGKASKP GLLASVAAVA AQKTGRPIRF ILERRDDMLI 840
TGGRHPLLGK YKIGFMNNGK IKAADIQLYI NGGCTPDDSE LVIEYALLKL ENAYKIPNLR 900
VRGRVCKTNL PSNTAFRGFG FPQGAFVTET CMSAVAAKCR LPPEKVRELN MYRTIDRTIH 960
NQEFDPTNLL QCWEACVENS SYYNRKKAVD EFNQQRFWKK RGIAIIPMKF SVGFPKTFYY 1020
QAAALVQIYT DGSVLVAHGG VELGQGINTK MIQVASRELK IPMSYIHLDE MSTVTVPNTV 1080
TTGASTGADV NGRAVQNACQ ILMKRLEPII KQNPSGTWEE WVKEAFVQSI SLSATGYFRG 1140
YQADMDWEKG EGDIFPYFVF GAACSEVEID CLTGAHKNIR TDIVMDGSFS INPAVDIGQI 1200
EGAFVQGLGL YTLEELKYSP EGVLYTRGPH QYKIASVTDI PEEFHVSLLT PTPNPKAIYS 1260
SKGLGEAGTF LGCSVFFAIA AAVAAAREER GLSPIWAINS PATAEVIRMA CEDQFTNLVP 1320
QTDSKCCKPW SIPVA
1336Fasta Sequence
>G3X982|Aox3|Mus musculus(Mouse)
MSPSKESDELIFFVNGKKVTERNADPEVNLLFYLRKVIRLTGTKYGCGGGDCGACTVMISRYDPISKRISHFSATACLVPICSLHGAAVTTVEGIGSTKTRIHPVQERIAKGHGTQCGFCTPGMVMSIYTLLRNHPEPSTEQIMETLGGNLCRCTGYRPIVESAKSFCPSSTCCQMNGEGKCCLDEEKNEPERKNSVCTKLYEKKEFQPLDPTQELIFPPELMRMAEESQNTVLTFRGERTTWIAPGTLNDLLELKMKHPSAPLVIGNTYLGLHMKFTDVSYPIIISPARILELFVVTNTKQGLTLGAGLSLTQVKNVLSDVVSRLPKEKTQIYCALLKQLKTLAGQQIRNVASLGGHIISRLPTSDLNPILGIGNCILNVASTEGIQQIPLNDHFLAGVPDAILKPEQVLISVFVPRSSKWEFVSAFRQAPRQQNAFATVNAGMKVVFKEDTNTITDLGILYGGIGATVISADKSCRQLIGRCWDEEMLDDAGKMICEEVSLLMAAPGGMEEYRKTLAISFLFMFYLDVLKQLKTRDPHKYPDISQKLLHILEDFPLTMPYGMQSFQDVDFQQPLQDPIGRPIMHQSGIKHATGEAVFCDDMSVLPGELFLAVVTSSKSHAKIISLDASEALASLGVVDVVTARDVPGDNGREEESLYAQDEVICVGQIVCAVAADSYAHAQQAAKKVKIVYQDIEPMIVTVQDALQYESFIGPERKLEQGNVEEAFQCADQILEGEVHLGGQEHFYMETQSVRVVPKGEDKEMDIYVSSQDAAFTQEMVARTLGIPKNRINCHVKRVGGAFGGKASKPGLLASVAAVAAQKTGRPIRFILERRDDMLITGGRHPLLGKYKIGFMNNGKIKAADIQLYINGGCTPDDSELVIEYALLKLENAYKIPNLRVRGRVCKTNLPSNTAFRGFGFPQGAFVTETCMSAVAAKCRLPPEKVRELNMYRTIDRTIHNQEFDPTNLLQCWEACVENSSYYNRKKAVDEFNQQRFWKKRGIAIIPMKFSVGFPKTFYYQAAALVQIYTDGSVLVAHGGVELGQGINTKMIQVASRELKIPMSYIHLDEMSTVTVPNTVTTGASTGADVNGRAVQNACQILMKRLEPIIKQNPSGTWEEWVKEAFVQSISLSATGYFRGYQADMDWEKGEGDIFPYFVFGAACSEVEIDCLTGAHKNIRTDIVMDGSFSINPAVDIGQIEGAFVQGLGLYTLEELKYSPEGVLYTRGPHQYKIASVTDIPEEFHVSLLTPTPNPKAIYSSKGLGEAGTFLGCSVFFAIAAAVAAAREERGLSPIWAINSPATAEVIRMACEDQFTNLVPQTDSKCCKPWSIPVA
|
| Keyword |
KW-0001--2Fe-2S
KW-0002--3D-structure
KW-0181--Complete proteome
KW-0963--Cytoplasm
KW-0274--FAD
KW-0285--Flavoprotein
KW-0408--Iron
KW-0411--Iron-sulfur
KW-0479--Metal-binding
KW-0500--Molybdenum
KW-0560--Oxidoreductase
KW-0597--Phosphoprotein
KW-1185--Reference proteome
|
| 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
|
| PROSITE |
PS00197--2FE2S_FER_1
PS51085--2FE2S_FER_2
PS51387--FAD_PCMH
|
| 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
|
| Gene Ontology |
GO:0005737--C:cytoplasm
GO:0051537--F:2 iron, 2 sulfur cluster binding
GO:0004031--F:aldehyde oxidase activity
GO:0009055--F:electron carrier activity
GO:0050660--F:flavin adenine dinucleotide binding
GO:0005506--F:iron ion binding
GO:0030151--F:molybdenum ion binding
GO:0051287--F:NAD binding
GO:0016614--F:oxidoreductase activity, acting on CH-OH group of donors
|
