ID A0A3P0X982_9BACT Unreviewed; 333 AA.
AC A0A3P0X982;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=NAD(P)-dependent alcohol dehydrogenase {ECO:0000313|EMBL:RRA49070.1};
GN ORFNames=D1Y84_13080 {ECO:0000313|EMBL:RRA49070.1};
OS Acidipila sp. EB88.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidipila.
OX NCBI_TaxID=2305226 {ECO:0000313|EMBL:RRA49070.1, ECO:0000313|Proteomes:UP000279598};
RN [1] {ECO:0000313|EMBL:RRA49070.1, ECO:0000313|Proteomes:UP000279598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB88 {ECO:0000313|EMBL:RRA49070.1,
RC ECO:0000313|Proteomes:UP000279598};
RA Pold G., Deangelis K.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RRA49070.1, ECO:0000313|Proteomes:UP000279598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB88 {ECO:0000313|EMBL:RRA49070.1,
RC ECO:0000313|Proteomes:UP000279598};
RA Horta L.;
RT "Genome sequence of EB88, a novel member of the group I Acidobacteria.";
RL Submitted (DEC-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|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:RRA49070.1}.
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DR EMBL; QWEV01000005; RRA49070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P0X982; -.
DR OrthoDB; 9806940at2; -.
DR Proteomes; UP000279598; Unassembled WGS sequence.
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; IPR029752; D-isomer_DH_CS1.
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:SF38; ALDEHYDE REDUCTASE AHR; 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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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:UP000279598};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 12..331
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 333 AA; 35560 MW; 527AFB92D07A2E49 CRC64;
MIQGFAVHAA GAELHTFKYD PGALRPSDVE ITISHCGVCH SDVSLIDNEW GFSKYPFIPG
HEVVGTVAAV GENVKHLKAG DQVGVGWQAD SCGYCEWCRR GEENLCAQAT PTCVGRHGGF
AERIRVDARF AILIPEGMDA AATAPLLCGG ITVYSPMRLH NVNASSRVGI IGIGGLGHMA
LQFARACGAD VTAFSSSADK EKEALDLGAH HFVNTRETKS LKALGSKFDF ILSTINVDQD
WSAYVTALRP HGSLVFVGIP PKPATFPVFP LISGVKSISG CNIGSPMQIA EMLDVASRHN
IRAVVENFAM RDANAAVERA RKSAVRYRAV LAN
//
