ID A0A0R1UVN2_9LACO Unreviewed; 342 AA.
AC A0A0R1UVN2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN ORFNames=FD50_GL001823 {ECO:0000313|EMBL:KRL97264.1};
OS Liquorilactobacillus satsumensis DSM 16230 = JCM 12392.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423801 {ECO:0000313|EMBL:KRL97264.1, ECO:0000313|Proteomes:UP000051166};
RN [1] {ECO:0000313|EMBL:KRL97264.1, ECO:0000313|Proteomes:UP000051166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16230 {ECO:0000313|EMBL:KRL97264.1,
RC ECO:0000313|Proteomes:UP000051166};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|RuleBase:RU364000}.
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:KRL97264.1}.
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DR EMBL; AZFQ01000053; KRL97264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1UVN2; -.
DR STRING; 1423801.FD50_GL001823; -.
DR PATRIC; fig|1423801.4.peg.1864; -.
DR Proteomes; UP000051166; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08252; AL_MDR; 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; IPR013154; ADH-like_N.
DR InterPro; IPR014182; ADH_Zn_typ-1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR02817; adh_fam_1; 1.
DR PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU364000};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364000};
KW Zinc {ECO:0000256|RuleBase:RU364000}.
FT DOMAIN 17..339
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 342 AA; 37900 MW; AE60110C94298514 CRC64;
MKKTMKVIGF KEHLPLTAAN SLQEFEVPRP QVQEHDLLVE VAAVSVNPVD VGVRRTGHGV
LQKPKVLGWD AVGIVKEIGS AVTLFKPGER VFYAGSFKRP GSNSEYQVVD ERIVGHAPEK
LTDAQAAAVP LTSLTAWEAL FEQLEIAQGP AKERTKTILI INGAGGVGSI ATQLADWAGL
KVIASASRRE TIRWVKQHGA QQTVNHRKNL VTEVRNLGYQ YVDYILGLSD LDGHWAEIAA
LIKPSGRIAA ITENKRPLDL KKLTKKRAKF AWEWMYTKSY YQTPDMLSQH VILEKMAALL
DQGIIKSTVT QELSPFNVAN LKRAHELVES NHMMGKVVIC KQ
//
