ID D6IHJ9_ECOLX Unreviewed; 339 AA.
AC D6IHJ9;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=YjgB oxidoreductase {ECO:0000313|EMBL:EFF03480.2};
GN ORFNames=ECDG_02681 {ECO:0000313|EMBL:EFF03480.2};
OS Escherichia coli B185.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=550676 {ECO:0000313|EMBL:EFF03480.2, ECO:0000313|Proteomes:UP000004669};
RN [1] {ECO:0000313|EMBL:EFF03480.2, ECO:0000313|Proteomes:UP000004669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B185 {ECO:0000313|EMBL:EFF03480.2,
RC ECO:0000313|Proteomes:UP000004669};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Escherichia coli B185.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; GG749190; EFF03480.2; -; Genomic_DNA.
DR RefSeq; WP_001300770.1; NZ_GG749190.1.
DR AlphaFoldDB; D6IHJ9; -.
DR Proteomes; UP000004669; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR047109; CAD-like.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF38; ALDEHYDE REDUCTASE AHR; 1.
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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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 13..335
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 339 AA; 36474 MW; 2B62E0E99468AEE0 CRC64;
MSMIKSYAAK EAGGELEVYE YDPGELKPQD VEVQVDYCGI CHSDLSMIDN EWGFSQYPLV
AGHEVIGRVV ALGSAAQDKG LQVGQRVGIG WTARSCGHCD ACISGNQINC EQGAVPTIMN
RGGFAEKLRA DWQWVIPLPE NIDIESAGPL LCGGITVFKP LLMHHITATS RVGVIGIGGL
GHIAIKLLHA MGCEVTAFSS NPAKEQEVLA MGADKVVNSR DPQALKALAG QFDLIINTVN
VSLDWQPYFE ALTYGGNFHT VGAVLTPLSV PAFTLIAGDR SVSGSATGTP YELRKLMRFA
ARSKVAPTTE LFPMSKINDA IQHVRDGKAR YRVVLKADF
//