ID A0A6I5BCZ9_9ACTN Unreviewed; 807 AA. AC A0A6I5BCZ9; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 14-DEC-2022, entry version 6. DE SubName: Full=Molybdopterin-dependent oxidoreductase {ECO:0000313|EMBL:MYQ53649.1}; GN ORFNames=GTW41_21015 {ECO:0000313|EMBL:MYQ53649.1}; OS Streptomyces sp. SID4941. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=2690283 {ECO:0000313|EMBL:MYQ53649.1, ECO:0000313|Proteomes:UP000450528}; RN [1] {ECO:0000313|EMBL:MYQ53649.1, ECO:0000313|Proteomes:UP000450528} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SID4941 {ECO:0000313|EMBL:MYQ53649.1, RC ECO:0000313|Proteomes:UP000450528}; RX PubMed=30705269; DOI=.1038/s41467-019-08438-0; RA Chevrette M.G., Carlson C.M., Ortega H.E., Thomas C., Ananiev G.E., RA Barns K.J., Book A.J., Cagnazzo J., Carlos C., Flanigan W., Grubbs K.J., RA Horn H.A., Hoffmann F.M., Klassen J.L., Knack J.J., Lewin G.R., RA McDonald B.R., Muller L., Melo W.G.P., Pinto-Tomas A.A., Schmitz A., RA Wendt-Pienkowski E., Wildman S., Zhao M., Zhang F., Bugni T.S., Andes D.R., RA Pupo M.T., Currie C.R.; RT "The antimicrobial potential of Streptomyces from insect microbiomes."; RL Nat. Commun. 10:516-516(2019). CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MYQ53649.1}. 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; WWJA01000221; MYQ53649.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6I5BCZ9; -. DR Proteomes; UP000450528; Unassembled WGS sequence. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 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_MoCoBD1. DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2. DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf. DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1. DR Pfam; PF01315; Ald_Xan_dh_C; 1. DR Pfam; PF02738; MoCoBD_1; 1. DR Pfam; PF20256; MoCoBD_2; 1. DR SMART; SM01008; Ald_Xan_dh_C; 1. DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1. DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1. PE 4: Predicted; FT DOMAIN 44..151 FT /note="Ald_Xan_dh_C" FT /evidence="ECO:0000259|SMART:SM01008" FT REGION 1..37 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..31 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 807 AA; 85775 MW; B6700E99B8949242 CRC64; MSTAPQPRTG SVPAGTPTKI TQGSQTRGGI GESTLRPDGT LKVTGEFAYS SDMWHEDMLW GHTLRSTVAH AEITSIDIGE ALATPGVYAV LTYDDLPAEM KNYGLEIQDT PVLAHGKVRH HGEPVALVAA DHPETARRAA AKIVIEYAEL PLITDEASAT APDAVLVHEG RTDHHIGHVP HPNIVHRQPV VRGDADAAAA RADVIVTGDY VFGMQDQAFL GPESGLAVPS EDGGIELYVA TQWLHSDLRQ IAPVLGLPEE KVRMTLSGVG GAFGGREDLS MQIHACLLAL RTGKPVKMVY NRFESFFGHV HRHPARLHYE HGATRDGKLT HMKCRIVLDG GAYASASPAV VGNASSLAVG PYAVEDVDIE AIALYSNNPP CGAMRGFGAV QACFAYEAQM DKLAAALDMD PVELRQLNAM EQGTLLPTGQ RVDSPAPVAE LLRRVKARPL PPERQWLSAD AEGSSVDVRA LPGGLSNTTH GEGVVRGVGY AVGLKNVGFS EGFDDYSTAW VRMEVINGEP VATVHTAMAE VGQGGVTVHA QIARTELGVS QVTIHPADTQ VGSAGSTSAS RQTYVTGGAV KHSCEAVREK VLEIGRRKLG TYHPAWATAE LLLEDGKVVT DGGEVLASLA EVLEDQAVDV ELEWRHRPTE PFDLRTGQGN GHVQYSFAAH RAVVEVDTEL GLVKVIELAC AQDVGKALNP LSVQGQIQGG TTQGLGVAVM EEIIVDPKTA KVRNPSFTDY LIPTILDTPT IPVDVLELAD DHAPYGLRGI GEAPTLSSTP AVLAAIRNAT GLELDRTPVR PEHIAGT //