ID A0A0S8KMN4_9CHLR Unreviewed; 384 AA.
AC A0A0S8KMN4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=AMJ93_05435 {ECO:0000313|EMBL:KPL23137.1};
OS Anaerolineae bacterium SM23_84.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703388 {ECO:0000313|EMBL:KPL23137.1, ECO:0000313|Proteomes:UP000052016};
RN [1] {ECO:0000313|EMBL:KPL23137.1, ECO:0000313|Proteomes:UP000052016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_84 {ECO:0000313|EMBL:KPL23137.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPL23137.1}.
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; LJUZ01000059; KPL23137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8KMN4; -.
DR Proteomes; UP000052016; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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 NCBIfam; NF041097; keto_inos_dh_IolM; 1.
DR PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 36..382
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 384 AA; 41802 MW; AA8D73CF8491C3FB CRC64;
MKALLLDAEW EPREGYRLSD FERETGKAIT GSNVWRNPSL VIQELDKPTP RSDEVLIRVK
SCGVCGSDIH FYETDEEGYI LYPGLTKFPT ILGHEFSGVI EEVGSEVKDL VPGDMVTAEE
MIWCGHCTAC RNGFPNHCEN LEEIGFTIPG AFAEYIAVGA KYCWKISDYL DVFGSEEKAY
EVGALTEPTC VSYNAVFERA GGFRPGAYVT VFGTGPIGLA SVGLAEAAGA GKIIAFEISP
ERRELAQKVG ADHVFDPREV NPGEVIMELT GGQGADFHIE AAGAPQVTVA EMEKSMAING
KIVQIGRAAQ RVPMYLETFQ VRRSQFYGSQ GHSGHGTFPN VIRLVASGRL DLSPIITARY
SLDGVVEGIA ESGQRRHGKI MVKP
//
