ID A0A0R2BVU4_9LACO Unreviewed; 371 AA.
AC A0A0R2BVU4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Aryl-alcohol dehydrogenase {ECO:0000313|EMBL:KRM82901.1};
GN ORFNames=FD21_GL000314 {ECO:0000313|EMBL:KRM82901.1};
OS Liquorilactobacillus vini DSM 20605.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1133569 {ECO:0000313|EMBL:KRM82901.1, ECO:0000313|Proteomes:UP000051576};
RN [1] {ECO:0000313|EMBL:KRM82901.1, ECO:0000313|Proteomes:UP000051576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20605 {ECO:0000313|EMBL:KRM82901.1,
RC ECO:0000313|Proteomes:UP000051576};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, 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:KRM82901.1}.
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DR EMBL; AYYX01000126; KRM82901.1; -; Genomic_DNA.
DR RefSeq; WP_010580031.1; NZ_AYYX01000126.1.
DR AlphaFoldDB; A0A0R2BVU4; -.
DR STRING; 1133569.FD21_GL000314; -.
DR PATRIC; fig|1133569.4.peg.334; -.
DR eggNOG; COG1062; Bacteria.
DR OrthoDB; 9806940at2; -.
DR Proteomes; UP000051576; 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; cd08278; benzyl_alcohol_DH; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF2; PKS_ER DOMAIN-CONTAINING PROTEIN-RELATED; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051576};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 12..362
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 371 AA; 39773 MW; 802FCDAD9473040E CRC64;
MKITAAVVEE KGGPFVLKDD IELAEMGPTD LQVRIVATGI CHSDEAIRKG DASLGYPVIL
GHEGSGIVEK VGSQVSDFSV GDHVVLSFYS DGTCDNCLRG IPTQCRSYAK CNLSGLRANG
TDHFTENGQH ISDMFNQSSF TTRTVVNQRN AVKVDKDLDL RKLGPLGCGY VTGSGTVFNN
LQPKPGQTIA VFGTGAVGLT AMMAGRISGC VKVIAVDIVD ERLTLAKELG ATQTINSKNE
DPVKKIKELT NGYGVDFTVD TTGVNPVMMQ AVQSLAQGGT AALIATAQNV TMSSWNDLCT
SDRKVVGVNM GDAIPQIDVP RLIEFYKLGM FDFDKTEKFY KFADINQANQ DSVSGKTIKP
VLIVDEDCQP E
//
