ALDO1_ORYSJ
ID ALDO1_ORYSJ Reviewed; 1358 AA.
AC Q7XH05; A3C2D3; Q0IZ18; Q8W2P4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable aldehyde oxidase 1;
DE Short=AO-1;
DE EC=1.2.3.1;
GN OrderedLocusNames=Os10g0138100, LOC_Os10g04860;
GN ORFNames=OsJ_30665 {ECO:0000312|EMBL:EAZ15246.1}, OSJNAa0087H07.7;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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;
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 -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF26047.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC099733; AAL70116.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP52052.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF26047.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014966; BAT09825.1; -; Genomic_DNA.
DR EMBL; CM000147; EAZ15246.1; -; Genomic_DNA.
DR EMBL; AK121557; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015614946.1; XM_015759460.1.
DR AlphaFoldDB; Q7XH05; -.
DR SMR; Q7XH05; -.
DR STRING; 4530.OS10T0138100-01; -.
DR PaxDb; Q7XH05; -.
DR PRIDE; Q7XH05; -.
DR EnsemblPlants; Os10t0138100-01; Os10t0138100-01; Os10g0138100.
DR GeneID; 4348072; -.
DR Gramene; Os10t0138100-01; Os10t0138100-01; Os10g0138100.
DR KEGG; osa:4348072; -.
DR eggNOG; KOG0430; Eukaryota.
DR HOGENOM; CLU_001681_1_1_1; -.
DR InParanoid; Q7XH05; -.
DR OMA; HWYWPKT; -.
DR OrthoDB; 48717at2759; -.
DR PlantReactome; R-OSA-1119486; IAA biosynthesis I.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR ExpressionAtlas; Q7XH05; baseline and differential.
DR Genevisible; Q7XH05; OS.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004031; F:aldehyde oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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 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; FAD; Flavoprotein;
KW Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..1358
FT /note="Probable aldehyde oxidase 1"
FT /id="PRO_0000247645"
FT DOMAIN 4..91
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 236..418
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 540..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 48
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 73
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT CONFLICT 221
FT /note="F -> L (in Ref. 6; AK121557)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="D -> V (in Ref. 6; AK121557)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="E -> G (in Ref. 6; AK121557)"
FT /evidence="ECO:0000305"
FT CONFLICT 1296
FT /note="H -> R (in Ref. 6; AK121557)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1358 AA; 145453 MW; 75B3A692C75D537D CRC64;
MGEAAAVVAV NGERYEAVGV DPSMTLLEFL RTRTPFRGPK LGCGEGGCGA CAVVVSKYDA
AADEVTSFSA SSCLTLLGSL HHCAVTTSEG IGNSRDGFHP VQRRLAGFHA SQCGFCTPGM
CVSIFSALAN ADRAASAAPP PPPTPPGFSR LTAADAERAV SGNLCRCTGY RPILDACKSF
AADVDLEDLG LNSFWKKGER ADITKLPAYS CTADVATFPE FLKSEIRSSG GAPAVAVTGD
GCWFHPRSIE EFHRLFECNL FDEMSVKIVA SNTGSGVYKD QDLHDKYINI SQIPELSAIN
RSSNGIEIGA AVSISKAIEI LRSDGGDAVV FRKIAYHLGK VASPFVRNTA TIGGNIIMAQ
RMSFPSDIAT VLLAAGSTVT IQQVASKRMC LTLEEFLKQP PCDSRTLLIS ISIPDWCSYD
GITFETFRAA PRPFGNAVSY VNSAFLARSS LDAASGSHLI EDVRLAFGAF GSEHAIRASK
VEEFLKGKLV SASVILEAVR LLKGVVSPAE GTTHPEYRVS LAVSYLFRFL SSLANGLDDK
PENANNVPNG SCTTNGTTNG SAESTVDSFD LPIKSRQEMV FSDEYKPVGK PIKKVGAELQ
ASGEAVYVDD IPAPKDCLYG AFIYSTHPHA HIKGVNFRSS LASQKVITVI TAKDIPTGGE
NVGSCFPMLG DEALFADPVA EFAGQNIGVV IAETQKYAYM AARQAVIEYN TENLQPPILT
VEDAVQHNSY FQVPPFLQPK PIGDFNQAMS EADHKIIDGE VKLGSQYYFY METQTALAFP
DEDNCITVYC SAQMPEVTQD IVARCLGVPF HNVRIITRRV GGGFGGKAMK ATHVATACAV
AAFKLRRPVR MYLDRKTDMI MAGGRHPMKA KYSVGFKSDG KITALHLDLK INAGISPEFS
PAIPYAIVGA LKKYSWGALA FDIKVCKTNV SSKSAMRAPG DAQGSFIAEA IVEHVASTLS
VATNTIRRKN LHDLESLKVF FGDSAAGEAS TSSYSLVIIF DRLASTPEYQ RRAAMVEQFN
GSSRWKKRGI SCVPITYSVT LRPSPGKVSI LNDGSIAVEV GGVEIGQGLW TKVKQMTAFA
LGQLCDDGGE GLLDNVRVIQ ADTLSMIQGG WTAGSTTSET SCEAVRKSCA ALVERLKPIK
EKAGTLPWKS FIAQASMASV KLTEHAYWTP DPTFTSYMNY GAATSEVEVD VLTGATTILR
SDLVYDCGQS LNPAVDLGQV EGAFVQGVGF FTNEEYATNA DGLVIHDGTW TYKIPTVDTI
PKQFNVELIN TARHHSRVLS SKASGEPPLL LASSVHCAMR EAIRAARREF AAVGGGTGGS
DQVTSFQMDV PATMPAVKEL CGLDVVERYL ESFSATTA
