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Aldehyde oxidase 1 (EC 1.2.3.1) (Azaheterocycle hydroxylase 1) (EC 1.17.3.-)

 AOXA_RAT                Reviewed;        1333 AA.
Q9Z0U5; Q9R240;
15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
10-OCT-2018, entry version 149.
RecName: Full=Aldehyde oxidase 1 {ECO:0000312|RGD:620528};
EC=1.2.3.1 {ECO:0000250|UniProtKB:O54754};
AltName: Full=Azaheterocycle hydroxylase 1 {ECO:0000305|PubMed:9224775};
EC=1.17.3.- {ECO:0000269|PubMed:9224775};
Name=Aox1 {ECO:0000312|RGD:620528}; Synonyms=Ao;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, BLOCKAGE OF
N-TERMINUS, HOMODIMER, AND VARIANTS 119-ALA-ARG-120; THR-649; LEU-1276
AND ARG-1315.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=9920943; DOI=10.1074/jbc.274.6.3878;
Wright R.M., Clayton D.A., Riley M.G., McManaman J.L., Repine J.E.;
"cDNA cloning, sequencing, and characterization of male and female rat
liver aldehyde oxidase (rAOX1). Differences in redox status may
distinguish male and female forms of hepatic APX.";
J. Biol. Chem. 274:3878-3886(1999).
[2]
FUNCTION AS AZAHETEROCYCLE OXIDASE, CATALYTIC ACTIVITY, ACTIVITY
REGULATION, AND KINETIC PARAMETERS.
PubMed=9224775;
Rashidi M.R., Smith J.A., Clarke S.E., Beedham C.;
"In vitro oxidation of famciclovir and 6-deoxypenciclovir by aldehyde
oxidase from human, guinea pig, rabbit, and rat liver.";
Drug Metab. Dispos. 25:805-813(1997).
[3]
FUNCTION IN SUPEROXIDE PRODUCTION, TISSUE SPECIFICITY, SUBCELLULAR
LOCATION, HOMODIMER, AND COFACTOR.
PubMed=17353002; DOI=10.1016/j.abb.2006.12.032;
Kundu T.K., Hille R., Velayutham M., Zweier J.L.;
"Characterization of superoxide production from aldehyde oxidase: an
important source of oxidants in biological tissues.";
Arch. Biochem. Biophys. 460:113-121(2007).
[4]
FUNCTION IN NITRIC OXIDE PRODUCTION, BIOPHYSICOCHEMICAL PROPERTIES,
AND ACTIVITY REGULATION.
PubMed=19801639; DOI=10.1074/jbc.M109.019125;
Li H., Kundu T.K., Zweier J.L.;
"Characterization of the magnitude and mechanism of aldehyde oxidase-
mediated nitric oxide production from nitrite.";
J. Biol. Chem. 284:33850-33858(2009).
[5]
IDENTIFICATION OF PARALOGS.
PubMed=23263164; DOI=10.1007/s00018-012-1229-5;
Kurosaki M., Bolis M., Fratelli M., Barzago M.M., 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. 70:1807-1830(2013).
[6]
FUNCTION, AND ACTIVITY REGULATION.
PubMed=23282065; DOI=10.3109/00498254.2012.755228;
Hamzeh-Mivehroud M., Rahmani S., Rashidi M.R., Hosseinpour Feizi M.A.,
Dastmalchi S.;
"Structure-based investigation of rat aldehyde oxidase inhibition by
flavonoids.";
Xenobiotica 43:661-670(2013).
-!- FUNCTION: Oxidase with broad substrate specificity, oxidizing
aromatic azaheterocycles, such as N1-methylnicotinamide, N-
methylphthalazinium and phthalazine, as well as aldehydes, such as
benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in
the metabolism of xenobiotics and drugs containing aromatic
azaheterocyclic substituents. Participates in the bioactivation of
prodrugs such as famciclovir, catalyzing the oxidation step from
6-deoxypenciclovir to penciclovir, which is a potent antiviral
agent. Is probably involved in the regulation of reactive oxygen
species homeostasis. Is a prominent source of superoxide
generation via the one-electron reduction of molecular oxygen.
Also catalyzes nitric oxide (NO) production; under anaerobic
conditions, reduces nitrite to NO with NADH or aldehyde as
electron donor, but under aerobic conditions, NADH is the
preferred substrate. These reactions may be catalyzed by several
isozymes. May play a role in adipogenesis.
{ECO:0000269|PubMed:17353002, ECO:0000269|PubMed:19801639,
ECO:0000269|PubMed:23282065, ECO:0000269|PubMed:9224775,
ECO:0000269|PubMed:9920943}.
-!- CATALYTIC ACTIVITY: An aldehyde + H(2)O + O(2) = a carboxylate +
H(2)O(2). {ECO:0000250|UniProtKB:O54754}.
-!- CATALYTIC ACTIVITY: Retinal + O(2) + H(2)O = retinoate + H(2)O(2).
{ECO:0000250|UniProtKB:O54754}.
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000269|PubMed:17353002};
Note=Binds 2 [2Fe-2S] clusters per subunit.
{ECO:0000269|PubMed:17353002};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:17353002};
Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:17353002};
-!- COFACTOR:
Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
Evidence={ECO:0000250|UniProtKB:O54754};
Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
{ECO:0000250|UniProtKB:O54754};
-!- ACTIVITY REGULATION: Inhibited by menadione and isovanillin. Not
inhibited by allopurinol, a xanthine dehydrogenase potent
inhibitor. Inhibited by the flavonoids quercetin, myricetin and
genistein. Nitric oxide generation is inhibited by raloxifene and
competitively inhibited by an increase in oxygen levels.
{ECO:0000269|PubMed:19801639, ECO:0000269|PubMed:23282065,
ECO:0000269|PubMed:9224775}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.37 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH
7) {ECO:0000269|PubMed:9224775};
KM=0.08 mM for famciclovir (at 37 degrees Celsius and pH 7)
{ECO:0000269|PubMed:9224775};
KM=3.0 mM for nitrite {ECO:0000269|PubMed:19801639};
KM=24 uM for NADH {ECO:0000269|PubMed:19801639};
KM=9.6 uM for 4-(dimethylamino)cinnamaldehyde
{ECO:0000269|PubMed:19801639};
Vmax=26 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate
{ECO:0000269|PubMed:9224775};
Vmax=41 nmol/min/mg enzyme with famciclovir as substrate
{ECO:0000269|PubMed:9224775};
Vmax=0.85 umol/sec/mg enzyme for nitrite reduction with NADH as
electron donor {ECO:0000269|PubMed:19801639};
Vmax=1.35 umol/sec/mg enzyme for nitrite reduction with 4-
(dimethylamino)cinnamaldehyde as electron donor
{ECO:0000269|PubMed:19801639};
pH dependence:
Optimum pH is 6.0 for nitrite oxide generation. Activity
decreases below pH 5.0 and above pH 8.0 (PubMed:19801639).
{ECO:0000269|PubMed:19801639};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17353002}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17353002}.
-!- TISSUE SPECIFICITY: Expression in liver (at protein level). Also
detected in heart, lung, spleen and kidney.
{ECO:0000269|PubMed:17353002, ECO:0000269|PubMed:9920943}.
-!- PTM: The N-terminus is blocked.
-!- POLYMORPHISM: The sequence variants between males and females
could be due to differences between individual animals, reflect
gender differences or arise from technical problems
(PubMed:9920943). The sequence shown here is that of a Sprague-
Dawley female. {ECO:0000269|PubMed:9920943}.
-!- MISCELLANEOUS: Male and female rats possess kinetically distinct
forms which may be due to differences in redox states.
{ECO:0000305|PubMed:9920943}.
-!- MISCELLANEOUS: AOX genes evolved from a xanthine oxidoreductase
ancestral precursor via a series of gene duplication and
suppression/deletion events. Different animal species contain a
different complement of AOX genes encoding an equivalent number of
AOX isoenzymes. In mammals, the two extremes are represented by
certain rodents such as mice and rats, which are endowed with 4
AOX genes, and by humans, whose genome is characterized by a
single active gene (PubMed:23263164).
{ECO:0000305|PubMed:23263164}.
-!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
{ECO:0000305}.
-!- CAUTION: The experimental design does not allow to distinguish
AOX1 from AOX3 in rat liver as the effector of the superoxide and
nitric oxide production (PubMed:17353002 and PubMed:19801639).
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF110477; AAD16999.1; -; mRNA.
EMBL; AF110478; AAD17000.1; -; mRNA.
RefSeq; NP_062236.2; NM_019363.3.
UniGene; Rn.15681; -.
ProteinModelPortal; Q9Z0U5; -.
SMR; Q9Z0U5; -.
STRING; 10116.ENSRNOP00000059651; -.
BindingDB; Q9Z0U5; -.
ChEMBL; CHEMBL1641355; -.
iPTMnet; Q9Z0U5; -.
PhosphoSitePlus; Q9Z0U5; -.
PaxDb; Q9Z0U5; -.
PRIDE; Q9Z0U5; -.
GeneID; 54349; -.
KEGG; rno:54349; -.
UCSC; RGD:620528; rat.
CTD; 316; -.
RGD; 620528; Aox1.
eggNOG; KOG0430; Eukaryota.
eggNOG; COG4630; LUCA.
eggNOG; COG4631; LUCA.
HOGENOM; HOG000191197; -.
HOVERGEN; HBG004182; -.
InParanoid; Q9Z0U5; -.
KO; K00157; -.
PhylomeDB; Q9Z0U5; -.
BRENDA; 1.2.3.1; 5301.
SABIO-RK; Q9Z0U5; -.
PRO; PR:Q9Z0U5; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
GO; GO:0004031; F:aldehyde oxidase activity; IDA:RGD.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0071949; F:FAD binding; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
GO; GO:0102797; F:geranial:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
GO; GO:0102798; F:heptaldehyde:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
GO; GO:0043546; F:molybdopterin cofactor binding; ISS:UniProtKB.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0050250; F:retinal oxidase activity; ISS:UniProtKB.
GO; GO:0004854; F:xanthine dehydrogenase activity; IBA:GO_Central.
GO; GO:0017144; P:drug metabolic process; ISS:UniProtKB.
GO; GO:0009115; P:xanthine catabolic process; IBA:GO_Central.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:RGD.
InterPro; IPR002888; 2Fe-2S-bd.
InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
InterPro; IPR006058; 2Fe2S_fd_BS.
InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
InterPro; IPR016208; Ald_Oxase/xanthine_DH.
InterPro; IPR014313; Aldehyde_oxidase.
InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
InterPro; IPR005107; CO_DH_flav_C.
InterPro; IPR036683; CO_DH_flav_C_dom_sf.
InterPro; IPR016166; FAD-bd_PCMH.
InterPro; IPR036318; FAD-bd_PCMH-like_sf.
InterPro; IPR002346; Mopterin_DH_FAD-bd.
InterPro; IPR022407; OxRdtase_Mopterin_BS.
Pfam; PF01315; Ald_Xan_dh_C; 1.
Pfam; PF02738; Ald_Xan_dh_C2; 1.
Pfam; PF03450; CO_deh_flav_C; 1.
Pfam; PF00941; FAD_binding_5; 1.
Pfam; PF00111; Fer2; 1.
Pfam; PF01799; Fer2_2; 1.
PIRSF; PIRSF000127; Xanthine_DH; 1.
SMART; SM01008; Ald_Xan_dh_C; 1.
SMART; SM01092; CO_deh_flav_C; 1.
SUPFAM; SSF47741; SSF47741; 1.
SUPFAM; SSF54292; SSF54292; 1.
SUPFAM; SSF54665; SSF54665; 1.
SUPFAM; SSF55447; SSF55447; 1.
SUPFAM; SSF56003; SSF56003; 1.
SUPFAM; SSF56176; SSF56176; 1.
TIGRFAMs; TIGR02969; mam_aldehyde_ox; 1.
PROSITE; PS00197; 2FE2S_FER_1; 1.
PROSITE; PS51085; 2FE2S_FER_2; 1.
PROSITE; PS51387; FAD_PCMH; 1.
PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
1: Evidence at protein level;
2Fe-2S; Complete proteome; Cytoplasm; FAD; Flavoprotein; Iron;
Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 1333 Aldehyde oxidase 1.
/FTId=PRO_0000166108.
DOMAIN 4 91 2Fe-2S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00465}.
DOMAIN 235 420 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
NP_BIND 263 270 FAD. {ECO:0000250|UniProtKB:Q06278}.
REGION 801 802 Molybdopterin binding.
{ECO:0000250|UniProtKB:Q06278}.
REGION 1083 1086 Molybdopterin binding.
{ECO:0000250|UniProtKB:Q06278}.
ACT_SITE 1265 1265 Proton acceptor; for azaheterocycle
hydroxylase activity.
{ECO:0000250|UniProtKB:O54754}.
METAL 43 43 Iron-sulfur 1 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
METAL 48 48 Iron-sulfur 1 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
METAL 51 51 Iron-sulfur 1 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
METAL 73 73 Iron-sulfur 1 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
METAL 113 113 Iron-sulfur 2 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
METAL 116 116 Iron-sulfur 2 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
METAL 148 148 Iron-sulfur 2 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
METAL 150 150 Iron-sulfur 2 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
BINDING 112 112 Molybdopterin.
{ECO:0000250|UniProtKB:Q06278}.
BINDING 150 150 Molybdopterin.
{ECO:0000250|UniProtKB:Q06278}.
BINDING 344 344 FAD; via amide nitrogen.
{ECO:0000250|UniProtKB:Q06278}.
BINDING 353 353 FAD. {ECO:0000250|UniProtKB:Q06278}.
BINDING 357 357 FAD. {ECO:0000250|UniProtKB:Q06278}.
BINDING 366 366 FAD. {ECO:0000250|UniProtKB:Q06278}.
BINDING 410 410 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250|UniProtKB:Q06278}.
BINDING 1042 1042 Molybdopterin; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q06278}.
BINDING 1198 1198 Molybdopterin.
{ECO:0000250|UniProtKB:Q06278}.
BINDING 1263 1263 Molybdopterin; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q06278}.
MOD_RES 1063 1063 Phosphoserine.
{ECO:0000250|UniProtKB:Q06278}.
VARIANT 119 120 GM -> AR (in Sprague-Dawley males; could
be unrelated to gender).
VARIANT 649 649 A -> T (in Sprague-Dawley males; could be
unrelated to gender).
{ECO:0000269|PubMed:9920943}.
VARIANT 1276 1276 F -> L (in Sprague-Dawley males; could be
unrelated to gender).
{ECO:0000269|PubMed:9920943}.
VARIANT 1315 1315 T -> R (in Sprague-Dawley males; could be
unrelated to gender).
{ECO:0000269|PubMed:9920943}.
SEQUENCE 1333 AA; 146921 MW; 516B6CE395EB05C8 CRC64;
MDPPQLLFYV NGQKVVENNV DPEMMLLPYL RKNLRLTGTK YGCGGGGCGA CTVMISRYNP
STKSIRHHPV NACLTPICSL YGTAVTTVEG IGNTRTRLHP VQERIAKCHS TQCGFCTPGM
VMSMYALLRN HPEPSLDQLT DALGGNLCRC TGYRPIIDAC KTFCRASGCC ESKENGVCCL
DQGINGSAEF QEGDETSPEL FSEKEFQPLD PTQELIFPPE LMRIAEKQPP KTRVFYSNRM
TWISPVTLEE LVEAKFKYPG APIVMGYTSV GPEVKFKGVF HPIIISPDRI EELSIINQTG
DGLTLGAGLS LDQVKDILTD VVQKLPEETT QTYRALLKHL RTLAGSQIRN MASLGGHIVS
RHLDSDLNPL LAVGNCTLNL LSKDGKRQIP LSEQFLRKCP DSDLKPQEVL VSVNIPCSRK
WEFVSAFRQA QRQQNALAIV NSGMRVLFRE GGGVIKELSI LYGGVGPTTI GAKNSCQKLI
GRPWNEEMLD TACRLVLDEV TLAGSAPGGK VEFKRTLIIS FLFKFYLEVL QGLKREDPGH
YPSLTNNYES ALEDLHSKHH WRTLTHQNVD SMQLPQDPIG RPIMHLSGIK HATGEAIYCD
DMPAVDRELF LTFVTSSRAH AKIVSIDLSE ALSLPGVVDI ITADHLQDAT TFGTETLLAT
DKVHCVGQLV CAVIADSETR AKQAAKHVKV VYRDLEPLIL TIEEAIQHKS FFESERKLEC
GNVDEAFKIA DQILEGEIHI GGQEHFYMET QSMLVVPKGE DGEIDIYVST QFPKHIQDIV
AATLKLSVNK VMCHVRRVGG AFGGKVGKTS IMAAITAFAA SKHGRAVRCT LERGEDMLIT
GGRHPYLGKY KVGFMRDGRI VALDVEHYCN GGSSLDESLW VIEMGLLKMD NAYKFPNLRC
RGWACRTNLP SHTALRGFGF PQAGLVTEAC VTEVAIRCGL SPEQVRTINM YKQIDNTHYK
QEFSAKTLFE CWRECMAKCS YSERKTAVGK FNAENSWKKR GMAVIPLKFP VGVGSVAMGQ
AAALVHIYLD GSALVSHGGI EMGQGVHTKM IQVVSRELKM PMSSVHLRGT STETVPNTNA
SGGSVVADLN GLAVKDACQT LLKRLEPIIS KNPQGTWKDW AQTAFDQSVS LSAVGYFRGY
ESNINWEKGE GHPFEYFVYG AACSEVEIDC LTGDHKNIRT DIVMDVGHSI NPALDIGQVE
GAFIQGMGLY TIEELSYSPQ GILYSRGPNQ YKIPAICDIP TEMHISFLPP SEHSNTLYSS
KGLGESGVFL GCSVFFAIHD AVRAARQERG ISGPWKLTSP LTPEKIRMAC EDKFTKMIPR
DEPGSYVPWN IPV


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