ALDO2_ORYSJ
ID ALDO2_ORYSJ Reviewed; 1355 AA.
AC Q852M1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable aldehyde oxidase 2;
DE Short=AO-2;
DE EC=1.2.3.1;
GN OrderedLocusNames=Os03g0790900, LOC_Os03g57690; ORFNames=OSJNBa0087O09.20;
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=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
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=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 [4]
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=AK100342; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC087096; AAO24920.1; -; Genomic_DNA.
DR EMBL; AP014959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK100342; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015630439.1; XM_015774953.1.
DR AlphaFoldDB; Q852M1; -.
DR SMR; Q852M1; -.
DR STRING; 4530.OS03T0790900-01; -.
DR PaxDb; Q852M1; -.
DR GeneID; 4334382; -.
DR KEGG; osa:4334382; -.
DR eggNOG; KOG0430; Eukaryota.
DR InParanoid; Q852M1; -.
DR OrthoDB; 48717at2759; -.
DR PlantReactome; R-OSA-1119374; Abscisic acid biosynthesis.
DR PlantReactome; R-OSA-1119486; IAA biosynthesis I.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q852M1; 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..1355
FT /note="Probable aldehyde oxidase 2"
FT /id="PRO_0000247646"
FT DOMAIN 9..96
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 244..422
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 544..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 53
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 56
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 1355 AA; 145064 MW; ECBDA2871B95BFC7 CRC64;
MGSEAAAARP VVVTVNGERY EAVGVDPSTT LLEFLRTRTP VRGPKLGCGE GGCGACVVVV
SKYDAVADEV TEFSASSCLT LLGSLHHCAV TTSEGIGNSR DGFHAVQRRL SGFHASQCGF
CTPGMCMSIY SALAKADRCS SRPSPPPGFS KLTAAEAEKA VSGNLCRCTG YRPIVDACKS
FAADVDLEDL GLNAFWKKGA DDERADVGKL PAYSGGAAVC TFPEFLKSEI RSSMGQANGG
APAVAVTGDG WFHPKSVEEF HRLFDSNLFD ERSVKIVASN TGSGVYKDQD LHDKYINISQ
ILELSAINRS SKGVEIGAVV SISKAIEILS DGGAVFRKIA DHLSKVASSF VQNTATIGGN
IIMAQRLSFP SDIATVLLAA GSTVTIQVAA KRMCITLEEF LKQPPCDSRT LLVSISIPDW
GSDDGITFES FRAAPRPLGN AVSYVNSAFL ARSSVDGSSG SHLIEDVCLA FGAFGAEHAI
RAREVEEFLK GKLVSAPVIL EAVRLLKGVV SPAEGTTHPE YRVSLAVSYL FRFLTSLANG
LDEPENANVP NGSCTNGTAN GSANSSPEKH SNVDSSDLPI KSRQEMVFSD EYKPVGKPIE
KTGAELQASG EAVYVDDIPA PKDCLYGAFI YSTHPHAHIK DINFRSSLAS QKVITVITAK
DIPTGGENIG SCFPMLGDEA LFVHPVSEFA GQNIGVVIAE TQKYAYMAAK QAVIEYSTEN
LQPPILTIED AVQHNSYFPV PPFLAPTPIG DFNQAMSEAD HKIIDGEVKL ESQYYFYMET
QTALAIPDED NCITLYVSAQ LPEITQNTVA RCLGIPYHNV RIITRRVGGG FGGKAMKAIH
VAAACAVAAF KLRRPVRMYL DRKTDMIMAG GRHPMKVKYS VGFKSDGKIT GLHFDLGMNG
GISPDCSPVL PVAIVGALKK YNWGALSFDI KVCKTNVSSK SAMRAPGDAQ GSFIAEAIVE
HIASTLSVDT NAIRRKNLHD FESLKVFYGN SAGDPSTYSL VTIFDKLASS PEYQQRAAMV
EHFNAGNRWK KRGISCVPIT YDVRLRPTPG KVSIMNDGSI AVEVGGVEIG QGLWTKVKQM
TAFALGQLCD DGGEGLIDKV RVIQADTLSM IQGGFTGGST TSETSCEAVR KSCAALVERL
KPIKEKAGTP PWKSLIAQAS MASVKLTEHA YWTPDPTFTS YLNYGAAISE VEVDVLTGET
TILRSDLVYD CGQSLNPAVD LGQVEGAFVQ GIGFFTNEEY TTNSDGLVIN DGTWTYKIPT
VDTIPKQFNV ELINSARDHK RVLSSKASGE PPLLLASSVH CAMREAIRAA RKEFAGAGGS
PLTFQMDVPA TMPIVKELCG LDVVERYLES FAAKA
