ID A3ANH3_ORYSJ Unreviewed; 1282 AA. AC A3ANH3; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 30-AUG-2017, entry version 69. 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; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947 {ECO:0000313|EMBL:EAZ28862.1}; RN [1] {ECO:0000313|EMBL:EAZ28862.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., RA Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., RA Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., RA Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., RA Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., RA Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., RA Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., RA Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., RA Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., RA 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). RN [2] {ECO:0000313|EMBL:EAZ28862.1} RP NUCLEOTIDE SEQUENCE. RA Wang J., Li R., Fan W., Huang Q., Zhang J., Zhou Y., Hu Y., Zi S., RA Li J., Ni P., Zheng H., Zhang Y., Zhao M., Hao Q., McDermott J., RA Samudrala R., Kristiansen K., Wong G.K.-S.; RT "Improved gene annotation of the rice (Oryza sativa) genomes."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|PIRSR:PIRSR000127-2}; CC -!- COFACTOR: CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; CC Evidence={ECO:0000256|PIRSR:PIRSR000127-3}; CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. CC {ECO:0000256|PIRSR:PIRSR000127-3}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000256|PIRSR:PIRSR000127-3}; CC Note=Binds 2 [2Fe-2S] clusters. {ECO:0000256|PIRSR:PIRSR000127-3}; 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 PaxDb; A3ANH3; -. DR eggNOG; KOG0430; Eukaryota. DR eggNOG; COG4630; LUCA. DR eggNOG; COG4631; LUCA. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR Gene3D; 1.10.150.120; -; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.30.365.10; -; 5. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.90.1170.50; -; 1. DR InterPro; IPR002888; 2Fe-2S-bd. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b. DR InterPro; IPR016208; Ald_Oxase/xanthine_DH. DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR005107; CO_DH_flav_C. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. 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 4: Predicted; KW 2Fe-2S {ECO:0000256|PIRSR:PIRSR000127-3}; KW FAD {ECO:0000256|PIRSR:PIRSR000127-2}; KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000127-2}; KW Iron {ECO:0000256|PIRSR:PIRSR000127-3}; KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR000127-3}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000127-3}; KW Molybdenum {ECO:0000256|PIRSR:PIRSR000127-3}. FT DOMAIN 10 97 2Fe-2S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51085}. FT DOMAIN 245 437 FAD-binding PCMH-type. FT {ECO:0000259|PROSITE:PS51387}. FT ACT_SITE 1217 1217 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR000127-1}. FT METAL 49 49 Iron-sulfur 1. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 54 54 Iron-sulfur 1. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 57 57 Iron-sulfur 1. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 79 79 Iron-sulfur 1. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 119 119 Iron-sulfur 2. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 122 122 Iron-sulfur 2. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 167 167 Iron-sulfur 2. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 169 169 Iron-sulfur 2. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 801 801 Molybdenum. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 832 832 Molybdenum; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000127-3}. FT METAL 1045 1045 Molybdenum; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR000127-3}. FT BINDING 373 373 FAD. {ECO:0000256|PIRSR:PIRSR000127-2}. FT BINDING 413 413 FAD; via amide nitrogen and carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR000127- FT 2}. FT BINDING 433 433 FAD. {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 //