ID A0A3D1BZB6_9ENTR Unreviewed; 346 AA. AC A0A3D1BZB6; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 14-DEC-2022, entry version 12. DE SubName: Full=Galactitol-1-phosphate 5-dehydrogenase {ECO:0000313|EMBL:HCC74151.1}; GN ORFNames=DEQ42_00190 {ECO:0000313|EMBL:HCC74151.1}; OS Shigella sp. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=625 {ECO:0000313|EMBL:HCC74151.1, ECO:0000313|Proteomes:UP000263458}; RN [1] {ECO:0000313|EMBL:HCC74151.1, ECO:0000313|Proteomes:UP000263458} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA10497 {ECO:0000313|EMBL:HCC74151.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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 -!- 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:HCC74151.1}. 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; DOZY01000003; HCC74151.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3D1BZB6; -. DR Proteomes; UP000263458; Unassembled WGS sequence. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt. 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 Zinc {ECO:0000256|RuleBase:RU361277}. FT DOMAIN 6..344 FT /note="Enoyl reductase (ER)" FT /evidence="ECO:0000259|SMART:SM00829" SQ SEQUENCE 346 AA; 37478 MW; B207881B4F157332 CRC64; MKSVVNDTDG IVRVAESVIP EIKHQDEVRV KIASSGLCGS DLPRIFKNGA HYYPITLGHE FSGYIDAVGS GVDDLHPDDA VACVPLLPCF TCPECLKGFY SQCAKYDFIG SRRDGGFAEY IVVKRKNVFA LPTDMPIEDG AFIEPITVGL HAFHLAQGCE NKNVIIIGAG TIGLLAIQCA VALGAKSVTA IDISSEKLAL AKSFGAMQTF NSSEMSAPQM QSVLRELRFN QLILETAGVP QTVELAVEIA GPHAQLALVG TLHQDLHLTS ATFGKILRKE LTVIGSWMNY SSPWPGQEWE TASRLLTERK LSLEPLIAHR GSFESFTQAV RDIARNAMPG KVLLIP //