AOXC_MOUSE
ID AOXC_MOUSE Reviewed; 1335 AA.
AC G3X982; B2RSI5; Q8VI15;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Aldehyde oxidase 3;
DE EC=1.2.3.1 {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336};
DE AltName: Full=Aldehyde oxidase homolog 1;
DE AltName: Full=Azaheterocycle hydroxylase 3;
DE EC=1.17.3.-;
GN Name=Aox3; Synonyms=Aoh1;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 206-224; 247-256;
RP 351-362; 807-823 AND 1291-1308, IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION AS OXIDASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=11562361; DOI=10.1074/jbc.m105744200;
RA Terao M., Kurosaki M., Marini M., Vanoni M.A., Saltini G., Bonetto V.,
RA Bastone A., Federico C., Saccone S., Fanelli R., Salmona M., Garattini E.;
RT "Purification of the aldehyde oxidase homolog 1 (AOH1) protein and cloning
RT of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. Identification of
RT a novel molybdo-flavoprotein gene cluster on mouse chromosome 1.";
RL J. Biol. Chem. 276:46347-46363(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=CD-1; TISSUE=Olfactory epithelium;
RX PubMed=15383531; DOI=10.1074/jbc.m408734200;
RA Kurosaki M., Terao M., Barzago M.M., Bastone A., Bernardinello D.,
RA Salmona M., Garattini E.;
RT "The aldehyde oxidase gene cluster in mice and rats. Aldehyde oxidase
RT homologue 3, a novel member of the molybdo-flavoenzyme family with
RT selective expression in the olfactory mucosa.";
RL J. Biol. Chem. 279:50482-50498(2004).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY TESTOSTERONE.
RX PubMed=18981221; DOI=10.1128/mcb.01385-08;
RA Terao M., Kurosaki M., Barzago M.M., Fratelli M., Bagnati R., Bastone A.,
RA Giudice C., Scanziani E., Mancuso A., Tiveron C., Garattini E.;
RT "Role of the molybdoflavoenzyme aldehyde oxidase homolog 2 in the
RT biosynthesis of retinoic acid: generation and characterization of a
RT knockout mouse.";
RL Mol. Cell. Biol. 29:357-377(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC 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 CRYSTALLIZATION, FUNCTION AS OXIDASE, SUBSTRATE SPECIFICITY, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND HOMODIMER.
RX PubMed=21705476; DOI=10.1124/dmd.111.040873;
RA Mahro M., Coelho C., Trincao J., Rodrigues D., Terao M., Garattini E.,
RA Saggu M., Lendzian F., Hildebrandt P., Romao M.J., Leimkuhler S.;
RT "Characterization and crystallization of mouse aldehyde oxidase 3: from
RT mouse liver to Escherichia coli heterologous protein expression.";
RL Drug Metab. Dispos. 39:1939-1945(2011).
RN [9]
RP 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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) IN COMPLEX WITH FE-S CLUSTERS; FAD
RP AND MO-MPT, FUNCTION AS OXIDASE, SUBSTRATE SPECIFICITY, COFACTOR, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, HOMODIMER, ACTIVITY REGULATION,
RP REACTION MECHANISM, ACTIVE SITE, AND MUTAGENESIS OF ALA-807; TYR-885;
RP LYS-889 AND GLU-1266.
RX PubMed=23019336; DOI=10.1074/jbc.m112.390419;
RA Coelho C., Mahro M., Trincao J., Carvalho A.T., Ramos M.J., Terao M.,
RA Garattini E., Leimkuhler S., Romao M.J.;
RT "The first mammalian aldehyde oxidase crystal structure: insights into
RT substrate specificity.";
RL J. Biol. Chem. 287:40690-40702(2012).
CC -!- FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic
CC azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well
CC as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key
CC role in the metabolism of xenobiotics and drugs containing aromatic
CC azaheterocyclic substituents. Is probably involved in the regulation of
CC reactive oxygen species homeostasis. May be a prominent source of
CC superoxide generation via the one-electron reduction of molecular
CC oxygen. May also catalyze nitric oxide (NO) production via the
CC reduction of nitrite to NO with NADH or aldehyde as electron donor.
CC {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:18981221,
CC ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}.
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:11562361,
CC ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:11562361};
CC Note=Binds 2 [2Fe-2S] clusters per subunit.
CC {ECO:0000269|PubMed:11562361};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11562361};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11562361};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000269|PubMed:11562361};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000269|PubMed:11562361};
CC -!- ACTIVITY REGULATION: Inhibited by potassium cyanide, menadione,
CC benzamidine, raloxifene and norharmane. {ECO:0000269|PubMed:11562361,
CC ECO:0000269|PubMed:23019336}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 uM for phthalazine {ECO:0000269|PubMed:11562361,
CC ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336};
CC KM=1.4 uM for phthalazine (at 37 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476,
CC ECO:0000269|PubMed:23019336};
CC KM=2.5 uM for benzaldehyde (at 37 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476,
CC ECO:0000269|PubMed:23019336};
CC KM=128.5 uM for N1-methylnicotinamide (at 37 degrees Celsius and pH
CC 8) {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476,
CC ECO:0000269|PubMed:23019336};
CC KM=32.3 uM for phenanthridine (at 37 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476,
CC ECO:0000269|PubMed:23019336};
CC KM=13 uM for benzaldehyde (at 37 degrees Celsius and pH 7.4)
CC {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476,
CC ECO:0000269|PubMed:23019336};
CC KM=29 uM for butyraldehyde (at 37 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476,
CC ECO:0000269|PubMed:23019336};
CC KM=173 uM for 2-OH-pyrimidine (at 37 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476,
CC ECO:0000269|PubMed:23019336};
CC Note=kcat is 4 sec(-1) for phthalazine oxidation (PubMed:11562361).
CC kcat is 130 min(-1) for benzaldehyde oxidation, 384 min(-1) for
CC butyraldehyde oxidation and 1279 min(-1) for 2-OH-pyrimidine
CC oxidation (PubMed:21705476). kcat is 41.1 min(-1) for phthalazine
CC oxidation, 41.9 min(-1) for benzaldehyde oxidation, 14.7 min(-1) for
CC N1-methylnicotinamide oxidation and 51.7 min(-1) for phenanthridine
CC oxidation (PubMed:23019336). {ECO:0000269|PubMed:11562361,
CC ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23019336}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11562361,
CC ECO:0000269|PubMed:15383531}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver (at protein level). In
CC liver, the expression is greater in males than females.
CC {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:15383531,
CC ECO:0000269|PubMed:18981221}.
CC -!- INDUCTION: Induced by testosterone. {ECO:0000269|PubMed:18981221}.
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; AF322178; AAL36596.1; -; Genomic_DNA.
DR EMBL; AF322144; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322145; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322146; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322147; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322148; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322149; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322150; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322151; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322152; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322153; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322154; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322155; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322156; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322157; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322158; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322159; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322160; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322161; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322162; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322163; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322164; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322165; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322166; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322167; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322168; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322169; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322170; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322171; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322172; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322173; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322174; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322175; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322176; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AF322177; AAL36596.1; JOINED; Genomic_DNA.
DR EMBL; AC025116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466548; EDL00068.1; -; Genomic_DNA.
DR EMBL; BC138876; AAI38877.1; -; mRNA.
DR CCDS; CCDS14969.1; -.
DR RefSeq; NP_076106.2; NM_023617.2.
DR PDB; 3ZYV; X-ray; 2.54 A; A/B/C/D=1-1335.
DR PDBsum; 3ZYV; -.
DR AlphaFoldDB; G3X982; -.
DR SMR; G3X982; -.
DR BioGRID; 214883; 1.
DR STRING; 10090.ENSMUSP00000049391; -.
DR iPTMnet; G3X982; -.
DR PhosphoSitePlus; G3X982; -.
DR SwissPalm; G3X982; -.
DR jPOST; G3X982; -.
DR MaxQB; G3X982; -.
DR PaxDb; G3X982; -.
DR PeptideAtlas; G3X982; -.
DR PRIDE; G3X982; -.
DR ProteomicsDB; 282130; -.
DR DNASU; 71724; -.
DR Ensembl; ENSMUST00000040999; ENSMUSP00000049391; ENSMUSG00000064294.
DR GeneID; 71724; -.
DR KEGG; mmu:71724; -.
DR UCSC; uc007bbm.1; mouse.
DR CTD; 71724; -.
DR MGI; MGI:1918974; Aox3.
DR VEuPathDB; HostDB:ENSMUSG00000064294; -.
DR eggNOG; KOG0430; Eukaryota.
DR GeneTree; ENSGT00950000183114; -.
DR HOGENOM; CLU_001681_1_2_1; -.
DR InParanoid; G3X982; -.
DR OMA; MRMAEDP; -.
DR OrthoDB; 48717at2759; -.
DR PhylomeDB; G3X982; -.
DR TreeFam; TF353036; -.
DR BRENDA; 1.2.3.1; 3474.
DR BioGRID-ORCS; 71724; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Aox3; mouse.
DR PRO; PR:G3X982; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; G3X982; protein.
DR Bgee; ENSMUSG00000064294; Expressed in left lobe of liver and 68 other tissues.
DR ExpressionAtlas; G3X982; baseline and differential.
DR Genevisible; G3X982; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0004031; F:aldehyde oxidase activity; IDA:MGI.
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:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0030151; F:molybdenum ion binding; IDA:MGI.
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; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS: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 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.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Cytoplasm; Direct protein sequencing; FAD;
KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1335
FT /note="Aldehyde oxidase 3"
FT /id="PRO_0000425247"
FT DOMAIN 8..95
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 236..421
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1266
FT /note="Proton acceptor; for azaheterocycle hydroxylase
FT activity"
FT /evidence="ECO:0000305|PubMed:23019336"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 52
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 55
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 77
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 116
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 117
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 120
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 152
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 154
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 264..271
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 354
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 358
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 367
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 411
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 802
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 1043
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:23019336"
FT BINDING 1199
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:23019336"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QE80"
FT MUTAGEN 807
FT /note="A->V: No effect on kinetic constants with smaller
FT substrates like benzaldehyde or phthalazine. Decreases
FT substrate affinity and slightly increases catalytic
FT efficiency for bulkier substrates like phenanthridine."
FT /evidence="ECO:0000269|PubMed:23019336"
FT MUTAGEN 885
FT /note="Y->M: Slightly decreases substrate affinity but no
FT effect on activity with smaller substrates like
FT benzaldehyde or phthalazine. Increases catalytic efficiency
FT with bulkier substrates like phenanthridine or more charged
FT substrates like N1-methylnicotinamide."
FT /evidence="ECO:0000269|PubMed:23019336"
FT MUTAGEN 889
FT /note="K->H: No effect on substrate affinity but decreases
FT catalytic efficiency for smaller substrates like
FT benzaldehyde or phthalazine. Increases substrate affinity
FT and activity for bulkier substrates like phenanthridine."
FT /evidence="ECO:0000269|PubMed:23019336"
FT MUTAGEN 1266
FT /note="E->Q: Loss of activity with different N-heterocyclic
FT compounds as substrates. 60% reduction of activity with
FT benzaldehyde."
FT /evidence="ECO:0000269|PubMed:23019336"
FT CONFLICT 308
FT /note="A -> T (in Ref. 1; AAL36596)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="K -> R (in Ref. 4; AAI38877)"
FT /evidence="ECO:0000305"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:3ZYV"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:3ZYV"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 121..134
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 312..323
FT /evidence="ECO:0007829|PDB:3ZYV"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 334..341
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 347..352
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 355..360
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:3ZYV"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 410..417
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 423..430
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 440..448
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 457..469
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 490..503
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 512..537
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 547..550
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 551..553
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 589..593
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 610..616
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 618..628
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 630..634
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 638..642
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 644..646
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 662..664
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 670..678
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 679..686
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 690..695
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 703..708
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 713..722
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 724..727
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 730..741
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 753..758
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 765..769
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 774..785
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 789..791
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 792..797
FT /evidence="ECO:0007829|PDB:3ZYV"
FT TURN 803..806
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 809..824
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 828..831
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 834..840
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 847..855
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 861..871
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 879..889
FT /evidence="ECO:0007829|PDB:3ZYV"
FT TURN 890..893
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 897..906
FT /evidence="ECO:0007829|PDB:3ZYV"
FT TURN 917..920
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 921..939
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 943..950
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 969..979
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 982..995
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 997..1011
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 1017..1020
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 1022..1028
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 1034..1036
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 1043..1045
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 1047..1059
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 1063..1065
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 1066..1068
FT /evidence="ECO:0007829|PDB:3ZYV"
FT TURN 1073..1075
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 1087..1105
FT /evidence="ECO:0007829|PDB:3ZYV"
FT TURN 1106..1108
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 1109..1112
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 1118..1127
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 1133..1138
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 1144..1146
FT /evidence="ECO:0007829|PDB:3ZYV"
FT TURN 1147..1150
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 1151..1153
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 1158..1169
FT /evidence="ECO:0007829|PDB:3ZYV"
FT TURN 1171..1173
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 1176..1185
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 1193..1212
FT /evidence="ECO:0007829|PDB:3ZYV"
FT TURN 1229..1231
FT /evidence="ECO:0007829|PDB:3ZYV"
FT TURN 1237..1239
FT /evidence="ECO:0007829|PDB:3ZYV"
FT STRAND 1242..1248
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 1258..1260
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 1267..1272
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 1273..1289
FT /evidence="ECO:0007829|PDB:3ZYV"
FT HELIX 1304..1310
FT /evidence="ECO:0007829|PDB:3ZYV"
FT TURN 1314..1316
FT /evidence="ECO:0007829|PDB:3ZYV"
SQ SEQUENCE 1335 AA; 146902 MW; 29683B03DD3E75E9 CRC64;
MSPSKESDEL IFFVNGKKVT ERNADPEVNL LFYLRKVIRL TGTKYGCGGG DCGACTVMIS
RYDPISKRIS HFSATACLVP ICSLHGAAVT TVEGIGSTKT RIHPVQERIA KGHGTQCGFC
TPGMVMSIYT LLRNHPEPST EQIMETLGGN LCRCTGYRPI VESAKSFCPS STCCQMNGEG
KCCLDEEKNE PERKNSVCTK LYEKKEFQPL DPTQELIFPP ELMRMAEESQ NTVLTFRGER
TTWIAPGTLN DLLELKMKHP SAPLVIGNTY LGLHMKFTDV SYPIIISPAR ILELFVVTNT
KQGLTLGAGL SLTQVKNVLS DVVSRLPKEK TQIYCALLKQ LKTLAGQQIR NVASLGGHII
SRLPTSDLNP ILGIGNCILN VASTEGIQQI PLNDHFLAGV PDAILKPEQV LISVFVPRSS
KWEFVSAFRQ APRQQNAFAT VNAGMKVVFK EDTNTITDLG ILYGGIGATV ISADKSCRQL
IGRCWDEEML DDAGKMICEE VSLLMAAPGG MEEYRKTLAI SFLFMFYLDV LKQLKTRDPH
KYPDISQKLL HILEDFPLTM PYGMQSFQDV DFQQPLQDPI GRPIMHQSGI KHATGEAVFC
DDMSVLPGEL FLAVVTSSKS HAKIISLDAS EALASLGVVD VVTARDVPGD NGREEESLYA
QDEVICVGQI VCAVAADSYA HAQQAAKKVK IVYQDIEPMI VTVQDALQYE SFIGPERKLE
QGNVEEAFQC ADQILEGEVH LGGQEHFYME TQSVRVVPKG EDKEMDIYVS SQDAAFTQEM
VARTLGIPKN RINCHVKRVG GAFGGKASKP GLLASVAAVA AQKTGRPIRF ILERRDDMLI
TGGRHPLLGK YKIGFMNNGK IKAADIQLYI NGGCTPDDSE LVIEYALLKL ENAYKIPNLR
VRGRVCKTNL PSNTAFRGFG FPQGAFVTET CMSAVAAKCR LPPEKVRELN MYRTIDRTIH
NQEFDPTNLL QCWEACVENS SYYNRKKAVD EFNQQRFWKK RGIAIIPMKF SVGFPKTFYY
QAAALVQIYT DGSVLVAHGG VELGQGINTK MIQVASRELK IPMSYIHLDE MSTVTVPNTV
TTGASTGADV NGRAVQNACQ ILMKRLEPII KQNPSGTWEE WVKEAFVQSI SLSATGYFRG
YQADMDWEKG EGDIFPYFVF GAACSEVEID CLTGAHKNIR TDIVMDGSFS INPAVDIGQI
EGAFVQGLGL YTLEELKYSP EGVLYTRGPH QYKIASVTDI PEEFHVSLLT PTPNPKAIYS
SKGLGEAGTF LGCSVFFAIA AAVAAAREER GLSPIWAINS PATAEVIRMA CEDQFTNLVP
QTDSKCCKPW SIPVA
