ID A0A0N1N9V1_9ACTN Unreviewed; 361 AA.
AC A0A0N1N9V1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Mycothiol-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:KPH99782.1};
GN ORFNames=OK006_1247 {ECO:0000313|EMBL:KPH99782.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPH99782.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPH99782.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPH99782.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-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:KPH99782.1}.
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DR EMBL; LJCU01000269; KPH99782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1N9V1; -.
DR PATRIC; fig|1592326.3.peg.10072; -.
DR Proteomes; UP000037912; 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; IPR017816; MycoS_dep_FDH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR03451; mycoS_dep_FDH; 1.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF19; RIBULOSE-5-PHOSPHATE REDUCTASE; 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..361
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 361 AA; 37363 MW; D721F8A6F9F67731 CRC64;
MAQEVRGVIA PGKNEPVRVE TIVVPDPGPG EAVVKIQACG VCHTDLHYKQ GGINDDFPFL
LGHEAAGIVE SVGDGVTDVA PGDFVVLNWR AVCGQCRACL RGRPWYCFNT HNAKQKMTLK
DGTELSPALG IGAFADKTLV AAGQCTKVDP AVSPAVAGLL GCGVMAGIGA ALNTGNVGRG
DSVAVIGCGG VGNAAIAGAR LAGAAKIIAV DIDDRKLTTA SKLGATHTVN STSTDPVEAI
QGLTGGFGAD VVIDAVGRPE TYKQAFYARD LAGTVVLVGV PTPEMKLELP LLDVFGRGGA
LKSSWYGDCL PSRDFPMLID LHLQGRLDLD AFVSETIALD GIEAAFERMH HGDVLRSVVV
L
//
