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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
 
 
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