ID A0A251SR47_HELAN Unreviewed; 1346 AA. AC A0A251SR47; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 19-JAN-2022, entry version 16. 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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; OC 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., Chaidir N., RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M., RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R., RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E., RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F., RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F., RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S., RA Vincourt P., Rieseberg L.H., Langlade N.B.; RT "The sunflower genome provides insights into oil metabolism, flowering and RT Asterid evolution."; RL Nature 546:148-152(2017). 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:49601; 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; CM007902; OTG01317.1; -; Genomic_DNA. DR STRING; 4232.A0A251SR47; -. DR EnsemblPlants; OTG01317; OTG01317; HannXRQ_Chr13g0400761. DR Gramene; OTG01317; OTG01317; HannXRQ_Chr13g0400761. DR OMA; HWYWPKT; -. DR OrthoDB; 48717at2759; -. 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:UniProt. 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; IBA:GO_Central. DR GO; GO:0006124; P:ferredoxin metabolic process; IEA:UniProt. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.30.43.10; -; 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; 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; 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; IPR016167; FAD-bd_PCMH_sub1. 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; 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 3: Inferred from homology; KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR000127-3}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000127-2}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000127-3}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000127- KW 3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000215914}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT DOMAIN 16..103 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51085" FT DOMAIN 236..424 FT /note="FAD-binding PCMH-type" FT /evidence="ECO:0000259|PROSITE:PS51387" FT NP_BIND 358..362 FT /note="FAD" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2" FT ACT_SITE 1277 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-1" FT METAL 55 FT /note="Iron-sulfur 1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 60 FT /note="Iron-sulfur 1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 63 FT /note="Iron-sulfur 1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 85 FT /note="Iron-sulfur 1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 125 FT /note="Iron-sulfur 2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 128 FT /note="Iron-sulfur 2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 172 FT /note="Iron-sulfur 2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 174 FT /note="Iron-sulfur 2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 783 FT /note="Molybdenum" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 814 FT /note="Molybdenum; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 927 FT /note="Molybdenum; via amide nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT METAL 1101 FT /note="Molybdenum; via amide nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 374 FT /note="FAD" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2" FT BINDING 414 FT /note="FAD; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2" FT BINDING 443 FT /note="FAD" FT /evidence="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 //