ID A0A2E8EFS6_9ARCH Unreviewed; 376 AA.
AC A0A2E8EFS6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=CL673_07370 {ECO:0000313|EMBL:MBQ04507.1};
OS Candidatus Bathyarchaeota archaeon.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=2026714 {ECO:0000313|EMBL:MBQ04507.1, ECO:0000313|Proteomes:UP000230510};
RN [1] {ECO:0000313|Proteomes:UP000230510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Graham E.D., Heidelberg J.F.;
RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT Global Oceans.";
RL Submitted (SEP-2017) 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|ARBA:ARBA00008072, 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:MBQ04507.1}.
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DR EMBL; PBSW01000061; MBQ04507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2E8EFS6; -.
DR Proteomes; UP000230510; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR GO; GO:0051262; P:protein tetramerization; IEA:UniProt.
DR CDD; cd08231; MDR_TM0436_like; 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; 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 8..374
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 376 AA; 40691 MW; F691F0DD43D30E89 CRC64;
MVKASVLEDV GRLAVHDYPR PDVGEGTMLI DMELCGVCGT DIHLYGGNMK VPFPVIPGHE
FVGRIKEIGE GAEKMEAKGK YLAEDDLVAV VPGTNLFCGT CYFCRLLPHK PTYCTNRRVM
GVNLSSGEPP HLLGGWAEEV FVDAAHYFVY KIPDGVPAEV AVLTEPMAVS SRAIERAYSP
GIQTSIKGFR SDDSVVVQGA GPIGLLAIAT ARIAGAGRII AVDMVDDRLE IAEKLGADYV
IDMRSFTDRG SRVAEVKRLT SGIGADVVIE CAGVPAAFAE GIELTRRGGR FVEVGHYTDP
GNVEINPHTI CMKDVDILGS WAYPPAQFDT ALQFLERGMD DLPLTEIITH KFRVTNAARS
IETVRSRKGI KMVITP
//