ALDO1_MAIZE
ID ALDO1_MAIZE Reviewed; 1358 AA.
AC O23887; C0P5A6;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Indole-3-acetaldehyde oxidase;
DE Short=IAA oxidase;
DE EC=1.2.3.7;
DE AltName: Full=Aldehyde oxidase;
DE Short=ZmAO-1;
GN Name=AO1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 235-272; 591-611 AND
RP 1234-1249, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Golden Cross Bantam 70; TISSUE=Coleoptile;
RX PubMed=9182554; DOI=10.1074/jbc.272.24.15280;
RA Sekimoto H., Seo M., Dohmae N., Takio K., Kamiya Y., Koshiba T.;
RT "Cloning and molecular characterization of plant aldehyde oxidase.";
RL J. Biol. Chem. 272:15280-15285(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 533-1358.
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Golden Cross Bantam 70;
RX PubMed=12226218; DOI=10.1104/pp.110.3.781;
RA Koshiba T., Saito E., Ono N., Yamamoto N., Sato M.;
RT "Purification and properties of flavin- and molybdenum-containing aldehyde
RT oxidase from coleoptiles of maize.";
RL Plant Physiol. 110:781-789(1996).
CC -!- FUNCTION: In higher plants aldehyde oxidases (AO) appear to be
CC homo- and heterodimeric assemblies of AO subunits with probably
CC different physiological functions. Involved in the biosynthesis of
CC auxin from (indol-3-yl)acetaldehyde. Can also use indole-3-aldehyde and
CC benzaldehyde as substrate. {ECO:0000269|PubMed:12226218}.
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:12226218};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:12226218};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000305|PubMed:12226218};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000305|PubMed:12226218};
CC -!- ACTIVITY REGULATION: Inhibited by 2-mercaptoethanol, p-
CC chloromercuribenzoate, and iodoacetate. {ECO:0000269|PubMed:12226218}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 uM for (indol-3-yl)acetaldehyde (at pH 7.4 and 30 degrees
CC Celsius, with O2 as electron acceptor) {ECO:0000269|PubMed:12226218};
CC KM=4.5 uM for indol-3-aldehyde (at pH 7.4 and 30 degrees Celsius,
CC with O2 as electron acceptor) {ECO:0000269|PubMed:12226218};
CC KM=1.5 uM for benzaldehyde (at pH 7.4 and 30 degrees Celsius, with O2
CC as electron acceptor) {ECO:0000269|PubMed:12226218};
CC KM=2.9 uM for protocatechualdehyde (at pH 7.4 and 30 degrees Celsius,
CC with O2 as electron acceptor) {ECO:0000269|PubMed:12226218};
CC KM=5 uM for (indol-3-yl)acetaldehyde (at pH 7.4 and 30 degrees
CC Celsius, with DCIP as electron acceptor)
CC {ECO:0000269|PubMed:12226218};
CC KM=14 uM for indol-3-aldehyde (at pH 7.4 and 30 degrees Celsius, with
CC DCIP as electron acceptor) {ECO:0000269|PubMed:12226218};
CC KM=5 uM for benzaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP
CC as electron acceptor) {ECO:0000269|PubMed:12226218};
CC KM=26 uM for protocatechualdehyde (at pH 7.4 and 30 degrees Celsius,
CC with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218};
CC KM=250 uM for phenylacetaldehyde (at pH 7.4 and 30 degrees Celsius,
CC with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218};
CC KM=26 uM for butyraldehyde (at pH 7.4 and 30 degrees Celsius, with
CC DCIP as electron acceptor) {ECO:0000269|PubMed:12226218};
CC KM=74 uM for propionaldehyde (at pH 7.4 and 30 degrees Celsius, with
CC DCIP as electron acceptor) {ECO:0000269|PubMed:12226218};
CC KM=345 uM for acetaldehyde (at pH 7.4 and 30 degrees Celsius, with
CC DCIP as electron acceptor) {ECO:0000269|PubMed:12226218};
CC Vmax=76 nmol/min/mg enzyme with (indol-3-yl)acetaldehyde as substrate
CC (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)
CC {ECO:0000269|PubMed:12226218};
CC Vmax=69 nmol/min/mg enzyme with indol-3-aldehyde as substrate (at pH
CC 7.4 and 30 degrees Celsius, with O2 as electron acceptor)
CC {ECO:0000269|PubMed:12226218};
CC Vmax=453 nmol/min/mg enzyme with benzaldehyde as substrate (at pH 7.4
CC and 30 degrees Celsius, with O2 as electron acceptor)
CC {ECO:0000269|PubMed:12226218};
CC Vmax=175 nmol/min/mg enzyme with protocatechualdehyde as substrate
CC (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)
CC {ECO:0000269|PubMed:12226218};
CC Vmax=28 nmol/min/mg enzyme with (indol-3-yl)acetaldehyde as substrate
CC (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)
CC {ECO:0000269|PubMed:12226218};
CC Vmax=190 nmol/min/mg enzyme with indol-3-aldehyde as substrate (at pH
CC 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)
CC {ECO:0000269|PubMed:12226218};
CC Vmax=247 nmol/min/mg enzyme with benzaldehyde as substrate (at pH 7.4
CC and 30 degrees Celsius, with DCIP as electron acceptor)
CC {ECO:0000269|PubMed:12226218};
CC Vmax=316 nmol/min/mg enzyme with protocatechualdehyde as substrate
CC (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)
CC {ECO:0000269|PubMed:12226218};
CC Vmax=120 nmol/min/mg enzyme with phenylacetaldehyde as substrate (at
CC pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)
CC {ECO:0000269|PubMed:12226218};
CC Vmax=113 nmol/min/mg enzyme with butyraldehyde as substrate (at pH
CC 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)
CC {ECO:0000269|PubMed:12226218};
CC Vmax=70 nmol/min/mg enzyme with propionaldehyde as substrate (at pH
CC 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)
CC {ECO:0000269|PubMed:12226218};
CC Vmax=57 nmol/min/mg enzyme with acetaldehyde as substrate (at pH 7.4
CC and 30 degrees Celsius, with DCIP as electron acceptor)
CC {ECO:0000269|PubMed:12226218};
CC pH dependence:
CC Optimum pH is 7-8. {ECO:0000269|PubMed:12226218};
CC -!- SUBUNIT: Aldehyde oxidases (AO) are homodimers and heterodimers of AO
CC subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, and, to a lower extent,
CC in mesocotyl, leaves and coleoptile. Accumulates in apical region of
CC maize coleoptiles (at protein level). {ECO:0000269|PubMed:9182554}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACN28172.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D88451; BAA23226.1; -; mRNA.
DR EMBL; BT063475; ACN28172.1; ALT_INIT; mRNA.
DR PIR; T01698; T01698.
DR RefSeq; NP_001105308.1; NM_001111838.1.
DR AlphaFoldDB; O23887; -.
DR SMR; O23887; -.
DR STRING; 4577.GRMZM2G141535_P01; -.
DR PaxDb; O23887; -.
DR PRIDE; O23887; -.
DR GeneID; 542228; -.
DR KEGG; zma:542228; -.
DR MaizeGDB; 275805; -.
DR eggNOG; KOG0430; Eukaryota.
DR OrthoDB; 48717at2759; -.
DR BRENDA; 1.2.3.1; 6752.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; O23887; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0050302; F:indole-3-acetaldehyde oxidase activity; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IDA:UniProtKB.
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; IDA:UniProtKB.
DR Gene3D; 3.10.20.30; -; 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; 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;
KW Direct protein sequencing; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Metal-binding; Molybdenum; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..1358
FT /note="Indole-3-acetaldehyde oxidase"
FT /id="PRO_0000418842"
FT DOMAIN 11..98
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 241..419
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 532..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 55
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 58
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT CONFLICT 1116
FT /note="T -> A (in Ref. 2; ACN28172)"
FT /evidence="ECO:0000305"
FT CONFLICT 1127..1129
FT /note="KLN -> RLK (in Ref. 2; ACN28172)"
FT /evidence="ECO:0000305"
FT CONFLICT 1162
FT /note="P -> A (in Ref. 2; ACN28172)"
FT /evidence="ECO:0000305"
FT CONFLICT 1289
FT /note="T -> A (in Ref. 2; ACN28172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1358 AA; 146683 MW; 82449227AFB14861 CRC64;
MGKEAGAAES STVVLAVNGK RYEAAGVAPS TSLLEFLRTQ TPVRGPKLGC GEGGCGACVV
LVSKYDPATD EVTEFSASSC LTLLHSVDRC SVTTSEGIGN TRDGYHPVQQ RLSGFHASQC
GFCTPGMCMS IFSALVKADN KSDRPDPPAG FSKITTSEAE KAVSGNLCRC TGYRPIVDTC
KSFASDVDLE DLGLNCFWKK GEEPAEVSRL PGYNSGAVCT FPEFLKSEIK STMKQVNDVP
IAASGDGWYH PKSIEELHRL FDSSWFDDSS VKIVASNTGS GVYKDQDLYD KYIDIKGIPE
LSVINKNDKA IELGSVVSIS KAIEVLSDGN LVFRKIADHL NKVASPFVRN TATIGGNIMM
AQRLPFESDV ATVLLAAGST VTVQVASKRL CFTLEEFLEQ PPCDSRTLLL SIFIPEWGSD
YVTFETFRAA PRPFGNAVSY VNSAFLARTS GSLLIEDICL AFGAYGVDHA IRAKKVEDFL
KGKSLSSFVI LEAIKLLKDT VSPSEGTTHH EYRVSLAVSF LFSFLSSLAN SSSAPSNIDT
PNGSYTHETG SNVDSPERHI KVDSNDLPIR SRQEMVFSDE YKPVGKPIKK VGAEIQASGE
AVYVDDIPAP KDCLYGAFIY STHPHAHVRS INFKSSLASQ KVITVITAKD IPSGGENIGS
SFLMQGEALF ADPIAEFAGQ NIGVVIAETQ RYANMAAKQA VVEYSTENLQ PPILTIEDAI
QRNSYIQIPP FLAPKPVGDY NKGMAEADHK ILSAEVKLES QYYFYMETQA ALAIPDEDNC
ITIYSSTQMP ELTQNLIARC LGIPFHNVRV ISRRVGGGFG GKAMKATHTA CACALAAFKL
RRPVRMYLDR KTDMIMAGGR HPMKAKYSVG FKSDGKITAL HLDLGINAGI SPDVSPLMPR
AIIGALKKYN WGTLEFDTKV CKTNVSSKSA MRAPGDVQGS FIAEAIIEHV ASALALDTNT
VRRKNLHDFE SLEVFYGESA GEASTYSLVS MFDKLALSPE YQHRAAMIEQ FNSSNKWKKR
GISCVPATYE VNLRPTPGKV SIMNDGSIAV EVGGIEIGQG LWTKVKQMTA FGLGQLCPDG
GECLLDKVRV IQADTLSLIQ GGMTAGSTTS ETSCETVRQS CVALVEKLNP IKESLEAKSN
TVEWSALIAQ ASMASVNLSA QPYWTPDPSF KSYLNYGAGT SEVEVDILTG ATTILRSDLV
YDCGQSLNPA VDLGQIEGCF VQGIGFFTNE DYKTNSDGLV IHDGTWTYKI PTVDNIPKEF
NVEMFNSAPD KKRVLSSKAS GEPPLVLATS VHCAMREAIR AARKEFSVST SPAKSAVTFQ
MDVPATMPVV KELCGLDVVE RYLENVSAAS AGPNTAKA
