ID E3EE88_PAEPS Unreviewed; 349 AA.
AC E3EE88;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:ADO55011.1};
GN Name=adhC1 {ECO:0000313|EMBL:ADO55011.1};
GN ORFNames=PPSC2_05035 {ECO:0000313|EMBL:ADO55011.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO55011.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO55011.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO55011.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
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}.
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DR EMBL; CP002213; ADO55011.1; -; Genomic_DNA.
DR RefSeq; WP_013369644.1; NC_014622.2.
DR AlphaFoldDB; E3EE88; -.
DR STRING; 1406.LK13_17440; -.
DR KEGG; ppm:PPSC2_05035; -.
DR PATRIC; fig|886882.15.peg.1016; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_2_9; -.
DR OMA; IVDQKFV; -.
DR OrthoDB; 9806940at2; -.
DR Proteomes; UP000006868; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF85; DEATH RESISTOR ADH DOMAIN CONTAINING TARGET, ISOFORM C; 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:UP000006868};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..341
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 349 AA; 37648 MW; D8EB7F91B1099BB2 CRC64;
MITTNARATF SPEGPFKLTT IERRDLQPHD VLIEIKYAGI CHSDIHTARG EWGPVNYPLV
PGHEIAGIVT QVGSEVRKFA IGDRVGVGCM VDSCGECVNC HQGEEQYCLN GNTGTYGAYD
RYGQYTQGGY SSHIVVTEDF VVSIPDGIEL DVAAPLLCAG ITTYSPLRHW GAAPGKKIAV
VGLGGLGHMA VKLAHAMGAE VTVLSQTLNK KEDGLRLGAD HYYATNDPET FKKLAGSFDL
IVNTVSAKID INAYLSLLAL DGTLVNVGAP AEPLPVQVLS LIGHRRSFAG SMIGGIRGTQ
EMLNFCAEHS ITPEIEVISA NQIDEAWERV LASDIRYRFV IDISTMENE
//