ID A3ANH3_ORYSJ Unreviewed; 1282 AA. AC A3ANH3; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 12-AUG-2020, entry version 84. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAZ28862.1}; GN ORFNames=OsJ_12899 {ECO:0000313|EMBL:EAZ28862.1}; 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 {ECO:0000313|EMBL:EAZ28862.1, ECO:0000313|Proteomes:UP000007752}; RN [1] {ECO:0000313|EMBL:EAZ28862.1, ECO:0000313|Proteomes:UP000007752} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000007752}; 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., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H., RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J., RA Samudrala R., Wang J., Wong G.K., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|PIRSR:PIRSR000127-2}; CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00006849}. 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; CM000140; EAZ28862.1; -; Genomic_DNA. DR Proteomes; UP000007752; Chromosome 3. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 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; 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; IPR002346; Mopterin_DH_FAD-bd. DR Pfam; PF01315; Ald_Xan_dh_C; 1. DR Pfam; PF02738; Ald_Xan_dh_C2; 2. 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; 2. 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 3: Inferred from homology; KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR000127-3}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000127-2}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}; KW Iron {ECO:0000256|PIRSR:PIRSR000127-3}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000127- KW 3}; Metal-binding {ECO:0000256|PIRSR:PIRSR000127-3}; KW Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|PIRSR:PIRSR000127- KW 3}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}. FT DOMAIN 10..97 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51085" FT DOMAIN 245..437 FT /note="FAD-binding PCMH-type" FT /evidence="ECO:0000259|PROSITE:PS51387" FT REGION 552..576 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1217 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-1" FT METAL 49 FT /note="Iron-sulfur 1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 54 FT /note="Iron-sulfur 1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 57 FT /note="Iron-sulfur 1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 79 FT /note="Iron-sulfur 1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 119 FT /note="Iron-sulfur 2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 122 FT /note="Iron-sulfur 2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 167 FT /note="Iron-sulfur 2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 169 FT /note="Iron-sulfur 2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 801 FT /note="Molybdenum" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 832 FT /note="Molybdenum; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 1045 FT /note="Molybdenum; via amide nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 373 FT /note="FAD" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2" FT BINDING 413 FT /note="FAD; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2" FT BINDING 433 FT /note="FAD" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2" SQ SEQUENCE 1282 AA; 137528 MW; D27E8901C2E2BEAA CRC64; MGSEAAAAAR AVVVAVNGER YEAVGVDPST TLLEFLRTRT PVRGPKLGCG EGGCGACVVV VSKYDAVADE VTEFSASSCL TLLGSLHHCA VTTSEGIGNS RDGFHAVQRR LSGFHASQCG FCTPGMCMSI YSALAKADKA SGRPAPPTGF SKITAAEAEK AVSGNLCRCT GYRPIVDACK SFAADVDLED LGLNAFWKKG VDDEHADINK LPAYSGGAAV CTFPEFLKSE IRSSMGQANG DTSAVVVTGD GWFHPKSVEE FHRLFDSNLF DERSVKIVAS NTGSGVYKDQ DLHDKYINIS QIPELSAINR SSKGVEIGAV VSISQAIDIL SDGGAVFRKI ADHLSKVASP FVRNTATIGG NIIMAQRLSF SSDIATVLLA AGSTVTIQVA AKRMCITLEE FLKQPPCDSR TLLVSISIPD WGSDDGITFQ TFRAAPRPLG NAVSYVNSAF LARSSVDGSS GSHLIEDVCL AFGPFGAKHA IRAREVEKFL KGKLVSAPVI LEAVRLLKGV VSPAEGTTHP EYRVSLAVSY LFKFLSSLTN GLDEPENANV PNGSFTNGTA NGIVDSSPEK HSNVDSSYLP IKSRQEMVFS DEYRPIGKPI EKTGAELQAS GEAVYVDDIS APKDCLYGAF IYSTHPHAHI KGVNFRSSLA SQKVITVITL KDIPTNGKNI GSCSPMLGDE ALFVDPVSEF AGQNIGVVIA ETQKYAYMAA KQSVIEYSTE NLQPPILTVE DAVQHNSYFQ VPPFLAPTPI GEFNQAMSEA DHKIIDGEVK LESQYYFYME TQTALAIPDE DNCITLYVSA QLPEITQNTV ARCLGIPYHN VRIITRRVGG GFGGKAMKAI HVATACAVAA FKLRRPVRMY LDRKTDMIMA GGRHPMKGSF IAEAIVEHIA STLSVDTNAI RRKNLHDFES LKVFYGNSAG DPSTYSLVTI FDKLASSPEY QQRAAVVEHF NAGSRWKKRG ISCVPITYDV RLRPSPGKVS IMNDGSIAVE VGGVEIGQGL WTKVKQMTAF ALGQLCDDGG EGLLDKVRVI QADTLSMIQG GFTGGSTTSE TSCEAVRKSS AALVERLKPI KEKAGTLPWK SLIAQASMAS VKLTEHAYWT PDPTFTSYLN YGAAISEVEV DVLTGETTIL RSDLVYDCGQ SLNPAVDLGQ VEGAFVQGIG FFTNEEYTTN SDGLVINDGT WTYKIPTVDT IPKQFNVELI NSARDHKRVL SSKASGEPPL LLASSVHCAM REAIRAARKE FAGAGGSSLT FQMDVPATMP IVKELCGLDV VERDLESFAA KA //