ID A3ANH3_ORYSJ Unreviewed; 1282 AA. AC A3ANH3; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 02-OCT-2024, entry version 100. 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}; 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., 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). 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., Li J., RA Ni P., Zheng H., Zhang Y., Zhao M., Hao Q., McDermott J., Samudrala R., RA Kristiansen K., Wong G.K.-S.; RT "Improved gene annotation of the rice (Oryza sativa) genomes."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC 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:190135; CC Evidence={ECO:0000256|ARBA:ARBA00034078}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000256|PIRSR:PIRSR000127-3}; CC Note=Binds 2 [2Fe-2S] clusters. {ECO:0000256|PIRSR:PIRSR000127-3}; 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:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1. DR Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1. DR Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 3. DR Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 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-like. DR InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1. DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2. 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:SF92; ALDEHYDE OXIDASE 1-RELATED; 1. DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1. DR Pfam; PF01315; Ald_Xan_dh_C; 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 Pfam; PF02738; MoCoBD_1; 1. DR Pfam; PF20256; MoCoBD_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; SSF54292; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1. DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1. DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1. DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1. DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 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}; NAD {ECO:0000256|ARBA:ARBA00023027}; KW 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 BINDING 49 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 54 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 57 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 79 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 119 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 122 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 167 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 169 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 373 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2" FT BINDING 413 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2" FT BINDING 433 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2" FT BINDING 801 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT /ligand_part="Mo" FT /ligand_part_id="ChEBI:CHEBI:28685" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 832 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT /ligand_part="Mo" FT /ligand_part_id="ChEBI:CHEBI:28685" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 1045 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT /ligand_part="Mo" FT /ligand_part_id="ChEBI:CHEBI:28685" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" 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 //