ID A0A398B8S6_9BACI Unreviewed; 339 AA.
AC A0A398B8S6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Zinc-binding alcohol dehydrogenase family protein {ECO:0000313|EMBL:RID84310.1};
GN ORFNames=D1953_13955 {ECO:0000313|EMBL:RID84310.1};
OS Peribacillus asahii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=228899 {ECO:0000313|EMBL:RID84310.1, ECO:0000313|Proteomes:UP000266016};
RN [1] {ECO:0000313|EMBL:RID84310.1, ECO:0000313|Proteomes:UP000266016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MA001 {ECO:0000313|EMBL:RID84310.1,
RC ECO:0000313|Proteomes:UP000266016};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus jemisoniae sp. nov., Bacillus chryseoplanitiae sp. nov., Bacillus
RT resnikiae sp. nov., and Bacillus frankliniae sp. nov., isolated from Viking
RT spacecraft and associated surfaces.";
RL Submitted (AUG-2018) 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|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:RID84310.1}.
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DR EMBL; QWVS01000026; RID84310.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A398B8S6; -.
DR Proteomes; UP000266016; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd08261; Zn_ADH7; 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; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000266016};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 9..338
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 339 AA; 37248 MW; E4D438F1A89C7F47 CRC64;
MKAVQVRKAH ELVIQEVEQP KISNSTDVLV KVKRVGICGS DMHIYHGTNP LATLPRVVGH
EVAGEVVEIG QDVTGVQVGD HVVVEPINYC GECYACRKGR QNVCEKLSVF GVHEDGGMRE
WFVLPEKQLH VVDPTLAWEE IVLAEPYTIG AQAIWRGEVE QGDTVLIQGA GPIGICILKM
AKLQGASVMI TDLSEERLAF AKENGADVTV HAGNEDVRQR VQEWTNGEGA NVVIDAVCLP
MTFELSFDVV SVAGRIVVLG FDERTSAIAQ LPITKKEVTV VGSRLQTNQF SKVVKLLNEG
QLRHNGLVTH TFSLDDVQEA FNFVEKHPEQ VRKAIIVFN
//
