ID W4LJA8_9BACT Unreviewed; 363 AA.
AC W4LJA8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:ETW98067.1};
GN ORFNames=ETSY2_43375 {ECO:0000313|EMBL:ETW98067.1};
OS Candidatus Entotheonella gemina.
OC Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia;
OC Entotheonella.
OX NCBI_TaxID=1429439 {ECO:0000313|EMBL:ETW98067.1, ECO:0000313|Proteomes:UP000019140};
RN [1] {ECO:0000313|EMBL:ETW98067.1, ECO:0000313|Proteomes:UP000019140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSY2 {ECO:0000313|Proteomes:UP000019140};
RX PubMed=24476823; DOI=10.1038/nature12959;
RA Wilson M.C., Mori T., Ruckert C., Uria A.R., Helf M.J., Takada K.,
RA Gernert C., Steffens U.A., Heycke N., Schmitt S., Rinke C., Helfrich E.J.,
RA Brachmann A.O., Gurgui C., Wakimoto T., Kracht M., Crusemann M.,
RA Hentschel U., Abe I., Matsunaga S., Kalinowski J., Takeyama H., Piel J.;
RT "An environmental bacterial taxon with a large and distinct metabolic
RT repertoire.";
RL Nature 506:58-62(2014).
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:ETW98067.1}.
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DR EMBL; AZHX01001983; ETW98067.1; -; Genomic_DNA.
DR AlphaFoldDB; W4LJA8; -.
DR PATRIC; fig|1429439.4.peg.7254; -.
DR HOGENOM; CLU_026673_14_1_7; -.
DR Proteomes; UP000019140; 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; cd08279; Zn_ADH_class_III; 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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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:UP000019140};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..360
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 363 AA; 38671 MW; 164011632ABE67E0 CRC64;
MQAAVFRRAH EPVTIESVDI DQPAGREVLV RTAASGVCHS DLHYVDGSVS YTGSTPIVLG
HEGAGVVEAV GDEVTTVRPG DHVIACLSGF CGTCQQCLTG HPNLCVNRII KRETSAPPRL
SQSGKPVMPF ADIGSYAEQM LCHENSLVQI DSDIPLDHAA LMGCGALTGL GAALRTSGLE
AGQSVAVFGC GGVGLSIIQG ARIGGARQII AVDMYNSKLG MAEAVGATHV VNTSEEEAVA
AIRDLTRGEG VDHAFEAVGL PTLVRQAVES LAIRGTATIV GVLPTGSMIE FPWEALRPEC
RVQTSRMGSN RFRVDIPRYL ELYRQGRLKL DEMVTRRRTL HDINDAFRAM KAGEVARSVL
LFE
//
