ID W0J7C1_9BACT Unreviewed; 358 AA.
AC W0J7C1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:AHF92671.1};
GN ORFNames=OPIT5_23025 {ECO:0000313|EMBL:AHF92671.1};
OS Opitutaceae bacterium TAV5.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=794903 {ECO:0000313|EMBL:AHF92671.1, ECO:0000313|Proteomes:UP000003813};
RN [1] {ECO:0000313|EMBL:AHF92671.1, ECO:0000313|Proteomes:UP000003813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAV5 {ECO:0000313|EMBL:AHF92671.1};
RX PubMed=25744998;
RA Kotak M., Isanapong J., Goodwin L., Bruce D., Chen A., Han C.S.,
RA Huntemann M., Ivanova N., Land M.L., Nolan M., Pati A., Woyke T.,
RA Rodrigues J.L.;
RT "Complete Genome Sequence of the Opitutaceae Bacterium Strain TAV5, a
RT Potential Facultative Methylotroph of the Wood-Feeding Termite
RT Reticulitermes flavipes.";
RL Genome Announc. 3:0-0(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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP007053; AHF92671.1; -; Genomic_DNA.
DR AlphaFoldDB; W0J7C1; -.
DR STRING; 794903.OPIT5_23025; -.
DR KEGG; obt:OPIT5_23025; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_2_0; -.
DR OrthoDB; 9806940at2; -.
DR Proteomes; UP000003813; 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; 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:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-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.
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:UP000003813};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 16..344
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 358 AA; 37871 MW; CA038732F431FBE5 CRC64;
MSKTETCSVK AYSAASATAP LAPDTIRRRE PTERDVQIEI LFCGVCHSDL HFTRNEWSGV
MPAAYPAVPG HEIVGRVTKV GPKVTKVKPG DLAGVGCMVG ADLANCPFCK AGNEQFSPTQ
IGTYGGTEPV IGGPTHGGYS ESIVVDEHFA LHVPANLPLA AVAPLLCAGI TTWSPLRHWK
VGPGKKAGIV GIGGLGHMGV KFARAFGAHV VVFTTSPGKK DDALRLGAHE VVISRNADEM
AKHAGTFDFI LDAVSAEHDI DAYLRLLAPD GNLTLVGAPE KPLAVSAFSL LMGRKSLSGS
PIGSIAETQE MLDFCGEHNI TADVEIIPIQ KINEAWDRLL KGDVKYRFSI DMASLKAG
//
