ALDOL_ORYSJ
ID ALDOL_ORYSJ Reviewed; 1342 AA.
AC Q6Z351;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Putative aldehyde oxidase-like protein;
GN OrderedLocusNames=Os07g0281700, Os07g0281800, LOC_Os07g18120;
GN ORFNames=P0557D09.31;
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=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 [2]
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).
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AP005260; BAC84232.1; -; Genomic_DNA.
DR EMBL; AP014963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q6Z351; -.
DR SMR; Q6Z351; -.
DR STRING; 39947.Q6Z351; -.
DR PaxDb; Q6Z351; -.
DR PRIDE; Q6Z351; -.
DR InParanoid; Q6Z351; -.
DR PlantReactome; R-OSA-1119374; Abscisic acid biosynthesis.
DR PlantReactome; R-OSA-1119486; IAA biosynthesis I.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; 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; 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; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Reference proteome.
FT CHAIN 1..1342
FT /note="Putative aldehyde oxidase-like protein"
FT /id="PRO_0000247648"
FT DOMAIN 221..408
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1342 AA; 145773 MW; 3F8F7A855B851DAA CRC64;
MSDCNSGGGE RRPNARATDA PPVRAPSGGA FRCRGCGACV ILIAKYNPKT DEVTEFNASS
CLTLLYSIHF CSIITTEGLG NTKDGFHAIQ KRMSGFHASQ CGFCTPGMCM SIFSSLVNAD
KSKKPDPPKG FSKLSVSEAE RSFSGNMCRC TGYRPIVDAC KSFASDVDLE DLGLNIFWKK
GDKHPDPTKL PSYTLGGGIC TFPDFLKSEI KSSIDFNDAS ISSPREGWYC PKNIKQYYKL
VNSGLFSESS VKVVVGNTST GVYKDQDLYD KYIDIAGIPE LSAIVRKDKG IEIGAATSIS
RTIEILNQES ESTSSPNGSV VFRKLAEHMS KVASPFVRNT ASIGGNIILA HKYPFRSDIA
TILLGAAATV NLQVSSKTLH VTLEQFLEQP PLGHNTLLLS IFIPHWASDC KKEHTLVFET
YRAAPRPLGN AVSYVNSAFL GHVSLDKSSG DNILSNLHLA FGAYGTEHAI RARKVEEYLT
GKILSASVVL EAIRLLRETI VPVEGTTHPE YRVSVAVGFL FSFLSPLCKG VIEPGKTLSI
SEDLVHTDNV HNMPLSSRRE TLSGDEYKPV GDPIKKYKVE LQASGEAIYV DDIPAPKNCL
YGEFIYSTQP LANVKSIKFK PSLASKKILT VVSAKDIPTG GRNIGSTFLF GDEEPLFGDP
IAEFAGQALG VVIAETQRYA DMAAKQAVVE YTTDGLKAPI LTVEQAVQNN SYFQVPPERA
PKQVGDFSKG MAEADHKIMS EEVKLASQYY FYMETQTALA IPDEDNTMTV YSSSQFPELA
QNVISKCLGI PFNNVRVITR RAGGGFGGKA VRSLHIATAA ALCAHTLRRP VRMYLNRNTD
MIMVGGRHPM KARYSVGFKS DGKITALHLD LLINAGISAD ASPVIPGTII SGLKKYNWGA
LSFDVKLCKT NNTSKSVMRA PGDTQGSFIA EAIIEHVAAI LSLDANTVRQ KNFHTYDSLV
LFYPDSAGES STYTLHSIFD RLASTSRYLQ RVESIKKFNS TNKWRKRGIS SVPLIFKVEP
RPAPGRVSVL NDGSIVVEVG GVELGQGLWT KVQQMTAFAL GQLWPKGCEG LLDRIRVLQS
DTLNLIQGGL TAGSTTSESS CAATLQACNM LIERLKPVME RLQLQSDTVS WDTLISQASQ
ENINLSASAY WVPEQDSNFY LNYGAGTSEV EVDLLTGAIT IIRSDLIYDC GKSLNPAVDL
GQIEGSFIQG IGFFIYEEHQ TNSDGLVISN STWDYKIPSV DTIPKQFNAE VLNTGYHKHR
VLSSKASGEP AVVLGASVHC AVREAIRAAR IEFAGNNGSG SSLLTFQLDV PAPMTVVKEL
CGLDIVEKYL EDLSNRGAAS GN