ID A0A0Q8LN60_9MICO Unreviewed; 340 AA.
AC A0A0Q8LN60;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Molecular chaperone GroES {ECO:0000313|EMBL:KRB36816.1};
GN ORFNames=ASD93_12345 {ECO:0000313|EMBL:KRB36816.1};
OS Microbacterium sp. Root180.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736483 {ECO:0000313|EMBL:KRB36816.1, ECO:0000313|Proteomes:UP000050802};
RN [1] {ECO:0000313|EMBL:KRB36816.1, ECO:0000313|Proteomes:UP000050802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root180 {ECO:0000313|EMBL:KRB36816.1,
RC ECO:0000313|Proteomes:UP000050802};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB36816.1, ECO:0000313|Proteomes:UP000050802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root180 {ECO:0000313|EMBL:KRB36816.1,
RC ECO:0000313|Proteomes:UP000050802};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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|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:KRB36816.1}.
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DR EMBL; LMHS01000003; KRB36816.1; -; Genomic_DNA.
DR RefSeq; WP_056122948.1; NZ_LMHS01000003.1.
DR AlphaFoldDB; A0A0Q8LN60; -.
DR STRING; 1736483.ASD93_12345; -.
DR OrthoDB; 9797931at2; -.
DR Proteomes; UP000050802; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000050802};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..334
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 340 AA; 35723 MW; ECB51449DB92D13D CRC64;
MLTATYSGDR TIEVSEAEPS TPAPGQVQIA VAYTGLCGTD LHIFHGSMDA RVQTPLVFGH
EMSGTIAAVG EGVTGWAVGD GVTVMPLAWD GTCPACLAGN QHICQNLDFI GIDSPGSLQA
LWNVPAETLV RLPAGVALDH AALVEPVAVA VHDVRRANLQ PGDTAVVIGG GPIGVLIATV
ARHFGADVLV IELDEKRRAQ IEGLSFATLD PRARDQVAVV EEWTGGAGAD VVFEVSGAAQ
AVRGATSLAK VRGTIVVVAI HPTPREIDLQ RVFWRELSIL GARVYERRDF ETAVELVADG
VIPADLLITR IVPLSKTAEA FADLEAGRAM KILVDVAGQR
//
