ID A0A1F8PAV6_9CHLR Unreviewed; 360 AA.
AC A0A1F8PAV6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 28-JUN-2023, entry version 17.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=A2Z15_09420 {ECO:0000313|EMBL:OGO20284.1};
OS Chloroflexi bacterium RBG_16_50_11.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797642 {ECO:0000313|EMBL:OGO20284.1, ECO:0000313|Proteomes:UP000179337};
RN [1] {ECO:0000313|EMBL:OGO20284.1, ECO:0000313|Proteomes:UP000179337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO20284.1}.
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DR EMBL; MGNJ01000024; OGO20284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8PAV6; -.
DR Proteomes; UP000179337; 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 Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 13..357
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 360 AA; 38483 MW; 94715D5B7E507412 CRC64;
MKAAVCYEFN KPVVIEDVTL AEPGKGDVKI RLAATAICHS DIHDWKGEMP GPTPFVGGHE
SAGHIDKLGA GVTSVKVGDP VVVSLLASCG QCYYCITGLP SLCENRFTPP KEPRVRNKKG
QPLQLKGNVG GFADYVVVNE SQVVKVPKEM PLDRAALLAC GVITGFGGVV NRAMVRPFQS
IVVMGAGGVG INAIQGAAYV GAYPIIAVDV LDSKMKMAMD FGATHMVNAR NEKAAEEIRK
LTGGRGAEFV FVTVGSIAAI KQGMSFTGQR GTTVLIGLPN FRDQLSFSPL EMIPSEKNLI
GGFMGATNLK IDIPNLIMLY QTGRLKLDEL ITGRFPLDRI NEAMALTEKG EGLRNVIMFE
//