AOXA_MOUSE
ID AOXA_MOUSE Reviewed; 1333 AA.
AC O54754; Q9WU85; Q9Z2Z5;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Aldehyde oxidase 1 {ECO:0000312|MGI:MGI:88035};
DE EC=1.2.3.1 {ECO:0000269|PubMed:10190983, ECO:0000269|PubMed:19401776};
DE AltName: Full=Azaheterocycle hydroxylase 1;
DE EC=1.17.3.-;
DE AltName: Full=Retinal oxidase {ECO:0000303|PubMed:10190983};
GN Name=Aox1 {ECO:0000312|MGI:MGI:88035}; Synonyms=Ao, Ro;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Liver;
RX PubMed=10377246; DOI=10.1042/bj3410071;
RA Kurosaki M., Demontis S., Barzago M.M., Garattini E., Terao M.;
RT "Molecular cloning of the cDNA coding for mouse aldehyde oxidase: tissue
RT distribution and regulation in vivo by testosterone.";
RL Biochem. J. 341:71-80(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS RETINAL OXIDASE, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND HOMODIMER.
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=10190983; DOI=10.1006/abbi.1999.1129;
RA Huang D.-Y., Furukawa A., Ichikawa Y.;
RT "Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit
RT and mouse livers and functional expression of recombinant mouse retinal
RT oxidase cDNA in Escherichia coli.";
RL Arch. Biochem. Biophys. 364:264-272(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=129/Sv; TISSUE=Thymus;
RX PubMed=10673024; DOI=10.1016/s0167-4781(99)00174-8;
RA Demontis S., Kurosaki M., Saccone S., Salvatore M., Garattini E., Terao M.;
RT "The mouse aldehyde oxidase gene: molecular cloning, chromosomal mapping
RT and functional characterization of the 5'-flanking region.";
RL Biochim. Biophys. Acta 1489:207-222(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 561-746, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=9243637; DOI=10.1097/00001756-199707070-00048;
RA Bendotti C., Prosperini E., Kurosaki M., Garattini E., Terao M.;
RT "Selective localization of mouse aldehyde oxidase mRNA in the choroid
RT plexus and motor neurons.";
RL NeuroReport 8:2343-2349(1997).
RN [5]
RP FUNCTION IN ADIPOGENESIS, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=18671973; DOI=10.1016/j.febslet.2008.07.034;
RA Weigert J., Neumeier M., Bauer S., Mages W., Schnitzbauer A.A., Obed A.,
RA Groeschl B., Hartmann A., Schaeffler A., Aslanidis C., Schoelmerich J.,
RA Buechler C.;
RT "Small-interference RNA-mediated knock-down of aldehyde oxidase 1 in 3T3-L1
RT cells impairs adipogenesis and adiponectin release.";
RL FEBS Lett. 582:2965-2972(2008).
RN [6]
RP FUNCTION AS OXIDASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, HOMODIMER,
RP KINETIC PARAMETERS, REACTION MECHANISM, ACTIVE SITE, AND MUTAGENESIS OF
RP VAL-806; MET-884 AND GLU-1265.
RX PubMed=19401776; DOI=10.1371/journal.pone.0005348;
RA Schumann S., Terao M., Garattini E., Saggu M., Lendzian F., Hildebrandt P.,
RA Leimkuhler S.;
RT "Site directed mutagenesis of amino acid residues at the active site of
RT mouse aldehyde oxidase AOX1.";
RL PLoS ONE 4:E5348-E5348(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP TISSUE SPECIFICITY, AND IDENTIFICATION OF PARALOGS.
RX PubMed=23263164; DOI=10.1007/s00018-012-1229-5;
RA Kurosaki M., Bolis M., Fratelli M., Barzago M.M., Pattini L., Perretta G.,
RA Terao M., Garattini E.;
RT "Structure and evolution of vertebrate aldehyde oxidases: from gene
RT duplication to gene suppression.";
RL Cell. Mol. Life Sci. 70:1807-1830(2013).
RN [9]
RP FUNCTION IN XENOBIOTIC METABOLISM, AND TISSUE SPECIFICITY.
RX PubMed=23462233; DOI=10.1093/toxsci/kft066;
RA Swenson T.L., Casida J.E.;
RT "Aldehyde oxidase importance in vivo in xenobiotic metabolism: imidacloprid
RT nitroreduction in mice.";
RL Toxicol. Sci. 133:22-28(2013).
CC -!- FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic
CC azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium
CC and phthalazine, as well as aldehydes, such as benzaldehyde, retinal,
CC pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics
CC and drugs containing aromatic azaheterocyclic substituents.
CC Participates in the bioactivation of prodrugs such as famciclovir,
CC catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir,
CC which is a potent antiviral agent. Also plays a role in the reductive
CC metabolism of the xenobiotic imidacloprid (IMI) via its nitroreduction
CC to nitrosoguanidine (IMI-NNO) and aminoguanidine (IMI-NNH(2)). Is
CC probably involved in the regulation of reactive oxygen species
CC homeostasis. May be a prominent source of superoxide generation via the
CC one-electron reduction of molecular oxygen. May also catalyze nitric
CC oxide (NO) production via the reduction of nitrite to NO with NADH or
CC aldehyde as electron donor. May play a role in adipogenesis. Cannot use
CC xanthine and hypoxanthine as substrate. {ECO:0000269|PubMed:10190983,
CC ECO:0000269|PubMed:18671973, ECO:0000269|PubMed:19401776,
CC ECO:0000269|PubMed:23462233}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2;
CC Xref=Rhea:RHEA:16829, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:29067; EC=1.2.3.1; Evidence={ECO:0000269|PubMed:10190983,
CC ECO:0000269|PubMed:19401776};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + retinal = H(+) + H2O2 + retinoate;
CC Xref=Rhea:RHEA:56736, ChEBI:CHEBI:15035, ChEBI:CHEBI:15036,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240; Evidence={ECO:0000269|PubMed:10190983,
CC ECO:0000269|PubMed:19401776};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:19401776};
CC Note=Binds 2 [2Fe-2S] clusters per subunit.
CC {ECO:0000269|PubMed:19401776};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:19401776};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:19401776};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000269|PubMed:19401776};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000269|PubMed:19401776};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.8 uM for retinal (at 37 degrees Celsius and pH 7.8)
CC {ECO:0000269|PubMed:10190983};
CC KM=97.7 uM for benzaldehyde (at 30 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:19401776};
CC KM=11.4 uM for phthalazine (at 30 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:19401776};
CC KM=55.8 uM for retinal (at 30 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:19401776};
CC KM=17.5 mM for acetaldehyde (at 30 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:19401776};
CC Vmax=807 nmol/min/mg enzyme with retinal as substrate (at 37 degrees
CC Celsius and pH 7.8) {ECO:0000269|PubMed:10190983};
CC Note=kcat is 317.6 min(-1) for benzaldehyde oxidation, 128.1 min(-1)
CC for phthalazine oxidation, 49.5 min(-1) for retinal oxidation, and
CC 519.9 min(-1) for acetaldehyde oxidation (at 30 degrees Celsius and
CC pH 7.5) (PubMed:19401776). However in this article, the measures are
CC done with the recombinant protein, which is only 20% active, due to
CC an incomplete saturation of the molybdenum cofactor with the sulfido
CC ligand (PubMed:19401776). {ECO:0000269|PubMed:19401776};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19401776}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10377246}.
CC -!- TISSUE SPECIFICITY: Highest expression in esophagus. Moderately low
CC expression in lung, liver, heart, Harderian gland, olfactory mucosa,
CC skin and testis. In brain, expression is very high in choroid plexus,
CC high in hind brain and low in hippocampus and cerebellum. In spinal
CC cord expression is strongest in anterior horns. Low expression detected
CC in spleen and eye. AOX1 expression in the livers of mice is
CC approximately seven times greater in males than females.
CC {ECO:0000269|PubMed:10377246, ECO:0000269|PubMed:23263164,
CC ECO:0000269|PubMed:23462233, ECO:0000269|PubMed:9243637}.
CC -!- DEVELOPMENTAL STAGE: Expressed in adult liver but not in neonatal or
CC embryonic liver. Not detected in preadipocytes but strongly induced in
CC mature adipocytes. {ECO:0000269|PubMed:10673024,
CC ECO:0000269|PubMed:18671973}.
CC -!- INDUCTION: Repressed by pioglitazone, fenofibrate and PPARA agonists.
CC Induced by testosterone. {ECO:0000269|PubMed:10377246,
CC ECO:0000269|PubMed:18671973}.
CC -!- MISCELLANEOUS: AOX genes evolved from a xanthine oxidoreductase
CC ancestral precursor via a series of gene duplication and
CC suppression/deletion events. Different animal species contain a
CC different complement of AOX genes encoding an equivalent number of AOX
CC isoenzymes. In mammals, the two extremes are represented by certain
CC rodents such as mice and rats, which are endowed with 4 AOX genes, and
CC by humans, whose genome is characterized by a single active gene
CC (PubMed:23263164). {ECO:0000305|PubMed:23263164}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF076216; AAC99382.1; -; mRNA.
DR EMBL; AB017482; BAA36834.1; -; mRNA.
DR EMBL; AF121945; AAD31763.1; -; Genomic_DNA.
DR EMBL; AF121911; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121912; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121913; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121914; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121915; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121916; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121917; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121918; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121919; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121920; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121921; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121922; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121923; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121924; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121925; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121926; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121927; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121928; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121929; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121930; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121931; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121932; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121933; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121934; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121935; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121936; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121937; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121938; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121939; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121940; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121941; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121942; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121943; AAD31763.1; JOINED; Genomic_DNA.
DR EMBL; AF121944; AAD31763.1; JOINED; Genomic_DNA.
DR CCDS; CCDS35575.1; -.
DR RefSeq; NP_033806.2; NM_009676.2.
DR AlphaFoldDB; O54754; -.
DR SMR; O54754; -.
DR STRING; 10090.ENSMUSP00000001027; -.
DR BindingDB; O54754; -.
DR ChEMBL; CHEMBL1641354; -.
DR iPTMnet; O54754; -.
DR PhosphoSitePlus; O54754; -.
DR jPOST; O54754; -.
DR MaxQB; O54754; -.
DR PaxDb; O54754; -.
DR PRIDE; O54754; -.
DR ProteomicsDB; 282129; -.
DR DNASU; 11761; -.
DR GeneID; 11761; -.
DR KEGG; mmu:11761; -.
DR CTD; 316; -.
DR MGI; MGI:88035; Aox1.
DR eggNOG; KOG0430; Eukaryota.
DR InParanoid; O54754; -.
DR OrthoDB; 48717at2759; -.
DR PhylomeDB; O54754; -.
DR BRENDA; 1.2.3.1; 3474.
DR Reactome; R-MMU-964975; Vitamins B6 activation to pyridoxal phosphate.
DR BioGRID-ORCS; 11761; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Aox1; mouse.
DR PRO; PR:O54754; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O54754; protein.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0004031; F:aldehyde oxidase activity; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IDA:MGI.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0043546; F:molybdopterin cofactor binding; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR014313; Aldehyde_oxidase.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR PIRSF; PIRSF000127; Xanthine_DH; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR TIGRFAMs; TIGR02969; mam_aldehyde_ox; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur; Lipid metabolism;
KW Metal-binding; Molybdenum; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1333
FT /note="Aldehyde oxidase 1"
FT /id="PRO_0000166106"
FT DOMAIN 4..91
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 235..420
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1265
FT /note="Proton acceptor; for azaheterocycle hydroxylase
FT activity"
FT /evidence="ECO:0000305|PubMed:19401776"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 73
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 112
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 113
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 116
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 148
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 150
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 150
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 263..270
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 344
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 353
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 357
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 366
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 410
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 801..802
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1042
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1083..1086
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1198
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1263
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT MOD_RES 1063
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT VARIANT 109
FT /note="H -> Q (in strain: 129/Sv)"
FT VARIANT 168
FT /note="A -> G (in strain: C57BL/6 X CBA and 129/Sv)"
FT VARIANT 449
FT /note="R -> T (in strain: C57BL/6 X CBA)"
FT VARIANT 492
FT /note="R -> A (in strain: C57BL/6 X CBA, requires 2
FT nucleotide substitutions)"
FT VARIANT 686..687
FT /note="KQ -> NE (in strain: 129/Sv)"
FT VARIANT 857
FT /note="E -> D (in strain: 129/Sv)"
FT VARIANT 983
FT /note="E -> D (in strain: C57BL/6 X CBA)"
FT VARIANT 1169
FT /note="N -> D (in strain: C57BL/6 X CBA and 129/Sv)"
FT VARIANT 1329
FT /note="C -> W (in strain: C57BL/6 X CBA and 129/Sv)"
FT MUTAGEN 806
FT /note="V->E: Decreases substrate affinity and activity on
FT benzaldehyde, phthalazine and acetaldehyde, while increases
FT affinity for more hydrophobic aldehydes like retinal.
FT Abolishes catalytic activity; when associated with R-884."
FT /evidence="ECO:0000269|PubMed:19401776"
FT MUTAGEN 884
FT /note="M->R: Abolishes catalytic activity on phthalazine
FT and acetaldehyde. Decreases catalytic efficiency on
FT benzaldehyde and retinal. Abolishes catalytic activity;
FT when associated with E-806."
FT /evidence="ECO:0000269|PubMed:19401776"
FT MUTAGEN 1265
FT /note="E->Q: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19401776"
SQ SEQUENCE 1333 AA; 146678 MW; 320CF0A3742F6AC5 CRC64;
MDPIQLLFYV NGQKVVEKNV DPEMMLLPYL RKNLRLTGTK YGCGGGGCGA CTVMISRYNP
STKAIRHHPV NACLTPICSL HGTAVTTVEG LGNTRTRLHP IQERIAKCHG TQCGFCTPGM
VMSMYALLRN HPEPTLDQLT DALGGNLCRC TGYRPIIDAC KTFCKASACC QSKENGVCCL
DQEINGLAES QEEDKTSPEL FSEEEFLPLD PTQELIFPPE LMRIAEKQPP KTRVFYGERV
TWISPVTLKE LVEAKFKYPQ APIVMGYTSV GPEVKFKGVF HPIIISPDRI EELGVISQAR
DGLTLGAGLS LDQVKDILAD IVQKLPEEKT QTYRALLKHL RTLAGSQIRN MASLGGHIVS
RHLDSDLNPL LAVGNCTLNL LSKDGERRIP LSEEFLRKCP EADLKPQEVL VSVNIPWSRK
WEFVSAFRQA QRQQNALAIV NSGMRVLFRE GGGVIEELSI LYGGVGSTII SAKNSCQRLI
GRPWNEGMLD TRCRLVLDEV TLAASAPGGK VEFKRTLIIS FLFKFYLEVS QGLKREDPGH
SPSLAGNHES ALDDLHSKHP WRTLTHQNVD PAQLPQDPIG RPIMHLSGIK HATGEAIYCD
DMPAVDRELF LTFVTSSRAH AKIVSIDLSE ALSLPGVVDI ITADHLQEAN TFGTETFLAT
DEVHCVGHLV CAVIADSETR AKQAAKQVKV VYQDLAPLIL TIEEAIQHKS FFKSERKLEC
GNVDEAFKIV DQILEGEIHI GGQEHFYMET QSMLVVPKGE DGEIDIYVST QFPKYIQDIV
AATLKLSANK VMCHVRRVGG AFGGKVGKTS ILAAITAFAA SKHGRAVRCI LERGEDMLIT
GGRHPYLGKY KAGFMNEGRI LALDVEHYCN GGCSLDESLW VIEMGLLKLD NAYKFPNLRC
RGWACRTNLP SNTALRGFGF PQAGLVTEAC ITEVAIKCGL SPEQVRTINM YKHVDTTHYK
QEFSAKALSE CWRECMAKCS YFERKAAIGK FNAENSWKKR GMAVIPLKFP VGIGSVAMGQ
AAALVHIYLD GSALVSHGGI EMGQGVHTKM IQVVSRELRM PMSSVHLRGT STETVPNTNA
SGGSVVADLN GLAVKDACQT LLKRLEPIIS KNPQGTWKDW AQTAFDQSIS LSAVGYFRGY
ESNIDWEKGE GHPFEYFVFG AACSEVEINC LTGDHKNIRT NIVMDVGHSI NPALDIGQVE
GAFIQGMGLY TIEELSYSPQ GTLYSRGPNQ YKIPAICDIP TEMHISFLPP SEHSNTLYSS
KGLGESGVFL GCSVFFAIHD AVKAARQERG ISGPWKLNSP LTPEKIRMAC EDKFTKMIPR
DEPGSYVPCN IPV
