ID G2ZAG3_LISIP Unreviewed; 329 AA.
AC G2ZAG3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Putative alcohol dehydrogenase {ECO:0000313|EMBL:CBW85187.1};
GN OrderedLocusNames=LIV_0706 {ECO:0000313|EMBL:CBW85187.1};
OS Listeria ivanovii (strain ATCC BAA-678 / PAM 55).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=881621 {ECO:0000313|EMBL:CBW85187.1, ECO:0000313|Proteomes:UP000001286};
RN [1] {ECO:0000313|EMBL:CBW85187.1, ECO:0000313|Proteomes:UP000001286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-678 / PAM 55 {ECO:0000313|Proteomes:UP000001286};
RX PubMed=22072644; DOI=10.1128/JB.06120-11;
RA Buchrieser C., Rusniok C., Garrido P., Hain T., Scortti M., Lampidis R.,
RA Karst U., Chakraborty T., Cossart P., Kreft J., Vazquez-Boland J.A.,
RA Goebel W., Glaser P.;
RT "Complete genome sequence of the animal pathogen Listeria ivanovii, which
RT provides insights into host specificities and evolution of the genus
RT Listeria.";
RL J. Bacteriol. 193:6787-6788(2011).
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DR EMBL; FR687253; CBW85187.1; -; Genomic_DNA.
DR RefSeq; WP_014092207.1; NZ_CVPH01000004.1.
DR AlphaFoldDB; G2ZAG3; -.
DR GeneID; 57075693; -.
DR KEGG; liv:LIV_0706; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_026673_26_3_9; -.
DR OMA; AQMDYNS; -.
DR OrthoDB; 9782155at2; -.
DR Proteomes; UP000001286; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR014188; Acrylyl-CoA_reductase_AcuI.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR02823; oxido_YhdH; 1.
DR PANTHER; PTHR43677:SF1; ACRYLYL-COA REDUCTASE ACUI-RELATED; 1.
DR PANTHER; PTHR43677; SHORT-CHAIN DEHYDROGENASE/REDUCTASE; 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.
PE 4: Predicted;
FT DOMAIN 15..326
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 329 AA; 35432 MW; D8AC5E53731C7C34 CRC64;
MKSFQALFIE KESETTSLQF REISLDTLPE NEVTIEVHYS GINYKDGLAV LPDGKIVSEY
PFVPGIDASG IVVETKTKRF QVGDEVIVTS YDFGVSYFGG YSEYIRVPAE WVVPLPAGLS
LKEAMILGTA GFTAALSVDA LEFSGVTPDA GKIAVSGGTG GVGSLSSAIL SKRNYQVVAS
SSKADAKEFL QKFGVSEVVS REAFQPEKIR ALDKQLFAGA IDCVGGKPLA YLLTAVQYGG
AVTTCGMSAG GKLDTTVFPF ILRGIQLFGI DSVLCPMPKR ERIWRRLATD FQLANLEELA
TEIPFSELPN ALHQVMNGGI TGRYLVKIK
//