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Database: UniProt
Entry: W4B031_9BACL
LinkDB: W4B031_9BACL
Original site: W4B031_9BACL 
ID   W4B031_9BACL            Unreviewed;       379 AA.
AC   W4B031;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Alcohol dehydrogenase GroES domain-containing protein {ECO:0000313|EMBL:ETT36834.1};
GN   ORFNames=C161_10003 {ECO:0000313|EMBL:ETT36834.1};
OS   Paenibacillus sp. FSL R5-192.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1226754 {ECO:0000313|EMBL:ETT36834.1, ECO:0000313|Proteomes:UP000019041};
RN   [1] {ECO:0000313|EMBL:ETT36834.1, ECO:0000313|Proteomes:UP000019041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R5-192 {ECO:0000313|EMBL:ETT36834.1,
RC   ECO:0000313|Proteomes:UP000019041};
RX   PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA   Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA   den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT   "Genomic comparison of sporeforming bacilli isolated from milk.";
RL   BMC Genomics 15:26-26(2014).
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:ETT36834.1}.
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DR   EMBL; ASPR01000014; ETT36834.1; -; Genomic_DNA.
DR   RefSeq; WP_036670053.1; NZ_ASPR01000014.1.
DR   AlphaFoldDB; W4B031; -.
DR   PATRIC; fig|1226754.4.peg.2047; -.
DR   Proteomes; UP000019041; 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; cd08283; FDH_like_1; 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; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..377
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   379 AA;  42033 MW;  B7A4CFBD8C03A34F CRC64;
     MRAVTFQGIK DIQVKEVEDP KLQQKDDIIV RITSTAICGS DLHIYQGALP AAKDYVIGHE
     PMGIVEEVGP EVTRVKKGDR VVLPFNIACG ECFYCNHDME SQCDNSNGNP DIHTGGYFGF
     TERYGNHPGG QAELLRVPYG NFTPFVIPES CELEDEALLF LSDVLPTAYW SVENAGVKPG
     DTVTVLGSGP IGLMTQKFAS MKGAKRVIAV DRLPYRLEKA KRLNDAEIFN FEDYDDMGEH
     IREITQGGTD VVIDCVGMDG KKTTLEEIGQ KLKLHGGSLS AIEIGMKAIR KFGTLQLTGV
     YGSSYNMFPL GNLFERNINL KMGQAPVIHY MPELFRKITA GEFDPTEIIS HRISLENASD
     AYRIFNDHED ECTKVILKP
//
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