ID O93734_9EURY Unreviewed; 330 AA. AC O93734; DT 01-MAY-1999, integrated into UniProtKB/TrEMBL. DT 01-MAY-1999, sequence version 1. DT 24-JAN-2024, entry version 83. DE SubName: Full=F420-dependent alcohol dehydrogenase {ECO:0000313|EMBL:CAA77275.1}; DE Flags: Fragment; GN Name=adf {ECO:0000313|EMBL:CAA77275.1}; OS Methanoculleus thermophilus. OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus. OX NCBI_TaxID=2200 {ECO:0000313|EMBL:CAA77275.1}; RN [1] {ECO:0000313|EMBL:CAA77275.1} RP NUCLEOTIDE SEQUENCE. RA Shimada M., Horigome T.; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:1RHC} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND ACTIVE SITE. RX PubMed=15016352; DOI=10.1016/j.str.2004.02.010; RA Aufhammer S.W., Warkentin E., Berk H., Shima S., Thauer R.K., Ermler U.; RT "Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a RT member of the bacterial luciferase family."; RL Structure 12:361-370(2004). 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; Y18729; CAA77275.1; -; Genomic_DNA. DR PDB; 1RHC; X-ray; 1.80 A; A=1-330. DR PDBsum; 1RHC; -. DR AlphaFoldDB; O93734; -. DR SMR; O93734; -. DR KEGG; ag:CAA77275; -. DR BRENDA; 1.1.98.5; 3272. DR EvolutionaryTrace; O93734; -. DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro. DR CDD; cd01097; Tetrahydromethanopterin_reductase; 1. DR Gene3D; 3.20.20.30; Luciferase-like domain; 1. DR InterPro; IPR019945; F420_G6P_DH-rel. DR InterPro; IPR011251; Luciferase-like_dom. DR InterPro; IPR036661; Luciferase-like_sf. DR NCBIfam; TIGR03557; F420_G6P_family; 1. DR PANTHER; PTHR43244; -; 1. DR PANTHER; PTHR43244:SF1; 5,10-METHYLENETETRAHYDROMETHANOPTERIN REDUCTASE; 1. DR Pfam; PF00296; Bac_luciferase; 1. DR SUPFAM; SSF51679; Bacterial luciferase-like; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1RHC}. FT DOMAIN 14..304 FT /note="Luciferase-like" FT /evidence="ECO:0000259|Pfam:PF00296" FT ACT_SITE 39 FT /note="EMO_00068 proton donor,EMO_00066 proton acceptor" FT /evidence="ECO:0007829|PDB:1RHC" FT ACT_SITE 108 FT /note="EMO_00033 electrostatic stabiliser,EMO_00066 proton FT acceptor,EMO_00068 proton donor" FT /evidence="ECO:0007829|PDB:1RHC" FT SITE 43 FT /note="EMO_00033 electrostatic stabiliser" FT /evidence="ECO:0007829|PDB:1RHC" FT NON_TER 330 FT /evidence="ECO:0000313|EMBL:CAA77275.1" SQ SEQUENCE 330 AA; 37158 MW; CD1528E3B0AF11EB CRC64; MKTQIGYFAS LEQYRPMDAL EQAIRAEKVG FDSVWVDDHF HPWYHDNAQS AQAWAWMGAA LQATKKVFIS TCITCPIMRY NPAIVAQTFA TLRQMYPGRV GVAVGAGEAM NEVPVTGEWP SVPVRQDMTV EAVKVMRMLW ESDKPVTFKG DYFTLDKAFL YTKPDDEVPL YFSGMGPKGA KLAGMYGDHL MTVAAAPSTL KNVTIPKFEE GAREAGKDPS KMEHAMLIWY SVDPDYDKAV EALRFWAGCL VPSMFKYKVY DPKEVQLHAN LVHCDTIKEN YMCATDAEEM IKEIERFKEA GINHFCLGNS SPDVNFGIDI FKEVIPAVRD //