ID A0A251SR47_HELAN Unreviewed; 1346 AA. AC A0A251SR47; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 28-MAR-2018, entry version 5. DE SubName: Full=Putative beta-grasp domain-containing protein {ECO:0000313|EMBL:OTG01317.1}; GN ORFNames=HannXRQ_Chr13g0400761 {ECO:0000313|EMBL:OTG01317.1}; OS Helianthus annuus (Common sunflower). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; campanulids; Asterales; Asteraceae; OC Asteroideae; Heliantheae alliance; Heliantheae; Helianthus. OX NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG01317.1, ECO:0000313|Proteomes:UP000215914}; RN [1] {ECO:0000313|Proteomes:UP000215914} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914}; RX PubMed=28538728; DOI=10.1038/nature22380; RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L., RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L., RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A., RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., RA Chaidir N., Claudel C., Donnadieu C., Faraut T., Fievet G., RA Helmstetter N., King M., Knapp S.J., Lai Z., Le Paslier M.C., RA Lippi Y., Lorenzon L., Mandel J.R., Marage G., Marchand G., RA Marquand E., Bret-Mestries E., Morien E., Nambeesan S., Nguyen T., RA Pegot-Espagnet P., Pouilly N., Raftis F., Sallet E., Schiex T., RA Thomas J., Vandecasteele C., Vares D., Vear F., Vautrin S., Crespi M., RA Mangin B., Burke J.M., Salse J., Munos S., Vincourt P., RA Rieseberg L.H., Langlade N.B.; RT "The sunflower genome provides insights into oil metabolism, flowering RT and Asterid evolution."; RL Nature 546:148-152(2017). 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; CM007902; OTG01317.1; -; Genomic_DNA. DR Proteomes; UP000215914; Chromosome 13. 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: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 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_2. DR InterPro; IPR036318; FAD-bd_2-like_sf. DR InterPro; IPR002346; Mopterin_DH_FAD-bd. 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 4: Predicted; KW 2Fe-2S {ECO:0000256|PIRSR:PIRSR000127-3}; KW Complete proteome {ECO:0000313|Proteomes:UP000215914}; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000215914}. FT DOMAIN 16 103 2Fe-2S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51085}. FT DOMAIN 236 424 FAD-binding PCMH-type. FT {ECO:0000259|PROSITE:PS51387}. FT NP_BIND 358 362 FAD. {ECO:0000256|PIRSR:PIRSR000127-2}. FT ACT_SITE 1277 1277 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR000127-1}. FT METAL 55 55 Iron-sulfur 1. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 60 60 Iron-sulfur 1. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 63 63 Iron-sulfur 1. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 85 85 Iron-sulfur 1. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 125 125 Iron-sulfur 2. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 128 128 Iron-sulfur 2. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 172 172 Iron-sulfur 2. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 174 174 Iron-sulfur 2. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 783 783 Molybdenum. {ECO:0000256|PIRSR: FT PIRSR000127-3}. FT METAL 814 814 Molybdenum; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000127-3}. FT METAL 927 927 Molybdenum; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR000127-3}. FT METAL 1101 1101 Molybdenum; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR000127-3}. FT BINDING 374 374 FAD. {ECO:0000256|PIRSR:PIRSR000127-2}. FT BINDING 414 414 FAD; via amide nitrogen and carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR000127- FT 2}. FT BINDING 443 443 FAD. {ECO:0000256|PIRSR:PIRSR000127-2}. SQ SEQUENCE 1346 AA; 146928 MW; D5A3105CBF3584E4 CRC64; MEDTQLTSTQ PLKHSQTLVF AVNGERVELT SVDPSTTLLQ FLRSHTRFKS VKLGCGEGGC GACNVLLSKF DTKLKQLEDY TVSSCLTLLC SINGCSITTT EGLGNIKDGF HSIHQRFAGF HASQCGFCTP GMCVSLFSAL VNSEKTCRPE PAFGSSKLTA SEAEKSISGN LCRCTGYRPI ADVCKSFAAD VDMEDLGLNS FWKKDAKLNK LPLYDSKQIT TYPEFLKKES KSTAVLNYQD KTWYSPVSVE ELGSLLESIS AENGMTVKLV AGNTGTGYYQ ETEYYNKYID LRCIPELSEI KKAGSRIEIG ATVSISKLIF ALKEHTKDDP TKEDDVVLKK IASHLEKIAS ESIRNVASVG GNLVMAQRKN FPSDIATVLL AVNSRVTILT GVKKETLTLE EFLEKPALDS RNVLLSVFIP CLRPTKNGYS KNVKSKLLFE TYRASPRPLG NALAYLNAAF SAEVCNVNDG VVINRIQLAF GSFGVKHAIR ASTVEKYLVG KKLSVDLISE AVKLIRVAIS PENGTSDPAY RSSLAASFLF DFLMPIVDPE ISSRLTIDDC ERTTLLSPAK QVIESSHEHY PVGEPVIKSG ATIQASGEAV FVDDIPSPLN CLHGAFIYST KPLARVKSIK LKSEKDVNAV VTFQDIPKGG ANIGAINHFG TDPLFSNELT QCAGQRIAFA VAETQKNADM AAGTATVDYD IEDLEPPILT VEQAVEKSSF FEVPLVLTPS QVGDFSKGMA ESDYQIHSAE IKLPSQYYFY MESQTALAVP DEDNCMVVYS SSQVPELVQR VISRCLNIPE HNVRVITRRV GGGFGGKGSK AMPVAAACAL AAYKLRRPVR TYVNRKTDMI LAGGRHPMKI NYTIGFKSNG KITALHLDVL INAGMSPDVS PVIPWKLVGS LKKYNFGALS FDIKVCKTNH SSKSAMRAPG EVQGSYIAEA VIEHVATHLS LDVGLVREMN FHSYDSLKLY YGNSAGDPLE YTLPTIWDKL MKSSNFDSRV EMVNKFNKNN IWRKKGISRV PILQNVSLRP TPGRVSILQD GSVVVEVGGI ELGQGLWTKV KQMTAYCLSA VKCDGTHGLL EKVRVIQADA LSMVQGGLTA GSTTSEASCE AIRLCCNVLV ERLVSLKEKV KEQMGSVSWE LLIMQANMKS VNLSASSYFV PEFTSRSYIN YGAAVSEVEV NLLTGETKML QTDIIYDCGQ SLNPAVDLGQ VEGAFVQGIG FFMLEEYLTN SDGLVVADST WTYKIPTIDT IPKQLNVHIL NSGHHKDRVL SSKASGEPPL LLAASVHCAT RAAIKEARNQ LDSWKGLNGS DTFFELDVPA TMPVVKTLCG LDNVEVYLQS LFMSRS //