ID K4QWS3_STRDJ Unreviewed; 361 AA.
AC K4QWS3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=S-(Hydroxymethyl)mycothiol dehydrogenase {ECO:0000313|EMBL:CCK25372.1};
DE EC=1.1.1.306 {ECO:0000313|EMBL:CCK25372.1};
GN ORFNames=BN159_0993 {ECO:0000313|EMBL:CCK25372.1};
OS Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK25372.1, ECO:0000313|Proteomes:UP000008043};
RN [1] {ECO:0000313|EMBL:CCK25372.1, ECO:0000313|Proteomes:UP000008043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC {ECO:0000313|Proteomes:UP000008043};
RX PubMed=23043000; DOI=10.1128/JB.01592-12;
RA Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA Pelzer S., Kalinowski J., Mack M.;
RT "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT heterologous production of the unique antibiotic roseoflavin.";
RL J. Bacteriol. 194:6818-6827(2012).
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}.
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DR EMBL; HE971709; CCK25372.1; -; Genomic_DNA.
DR RefSeq; WP_015655769.1; NC_020504.1.
DR AlphaFoldDB; K4QWS3; -.
DR STRING; 1214101.BN159_0993; -.
DR KEGG; sdv:BN159_0993; -.
DR PATRIC; fig|1214101.3.peg.1004; -.
DR eggNOG; COG1062; Bacteria.
DR HOGENOM; CLU_026673_14_1_11; -.
DR OrthoDB; 334894at2; -.
DR Proteomes; UP000008043; Chromosome.
DR GO; GO:0050607; F:mycothiol-dependent formaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:CCK25372.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008043};
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; 37861 MW; 27BE04246E2C2A62 CRC64;
MAQQVRGVIA PGKDEPVRVE TIVIPDPGPG EAVVRVQACG VCHTDLHYKQ GGISDEFPFL
LGHEAAGVVE SVGDGVTDVA PGDFVVLNWR AVCGRCRACL RGRPWYCFDT HNAEQRMTLT
DGTELSPALG IGAFAEKTLV AAGQCTKVDP AVSPQVAGLL GCGVMAGIGA AINTGQVGRG
DTVAVIGCGG VGDAAVAGAN LAGAAKIIAV DIDDRKLAMA RTMGATHTVN SRESDPVEAI
RELTGGFGAD VVIEAVGRPE TYKQAFYARD LAGTVVLVGV PTPEMKLELP LLDVFGRGGA
LKSSWYGDCL PSRDFPMLID LHLQGRLDLE AFVTETIELT DVEKAFERMH EGDVLRSVVV
L
//