ALDO2_MAIZE
ID ALDO2_MAIZE Reviewed; 1349 AA.
AC O23888;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Indole-3-acetaldehyde oxidase;
DE Short=IAA oxidase;
DE EC=1.2.3.7;
DE AltName: Full=Aldehyde oxidase-2;
DE Short=ZmAO-2;
GN Name=AO2;
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], 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).
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.
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 -!- 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; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250};
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 coleoptiles, and, to a lower
CC extent, in mesocotyl and roots. {ECO:0000269|PubMed:9182554}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D88452; BAA23227.1; -; mRNA.
DR PIR; T01699; T01699.
DR RefSeq; NP_001105309.1; NM_001111839.1.
DR AlphaFoldDB; O23888; -.
DR SMR; O23888; -.
DR STRING; 4577.GRMZM5G899851_P01; -.
DR PaxDb; O23888; -.
DR PRIDE; O23888; -.
DR GeneID; 542229; -.
DR KEGG; zma:542229; -.
DR eggNOG; KOG0430; Eukaryota.
DR OrthoDB; 48717at2759; -.
DR BRENDA; 1.2.3.1; 6752.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; O23888; 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; ISS:UniProtKB.
DR GO; GO:0050302; F:indole-3-acetaldehyde oxidase activity; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; ISS: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; ISS: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 2: Evidence at transcript 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..1349
FT /note="Indole-3-acetaldehyde oxidase"
FT /id="PRO_0000418843"
FT DOMAIN 7..94
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 237..415
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 54
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 1349 AA; 145176 MW; 8C0BCDF57C9165BA CRC64;
MEMGKAAAVV LAVNGKRYEA AGVDPSTTLL EFLRTHTPVR GPKLGCGEGG CGACVVLVSK
YDPATDEVTE FSASSCLTLL HSVDRCSVTT SEGIGNTKDG YHPVQQRLSG FHASQCGFCT
PGMCMSIFSA LVKADKAANR PAPPAGFSKL TSSEAEKAVS GNLCRCTGYR PIVDACKSFA
ADVDLEDLGL NCFWKKGDEP ADVSKLPGYN SGDVCTFPDF LKSEMKSSIQ QANSAPVPVS
DDGWYRPRSI DELHRLFQSS SFDENSVKIV ASNTGSGVYK DQDLYDKYID IKGIPELSVI
NRNDKGIELG SVVSISKAIE VLSDGNLVFR KIAGHLNKVA SPFVRNTATI GGNIVMAQRL
PFASDIATIL LAAGSTVTIQ VASKRLCFTL EEFLQQPPCD SRTLLLSIFI PEWGSNDVTF
ETFRAAPRPL GNAVSYVNSA FLARTSLDAA SKDHLIEDIC LAFGAYGADH AIRARKVEDY
LKGKTVSSSV ILEAVRLLKG SIKPSEGSTH PEYRISLAVS FLFTFLSSLA NSLNESAKVS
GTNEHSPEKQ LKLDINDLPI RSRQEIFFTD AYKPVGKAIK KAGVEIQASG EAVYVDDIPA
PKDCLYGAFI YSTHPHAHVK SINFKPSLAS QKIITVITAK DIPSGGQNVG YSFPMIGEEA
LFADPVAEFA GQNIGVVIAQ TQKYAYMAAK QAIIEYSTEN LQPPILTIED AIERSSFFQT
LPFVAPKPVG DYDKGMSEAD HKILSAEVKI ESQYFFYMEP QVALAIPDED NCITIYFSTQ
LPESTQNVVA KCVGIPFHNV RVITRRVGGG FGGKALKSMH VACACAVAAL KLQRPVRMYL
DRKTDMIMAG GRHPMKVKYS VGFKSNGKIT ALHLDLGING GISPDMSPMI AAPVIGSLKK
YNWGNLAFDT KVCKTNVSSK SSMRAPGDAQ GSFIAEAIIE HVASALSADT NTIRRKNLHD
FESLAVFFGD SAGEASTYSL VTMFDKLASS PEYQHRAEMV EQFNRSNKWK KRGISCVPVT
YEVQLRPTPG KVSIMNDGSI AVEVGGVELG QGLWTKVKQM TAFGLGQLCP GGGESLLDKV
RVIQADTLSM IQGGVTGGST TSETSCEAVR KSCVALVESL KPIKENLEAK TGTVEWSALI
AQASMASVNL SAHAYWTPDP TFTSYLNYGA GTSEVEIDVL TGATTILRSD LVYDCGQSLN
PAVDLGQVEG AFVQGVGFFT NEEYATNSDG LVIHDGTWTY KIPTVDTIPK QFNVELINSA
RDQKRVLSSK ASGEPPLLLA SSVHCAMREA IRAARKEFSV CTGPANSAIT FQMDVPATMP
VVKELCGLDV VERYLESVSA ASPTNTAKA
