ID F4CIU5_PSEUX Unreviewed; 370 AA.
AC F4CIU5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=Alcohol dehydrogenase GroES domain protein {ECO:0000313|EMBL:AEA22924.1};
GN OrderedLocusNames=Psed_0661 {ECO:0000313|EMBL:AEA22924.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA22924.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA22924.1, ECO:0000313|Proteomes:UP000007809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC {ECO:0000313|Proteomes:UP000007809};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; CP002593; AEA22924.1; -; Genomic_DNA.
DR RefSeq; WP_013672865.1; NC_015312.1.
DR AlphaFoldDB; F4CIU5; -.
DR STRING; 675635.Psed_0661; -.
DR KEGG; pdx:Psed_0661; -.
DR eggNOG; COG1062; Bacteria.
DR HOGENOM; CLU_026673_14_1_11; -.
DR OMA; SMAPIGI; -.
DR OrthoDB; 3265141at2; -.
DR Proteomes; UP000007809; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08279; Zn_ADH_class_III; 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; IPR023921; ADH_Zn_actinomycetes.
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 NCBIfam; TIGR03989; Rxyl_3153; 1.
DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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:UP000007809};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 12..366
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 370 AA; 38897 MW; 3917BAD2EAAD33C8 CRC64;
MKTTAAVLHE VGKPLQIEEL DLADPGEHEV RVRWTHTGLC HSDLHVLQGD LGAWLPIVLG
HEGAGIVEEV GPGVTRVAPG DHFVASFLPT CGTCHWCAIG RQNLCDMGAA TMRGHLPSGN
WPLSGKAGRY GAMCMIGAFS THGVIHESSA VKIAPEFPLQ VAALVGCGVP TGWGSAVNSA
NVRPGDTVVI YGIGGIGINA VQGARLAGGR HIIAVDPVQL KRDTAMSLGA THAVATAEEA
KELAKDLSRG VGATSAIITV GNVTSDVVDA AFEAISKDGT VVITALAPFA DRTITLSGTE
AVLWRKTIRG SLFGDCNPTT DIPRLLELYR DGSLKLDELI TRTYTLDQIN EGYEHLLAGE
LVRGVIVHEH
//