ALDO4_ARATH
ID ALDO4_ARATH Reviewed; 1337 AA.
AC Q7G191; O23027; O49157; Q7GB29;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Aldehyde oxidase 4 {ECO:0000303|PubMed:10972874};
DE Short=AO-4 {ECO:0000303|PubMed:10972874};
DE Short=AtAO-4 {ECO:0000303|PubMed:10972874};
DE Short=AtAO2 {ECO:0000303|PubMed:9655945};
DE EC=1.2.3.1 {ECO:0000269|PubMed:19297586, ECO:0000269|PubMed:28188272};
DE AltName: Full=Benzaldehyde oxidase {ECO:0000305|PubMed:19297586};
DE AltName: Full=Indole-3-acetaldehyde oxidase {ECO:0000305|PubMed:19297586};
DE Short=IAA oxidase {ECO:0000305|PubMed:19297586};
DE EC=1.2.3.7 {ECO:0000269|PubMed:19297586};
GN Name=AAO4 {ECO:0000303|PubMed:10972874};
GN Synonyms=AO2 {ECO:0000303|PubMed:9655945};
GN OrderedLocusNames=At1g04580 {ECO:0000312|Araport:AT1G04580};
GN ORFNames=T1G11.17 {ECO:0000312|EMBL:AAB80640.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RA Seo M., Koshiba T.;
RT "Arabidopsis aldehyde oxidase cDNA.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1082-1337.
RC STRAIN=cv. Wassilewskija; TISSUE=Root;
RX PubMed=9655945; DOI=10.1016/s0167-4781(98)00085-2;
RA Hoff T., Frandsen G.I., Rocher A., Mundy J.;
RT "Biochemical and genetic characterization of three molybdenum cofactor
RT hydroxylases in Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1398:397-402(1998).
RN [5]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=10972874; DOI=10.1046/j.1365-313x.2000.00812.x;
RA Seo M., Koiwai H., Akaba S., Komano T., Oritani T., Kamiya Y., Koshiba T.;
RT "Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana.";
RL Plant J. 23:481-488(2000).
RN [6]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15574845; DOI=10.1093/pcp/pch198;
RA Seo M., Aoki H., Koiwai H., Kamiya Y., Nambara E., Koshiba T.;
RT "Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene family
RT revealed a major role of AAO3 in ABA biosynthesis in seeds.";
RL Plant Cell Physiol. 45:1694-1703(2004).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=19297586; DOI=10.1104/pp.109.135848;
RA Ibdah M., Chen Y.-T., Wilkerson C.G., Pichersky E.;
RT "An aldehyde oxidase in developing seeds of Arabidopsis converts
RT benzaldehyde to benzoic Acid.";
RL Plant Physiol. 150:416-423(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY ALDEHYDE; HYDROGEN PEROXIDE
RP AND DEHYDRATION, AND CATALYTIC ACTIVITY.
RX PubMed=28188272; DOI=10.1104/pp.16.01939;
RA Srivastava S., Brychkova G., Yarmolinsky D., Soltabayeva A., Samani T.,
RA Sagi M.;
RT "Aldehyde oxidase 4 plays a critical role in delaying silique senescence by
RT catalyzing aldehyde detoxification.";
RL Plant Physiol. 173:1977-1997(2017).
CC -!- FUNCTION: Aldehyde oxidase with a broad substrate specificity
CC (PubMed:28188272). Involved in the accumulation of benzoic acid (BA) in
CC siliques (PubMed:19297586). Delays and protects siliques from
CC senescence by catalyzing aldehyde detoxification in siliques. Catalyzes
CC the oxidation of an array of aromatic and aliphatic aldehydes,
CC including vanillin and the reactive carbonyl species (RCS) acrolein, 4-
CC hydroxyl-2-nonenal (HNE), and malondialdehyde (MDA) (PubMed:28188272).
CC {ECO:0000269|PubMed:19297586, ECO:0000269|PubMed:28188272}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + indole-3-acetaldehyde + O2 = (indol-3-yl)acetate + H(+)
CC + H2O2; Xref=Rhea:RHEA:16277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18086,
CC ChEBI:CHEBI:30854; EC=1.2.3.7;
CC Evidence={ECO:0000269|PubMed:19297586};
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:19297586,
CC ECO:0000269|PubMed:28188272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzaldehyde + H2O + O2 = benzoate + H(+) + H2O2;
CC Xref=Rhea:RHEA:58960, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16150, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17169; Evidence={ECO:0000269|PubMed:19297586,
CC ECO:0000269|PubMed:28188272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanal + O2 = H(+) + H2O2 + hexanoate;
CC Xref=Rhea:RHEA:58964, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17120,
CC ChEBI:CHEBI:88528; Evidence={ECO:0000269|PubMed:28188272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-naphthaldehyde + H2O + O2 = 1-naphthoate + H(+) + H2O2;
CC Xref=Rhea:RHEA:58968, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:36298,
CC ChEBI:CHEBI:52367; Evidence={ECO:0000269|PubMed:28188272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + vanillin = H(+) + H2O2 + vanillate;
CC Xref=Rhea:RHEA:58972, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16632,
CC ChEBI:CHEBI:18346; Evidence={ECO:0000269|PubMed:28188272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + malonaldehyde + O2 = 3-oxopropanoate + H(+) + H2O2;
CC Xref=Rhea:RHEA:58976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:566274; Evidence={ECO:0000269|PubMed:28188272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citral + H2O + O2 = 3,7-dimethylocta-2,6-dienoate + H(+) +
CC H2O2; Xref=Rhea:RHEA:58980, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:23316,
CC ChEBI:CHEBI:142930; Evidence={ECO:0000269|PubMed:28188272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acrolein + H2O + O2 = acrylate + H(+) + H2O2;
CC Xref=Rhea:RHEA:58984, ChEBI:CHEBI:15368, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:37080; Evidence={ECO:0000269|PubMed:28188272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-hydroxynon-2-enal + H2O + O2 = (E)-4-hydroxynon-2-enoate
CC + H(+) + H2O2; Xref=Rhea:RHEA:58988, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:58968, ChEBI:CHEBI:142920;
CC Evidence={ECO:0000269|PubMed:28188272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamaldehyde + H2O + O2 = (E)-cinnamate + H(+) + H2O2;
CC Xref=Rhea:RHEA:58992, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15669, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16731; Evidence={ECO:0000269|PubMed:28188272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + indole-3-carbaldehyde + O2 = H(+) + H2O2 + indole-3-
CC carboxylate; Xref=Rhea:RHEA:58996, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:28238, ChEBI:CHEBI:62448;
CC Evidence={ECO:0000269|PubMed:28188272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + propanal = H(+) + H2O2 + propanoate;
CC Xref=Rhea:RHEA:59000, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17153,
CC ChEBI:CHEBI:17272; Evidence={ECO:0000269|PubMed:28188272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanal + H2O + O2 = dodecanoate + H(+) + H2O2;
CC Xref=Rhea:RHEA:59004, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18262,
CC ChEBI:CHEBI:27836; Evidence={ECO:0000269|PubMed:28188272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + salicylaldehyde = H(+) + H2O2 + salicylate;
CC Xref=Rhea:RHEA:59008, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16008, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:30762; Evidence={ECO:0000269|PubMed:28188272};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:P80457};
CC Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250|UniProtKB:P80457};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P80457};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000250|UniProtKB:P80457};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250|UniProtKB:P80457};
CC -!- ACTIVITY REGULATION: Inhibited by Cu(2+).
CC {ECO:0000269|PubMed:19297586}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23 uM for benzoic acid (BA) (at pH7, in the presence of NAD(+))
CC {ECO:0000269|PubMed:19297586};
CC KM=2.07 uM for indole-3-acetaldehyde (at pH7)
CC {ECO:0000269|PubMed:19297586};
CC KM=103.9 uM for cinnamylaldehyde (at pH7)
CC {ECO:0000269|PubMed:19297586};
CC Vmax=1.2 nmol/sec/mg enzyme with benzoic acid (BA) as substrate (at
CC pH7, in the presence of NAD(+)) {ECO:0000269|PubMed:19297586};
CC Vmax=1.5 nmol/sec/mg enzyme with indole-3-acetaldehyde as substrate
CC (at pH7) {ECO:0000269|PubMed:19297586};
CC Vmax=5.5 nmol/sec/mg enzyme with cinnamylaldehyde as substrate (at
CC pH7) {ECO:0000269|PubMed:19297586};
CC Note=kcat is 95.2 sec(-1) with benzoic acid (BA) as substrate, 1.904
CC sec(-1) with indole-3-acetaldehyde as substrate, and 436.5 sec(-1)
CC with cinnamylaldehyde as substrate (at pH 7, PubMed:19297586).;
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:19297586};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:19297586};
CC -!- SUBUNIT: Aldehyde oxidases (AO) are homodimers and heterodimers of AO
CC subunits. {ECO:0000250|UniProtKB:Q7G193}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:19297586}.
CC -!- TISSUE SPECIFICITY: Transcripts expressed at high levels in developing
CC siliques and at low levels in dry seeds. {ECO:0000269|PubMed:10972874,
CC ECO:0000269|PubMed:15574845, ECO:0000269|PubMed:28188272}.
CC -!- INDUCTION: Induced by dehydration, in rosette leaves but not in roots
CC (PubMed:10972874, PubMed:28188272). Induced by hydrogen peroxide
CC H(2)O(2) and aldehyde treatment (PubMed:28188272).
CC {ECO:0000269|PubMed:10972874, ECO:0000269|PubMed:28188272}.
CC -!- DISRUPTION PHENOTYPE: Plants have normal abscisic acid (ABA) levels,
CC normal germination and are not affected in abscisic aldehyde oxidase
CC activity in siliques, dry seeds and leaves. Reduced levels of benzoic
CC acid (BA), 3-benzoyloxypropylglucosinolate and 4-
CC benzoyloxybutylglucosinolate in seeds. Senesced siliques accumulate
CC high endogenous reactive carbonyl species (RCS) levels associated with
CC enhanced senescence molecular markers, have an increased chlorophyll
CC degradation, and exhibit early seed shattering. Severe tissue damage
CC and enhanced malondialdehyde levels and senescence symptoms in siliques
CC treated with several aldehydes. Increased endogenous reactive carbonyl
CC species (RCS) and higher expression levels of senescence marker genes,
CC leading to premature siliques senescence in response to abiotic
CC stresses such as dark and ultraviolet C irradiation (PubMed:28188272).
CC {ECO:0000269|PubMed:15574845, ECO:0000269|PubMed:19297586,
CC ECO:0000269|PubMed:28188272}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB80640.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB037271; BAA90299.1; -; mRNA.
DR EMBL; AC002376; AAB80640.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27717.1; -; Genomic_DNA.
DR EMBL; AF039897; AAC39511.1; -; mRNA.
DR PIR; D86178; D86178.
DR PIR; T52051; T52051.
DR RefSeq; NP_563711.1; NM_100337.3.
DR AlphaFoldDB; Q7G191; -.
DR SMR; Q7G191; -.
DR STRING; 3702.AT1G04580.1; -.
DR iPTMnet; Q7G191; -.
DR PaxDb; Q7G191; -.
DR PRIDE; Q7G191; -.
DR ProteomicsDB; 244968; -.
DR EnsemblPlants; AT1G04580.1; AT1G04580.1; AT1G04580.
DR GeneID; 839488; -.
DR Gramene; AT1G04580.1; AT1G04580.1; AT1G04580.
DR KEGG; ath:AT1G04580; -.
DR Araport; AT1G04580; -.
DR TAIR; locus:2197798; AT1G04580.
DR eggNOG; KOG0430; Eukaryota.
DR HOGENOM; CLU_001681_1_1_1; -.
DR InParanoid; Q7G191; -.
DR OMA; KKLPPYN; -.
DR OrthoDB; 48717at2759; -.
DR PhylomeDB; Q7G191; -.
DR BioCyc; ARA:AT1G04580-MON; -.
DR BioCyc; MetaCyc:AT1G04580-MON; -.
DR BRENDA; 1.2.3.1; 399.
DR PRO; PR:Q7G191; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q7G191; baseline and differential.
DR Genevisible; Q7G191; AT.
DR GO; GO:0005829; C:cytosol; TAS:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004031; F:aldehyde oxidase activity; IMP:UniProtKB.
DR GO; GO:0018488; F:aryl-aldehyde oxidase activity; IDA:TAIR.
DR GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IDA:TAIR.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050302; F:indole-3-acetaldehyde oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0110096; P:cellular response to aldehyde; IEP:UniProtKB.
DR GO; GO:0019760; P:glucosinolate metabolic process; IMP:TAIR.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR CDD; cd00207; fer2; 1.
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; 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 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; Abscisic acid biosynthesis; Auxin biosynthesis; Cytoplasm; FAD;
KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..1337
FT /note="Aldehyde oxidase 4"
FT /id="PRO_0000166112"
FT DOMAIN 4..91
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 225..409
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1265
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80457"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 73
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80457"
FT BINDING 113
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80457"
FT BINDING 116
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80457"
FT BINDING 155
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80457"
FT BINDING 157
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80457"
FT BINDING 259..266
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P80457"
FT BINDING 342..346
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P80457"
FT BINDING 358
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P80457"
FT BINDING 399
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P80457"
FT BINDING 771
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250|UniProtKB:P80457"
FT BINDING 802
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250|UniProtKB:P80457"
FT BINDING 915
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250|UniProtKB:P80457"
FT CONFLICT 1257
FT /note="V -> I (in Ref. 4; AAC39511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1337 AA; 147304 MW; 8DCF487FA3F7D6B8 CRC64;
MAGDDLVFAV NGEKFEVLSV NPSTTLLEFL RSNTCFKSVK LSCGEGGCGA CIVILSKYDP
VLDQVEEYSI NSCLTLLCSL NGCSITTSDG LGNTEKGFHP IHKRFAGFHA SQCGFCTPGM
CISLYSALSK AHNSQSSPDY LTALAAEKSI AGNLCRCTGY RPIADACKSF ASDVDIEDLG
FNSFWRKGES REEMLKKLPP YNPEKDLITF PDFLKEKIKC QHNVLDQTRY HWSTPGSVAE
LQEILATTNP GKDRGLIKLV VGNTGTGYYK EEKQYGRYID ISHIPEMSMI KKDDREIEIG
AVVTISKVID ALMEENTSAY VFKKIGVHME KVANHFIRNS GSIGGNLVMA QSKSFPSDIT
TLLLAADASV HMINAGRHEK LRMGEYLVSP PILDTKTVLL KVHIPRWIAS STTGLLFETY
RAALRPIGSA LPYINAAFLA VVSHDASSSG IIVDKCRLAF GSYGGYHSIR AREVEDFLTG
KILSHSVLYE AVRLLKGIIV PSIDTSYSEY KKSLAVGFLF DFLYPLIESG SWDSEGKHID
GHIDPTICLP LLSSAQQVFE SKEYHPVGEA IIKFGAEMQA SGEAVYVDDI PSLPHCLHGA
FIYSTKPLAW IKSVGFSGNV TPIGVLAVIT FKDIPEVGQN IGYITMFGTG LLFADEVTIS
AGQIIALVVA DTQKHADMAA HLAVVEYDSR NIGTPVLSVE DAVKRSSLFE VPPEYQPEPV
GDISKGMAEA DRKIRSVELR LGSQYFFYME TQTALALPDE DNCLVVYSST QAPEFTQTVI
ATCLGIPEHN VRVITRRVGG GFGGKAIKSM PVATACALAA KKMQRPVRIY VNRKTDMIMA
GGRHPLKITY SVGFRSDGKL TALDLNLFID AGSDVDVSLV MPQNIMNSLR KYDWGALSFD
IKVCKTNLPS RTSLRAPGEV QGSYIAESII ENVASSLKMD VDVVRRINLH TYESLRKFYK
QAAGEPDEYT LPLLWDKLEV SADFRRRAES VKEFNRCNIW RKRGISRVPI IHLVIHRPTP
GKVSILNDGS VAVEVAGIEV GQGLWTKVQQ MVAYGLGMIK CEGSDDLLER IRLLQTDTLS
MSQSSYTAGS TTSENCCEAV RLCCGILVER LRPTMNQILE NARSVTWDML IQQANAQSVD
LSARTFYKPE SSSAEYLNYG VGASEVEVDL VTGRTEIIRS DIIYDCGKSL NPAVDLGQIE
GAFVQGIGFF MYEEYTTNEN GLVNEEGTWD YKIPTIDTIP KQFNVQILNS GHHKNRVLSS
KASGEPPLLV AASVHCATRS AIREARKQYL SWNCIDDDHR ERCDLGFELP VPATMPVVKQ
LCGLESIEKY LEWKTYP
