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Aldehyde oxidase 1 (EC 1.2.3.1) (Azaheterocycle hydroxylase 1) (EC 1.17.3.-) (Retinal oxidase) (Retinoic acid synthase)

 AOXA_RABIT              Reviewed;        1334 AA.
P80456; Q9XTA9;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
15-MAY-2002, sequence version 2.
30-AUG-2017, entry version 128.
RecName: Full=Aldehyde oxidase 1 {ECO:0000250|UniProtKB:Q06278};
EC=1.2.3.1 {ECO:0000269|PubMed:8305467, ECO:0000269|PubMed:9224775};
AltName: Full=Azaheterocycle hydroxylase 1;
EC=1.17.3.-;
AltName: Full=Retinal oxidase;
AltName: Full=Retinoic acid synthase;
Name=AOX1 {ECO:0000250|UniProtKB:Q06278}; Synonyms=AO;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 857-884; 891-943 AND
1272-1293, FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=Japanese white; TISSUE=Liver;
PubMed=10190983; DOI=10.1006/abbi.1999.1129;
Huang D.-Y., Furukawa A., Ichikawa Y.;
"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.";
Arch. Biochem. Biophys. 364:264-272(1999).
[2]
PROTEIN SEQUENCE OF 203-231 AND 574-597, FUNCTION AS OXIDASE, AND
COFACTOR.
TISSUE=Liver;
PubMed=7556219; DOI=10.1111/j.1432-1033.1995.646zz.x;
Turner N.A., Doyle W.A., Ventom A.M., Bray R.C.;
"Properties of rabbit liver aldehyde oxidase and the relationship of
the enzyme to xanthine oxidase and dehydrogenase.";
Eur. J. Biochem. 232:646-657(1995).
[3]
FUNCTION AS OXIDASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
BIOPHYSICOCHEMICAL PROPERTIES, HOMODIMER, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, REACTION MECHANISM, BLOCKAGE OF N-TERMINUS, AND ENZYME
REGULATION.
PubMed=8305467; DOI=10.1016/0167-4838(94)90039-6;
Tsujita M., Tomita S., Miura S., Ichikawa Y.;
"Characteristic properties of retinal oxidase (retinoic acid synthase)
from rabbit hepatocytes.";
Biochim. Biophys. Acta 1204:108-116(1994).
[4]
FUNCTION AS AZAHETEROCYCLE OXIDASE, CATALYTIC ACTIVITY, ENZYME
REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
[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).
-!- 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 key 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. 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. May play
a role in adipogenesis. Cannot use hypoxanthine and all-trans-
retinol as substrate. {ECO:0000269|PubMed:10190983,
ECO:0000269|PubMed:7556219, ECO:0000269|PubMed:8305467,
ECO:0000269|PubMed:9224775}.
-!- CATALYTIC ACTIVITY: An aldehyde + H(2)O + O(2) = a carboxylate +
H(2)O(2). {ECO:0000269|PubMed:8305467,
ECO:0000269|PubMed:9224775}.
-!- CATALYTIC ACTIVITY: Retinal + O(2) + H(2)O = retinoate + H(2)O(2).
{ECO:0000269|PubMed:8305467, ECO:0000269|PubMed:9224775}.
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000269|PubMed:7556219,
ECO:0000269|PubMed:8305467};
Note=Binds 2 [2Fe-2S] clusters per subunit.
{ECO:0000269|PubMed:7556219, ECO:0000269|PubMed:8305467};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:7556219,
ECO:0000269|PubMed:8305467};
Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:7556219,
ECO:0000269|PubMed:8305467};
-!- COFACTOR:
Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
Evidence={ECO:0000269|PubMed:7556219,
ECO:0000269|PubMed:8305467};
Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
{ECO:0000269|PubMed:7556219, ECO:0000269|PubMed:8305467};
-!- ENZYME REGULATION: Inhibited by hydralazine and menadione. Not
inhibited by BOF-4272 or allopurinol, xanthine dehydrogenase
potent inhibitors. In contrast to guinea pig, human and rat,
isovanillin is not an inhibitor but a substrate for AOX1 in
rabbit. {ECO:0000269|PubMed:8305467, ECO:0000269|PubMed:9224775}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=8 uM for all-trans-retinal {ECO:0000269|PubMed:8305467,
ECO:0000269|PubMed:9224775};
KM=13 uM for 9-cis-retinal {ECO:0000269|PubMed:8305467,
ECO:0000269|PubMed:9224775};
KM=0.9 mM for 13-cis-retinal {ECO:0000269|PubMed:8305467,
ECO:0000269|PubMed:9224775};
KM=0.11 mM for N-methylnicotinamide {ECO:0000269|PubMed:8305467,
ECO:0000269|PubMed:9224775};
KM=94.7 uM for O(2) {ECO:0000269|PubMed:8305467,
ECO:0000269|PubMed:9224775};
KM=0.44 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH
7) {ECO:0000269|PubMed:8305467, ECO:0000269|PubMed:9224775};
KM=45 uM for isovanillin (at 37 degrees Celsius and pH 7)
{ECO:0000269|PubMed:8305467, ECO:0000269|PubMed:9224775};
Vmax=192 nmol/min/mg enzyme with all-trans-retinal as substrate
{ECO:0000269|PubMed:8305467, ECO:0000269|PubMed:9224775};
Vmax=57 nmol/min/mg enzyme with 9-cis-retinal as substrate
{ECO:0000269|PubMed:8305467, ECO:0000269|PubMed:9224775};
Vmax=105 nmol/min/mg enzyme with 13-cis-retinal as substrate
{ECO:0000269|PubMed:8305467, ECO:0000269|PubMed:9224775};
Vmax=267 nmol/min/mg enzyme with N-methylnicotinamide as
substrate {ECO:0000269|PubMed:8305467,
ECO:0000269|PubMed:9224775};
Vmax=114 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate
{ECO:0000269|PubMed:8305467, ECO:0000269|PubMed:9224775};
Vmax=211 nmol/min/mg enzyme with isovanillin as substrate
{ECO:0000269|PubMed:8305467, ECO:0000269|PubMed:9224775};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8305467}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8305467}.
-!- 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.
{ECO:0000269|PubMed:10190983, ECO:0000269|PubMed:8305467}.
-!- PTM: The N-terminus is blocked.
-!- MISCELLANEOUS: The reaction follows an ordered Bi-Bi kinetic
mechanism. During retinal oxidation, incorporates the oxygen of
water into retinoate, but not that of molecular oxygen
(PubMed:8305467). {ECO:0000305|PubMed:8305467}.
-!- 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}.
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EMBL; AB009345; BAA81726.1; -; mRNA.
RefSeq; NP_001075459.1; NM_001081990.1.
UniGene; Ocu.2359; -.
ProteinModelPortal; P80456; -.
SMR; P80456; -.
STRING; 9986.ENSOCUP00000012025; -.
BindingDB; P80456; -.
ChEMBL; CHEMBL1641356; -.
GeneID; 100008601; -.
KEGG; ocu:100008601; -.
CTD; 316; -.
eggNOG; KOG0430; Eukaryota.
eggNOG; COG4630; LUCA.
eggNOG; COG4631; LUCA.
HOGENOM; HOG000191197; -.
HOVERGEN; HBG004182; -.
InParanoid; P80456; -.
KO; K00157; -.
BRENDA; 1.2.3.1; 1749.
SABIO-RK; P80456; -.
PRO; PR:P80456; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0004031; F:aldehyde oxidase activity; IEA:UniProtKB-EC.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
Gene3D; 1.10.150.120; -; 1.
Gene3D; 3.10.20.30; -; 1.
Gene3D; 3.30.365.10; -; 4.
Gene3D; 3.30.43.10; -; 1.
Gene3D; 3.30.465.10; -; 1.
Gene3D; 3.90.1170.50; -; 1.
InterPro; IPR002888; 2Fe-2S-bd.
InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
InterPro; IPR006058; 2Fe2S_fd_BS.
InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
InterPro; IPR016208; Ald_Oxase/xanthine_DH.
InterPro; IPR014313; Aldehyde_oxidase.
InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
InterPro; IPR012675; Beta-grasp_dom.
InterPro; IPR005107; CO_DH_flav_C.
InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
InterPro; IPR016166; FAD-bd_2.
InterPro; IPR016167; FAD-bd_2_sub1.
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; Direct protein sequencing; FAD;
Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum;
Oxidoreductase; Phosphoprotein; Reference proteome.
CHAIN 1 1334 Aldehyde oxidase 1.
/FTId=PRO_0000166107.
DOMAIN 5 92 2Fe-2S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00465}.
DOMAIN 236 421 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
NP_BIND 264 271 FAD. {ECO:0000250|UniProtKB:Q06278}.
REGION 802 803 Molybdopterin binding.
{ECO:0000250|UniProtKB:Q06278}.
REGION 1084 1087 Molybdopterin binding.
{ECO:0000250|UniProtKB:Q06278}.
ACT_SITE 1266 1266 Proton acceptor; for azaheterocycle
hydroxylase activity.
{ECO:0000250|UniProtKB:O54754}.
METAL 44 44 Iron-sulfur 1 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
METAL 49 49 Iron-sulfur 1 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
METAL 52 52 Iron-sulfur 1 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
METAL 74 74 Iron-sulfur 1 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
METAL 114 114 Iron-sulfur 2 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
METAL 117 117 Iron-sulfur 2 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
METAL 149 149 Iron-sulfur 2 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
METAL 151 151 Iron-sulfur 2 (2Fe-2S).
{ECO:0000250|UniProtKB:Q06278}.
BINDING 113 113 Molybdopterin.
{ECO:0000250|UniProtKB:Q06278}.
BINDING 151 151 Molybdopterin.
{ECO:0000250|UniProtKB:Q06278}.
BINDING 345 345 FAD; via amide nitrogen.
{ECO:0000250|UniProtKB:Q06278}.
BINDING 354 354 FAD. {ECO:0000250|UniProtKB:Q06278}.
BINDING 358 358 FAD. {ECO:0000250|UniProtKB:Q06278}.
BINDING 367 367 FAD. {ECO:0000250|UniProtKB:Q06278}.
BINDING 411 411 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250|UniProtKB:Q06278}.
BINDING 1043 1043 Molybdopterin; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q06278}.
BINDING 1199 1199 Molybdopterin.
{ECO:0000250|UniProtKB:Q06278}.
BINDING 1264 1264 Molybdopterin; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q06278}.
MOD_RES 1064 1064 Phosphoserine.
{ECO:0000250|UniProtKB:Q06278}.
SEQUENCE 1334 AA; 147138 MW; 0747A0569C2C062A CRC64;
MEPAPELLFY VNGRKVVEKQ VDPETMLLPY LRKKLRLTGT KYGCGGGGCG ACTVMISRYN
RVTKKIRHYP VNACLTPICS LYGAAVTTVE GIGSTTTRLH PVQERIAKFH GTQCGFCTPG
MVMSMYALLR NHPEPTLDQL ADALGGNLCR CTGYRPIIEA YKTFCKTSDC CQNKENGFCC
LDQGINGLPE VEEENQTRPN LFSEEEYLPL DPTQELIFPP ELMTMAEKQP QRTRVFSGER
MMWISPVTLK ALLEAKSTYP QAPVVMGNTS VGPGVKFKGI FHPVIISPDS IEELNVVSHT
HSGLTLGAGL SLAQVKDILA DVVQKVPEEN AQTYRALLKH LGTLAGSQIR NMASLGGHII
SRHLDSDLNP LLAVGNCTLN VLSKEGERQI PLDEQFLSRC PEADLKPQEI LASVHIPYSR
KWEFVLAFRQ AQRKQNALAI VNSGMRVFFG EGDGIIRELA ISYGGVGPTI ICAKNSCQKL
IGRSWNEEML DTACRLILDE VSLPGSAPGG KVEFKRTLII SFLFKFYLEV SQILKRMAPG
LSPHLADKYE SALQDLHARY SWSTLKDQDV DARQLSQDPI GHPVMHLSGV KHATGEAIYL
DDMPAVDQEL FMAFVTSPRA HAKIVSTDLL EALSLPGVVD IVTAEHLQDG NTFYTEKLLA
ADEVLCVGQL VCAVIAESEV QAKQAAKQVK IVYEDLEPVI LSIEEAIEQK SFFEPERKLE
YGNVDEAFKV VDQILEGEIH MGGQEHFYME TQSVLVVPKG EDQEMDVYAS TQFPKYIQDM
VAAVLKLPVN KVMCHVKRVG GAFGGKVFKA SIMAAIAAFA ANKHGRAVRC ILERGEDMLI
TGGRHPYLGK YKAGFMNDGR IVALDVEHYS NGGCSLDESL LVIEMGLLKM ENAYKFPNLR
CRGWACRTNL PSNTAFRGFG FPQAGLITEC CITEVAAKCG LSPEKVRAIN FYKEIDQTPY
KQEINAKNLT QCWNECLAKS SYFQRKVAVE KFNAENYWKQ RGLAIIPFKY PRGLGSVAYG
QAAALVHVYL DGSVLVTHGG IEMGQGVHTK MIQVVSRELK MPMSNVHLRG TSTETVPNTN
ASGGSVVADL NGLAVKDACQ TLLKRLEPII NKNPQGTWKE WAQAAFDKSI SLSATGYFRG
YDSNIDWDKG EGHPFEYFVY GAACSEVEID CLTGDHKTIR TDIVMDVGYS INPALDIGQV
EGAFIQGMGL YTIEELHYSP QGILYSRGPN QYKIPAICDI PAELNVTFLP PSEKSNTLYS
SKGLGESGVF MGCSVFFAIR EAVCAARQAR GLSAPWKLSS PLTPEKIRMA CEDKFTKMIP
RDKPGSYVPW NVPV


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Genprice Inc, Invoices and accounting
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