ID A0A1M3BNX6_9ACTN Unreviewed; 369 AA.
AC A0A1M3BNX6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=S-(Hydroxymethyl)glutathione dehydrogenase {ECO:0000313|EMBL:OJU86093.1};
GN ORFNames=BGO11_04755 {ECO:0000313|EMBL:OJU86093.1};
OS Solirubrobacterales bacterium 70-9.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales.
OX NCBI_TaxID=1895833 {ECO:0000313|EMBL:OJU86093.1, ECO:0000313|Proteomes:UP000184118};
RN [1] {ECO:0000313|EMBL:OJU86093.1, ECO:0000313|Proteomes:UP000184118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-9 {ECO:0000313|EMBL:OJU86093.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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|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:OJU86093.1}.
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DR EMBL; MKSH01000012; OJU86093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3BNX6; -.
DR Proteomes; UP000184118; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 12..217
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 369 AA; 38654 MW; D173149DE305C64E CRC64;
MKIRAAVLEE FGQPLAVQEV ELAEPRAGEV LVRLEACGVC HTDLYTASGA DPSGYAPAVL
GHEGAGVVEK VGEGVGSVAP GDHVVTLFSP QCRECVHCVD PRTNLCMAIR AEQNLGHLPD
GSVRLSRGGE DIRHFMGCST FAEYTVMPEI ALAKVNPEAP FEHIALFACG LSTGLGAAIN
TAAVEPGTTC VIFGAGMVGL GAVAGCRLQG AERIICVDMS EDRLQLAKGQ GATDTMIGGP
DAVQQILAMT DGEFGADYSF EATGNVKVMQ QALEATRMAW GLCTVAGVAG KGETLDVVPR
LLITGRRVAG SSFGGVKGRD QVPVLIERAM AGEIDVAPFI SHKITLDEVN RGFELMEAQD
GIRSVIEFN
//
