ID A0A0G3AHC5_9ACTN Unreviewed; 334 AA. AC A0A0G3AHC5; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 14-DEC-2022, entry version 18. DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:AKJ13411.1}; GN ORFNames=ABB07_26290 {ECO:0000313|EMBL:AKJ13411.1}; OS Streptomyces incarnatus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ13411.1, ECO:0000313|Proteomes:UP000035366}; RN [1] {ECO:0000313|EMBL:AKJ13411.1, ECO:0000313|Proteomes:UP000035366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366}; RX PubMed=26159526; RA Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K., RA Tamura T.; RT "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces RT the Nucleoside Antibiotic Sinefungin."; RL Genome Announc. 3:e00715-e00715(2015). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU361277}; CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {ECO:0000256|RuleBase:RU361277}. 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; CP011497; AKJ13411.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0G3AHC5; -. DR STRING; 665007.ABB07_26290; -. DR EnsemblBacteria; AKJ13411; AKJ13411; ABB07_26290. DR PATRIC; fig|665007.5.peg.5583; -. DR Proteomes; UP000035366; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR InterPro; IPR013149; ADH-like_C. DR InterPro; IPR013154; ADH_N. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020843; PKS_ER. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; GroES-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 3: Inferred from homology; KW Metal-binding {ECO:0000256|RuleBase:RU361277}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000035366}; KW Zinc {ECO:0000256|RuleBase:RU361277}. FT DOMAIN 11..332 FT /note="Enoyl reductase (ER)" FT /evidence="ECO:0000259|SMART:SM00829" SQ SEQUENCE 334 AA; 34575 MW; 27497F633B2E927A CRC64; MSTAVVVEAP GRHRLVAHTP REPGPGEALV AVHAVGICGS DREVYQGNRP EGYVRYPLTP GHEWSGTVSE VGAGVPAGLV GRKVVGEGFR NCQVCDRCHA GETTLCTDGY EETGFTQPGA MAGTLTLPAR LLHVLPDDAD LTAAALLEPA ACVAAAALKA RALPGERVAV VGTGTLGMFA VQFLKAVSPA ELLVVGTGND REALARRFGA TGFRLKDQEL PDDMDVVIET AGSASAARTA AALLRRGGRL VLTGIPAPGA DGLDPTDLVV RQLEVHTVFG APPDAWAHTV RVFGAGLLDP LPLVTHELPL TGFPQAIELV GAGDPKVGKV LLRP //