ID   A0A2P8DII0_9ACTN        Unreviewed;       581 AA.
AC   A0A2P8DII0;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=S-(Hydroxymethyl)mycothiol dehydrogenase {ECO:0000313|EMBL:PSK97036.1};
GN   ORFNames=CLV63_10939 {ECO:0000313|EMBL:PSK97036.1};
OS   Murinocardiopsis flavida.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Murinocardiopsis.
OX   NCBI_TaxID=645275 {ECO:0000313|EMBL:PSK97036.1, ECO:0000313|Proteomes:UP000240542};
RN   [1] {ECO:0000313|EMBL:PSK97036.1, ECO:0000313|Proteomes:UP000240542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45312 {ECO:0000313|EMBL:PSK97036.1,
RC   ECO:0000313|Proteomes:UP000240542};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) 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:PSK97036.1}.
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DR   EMBL; PYGA01000009; PSK97036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8DII0; -.
DR   OrthoDB; 334894at2; -.
DR   Proteomes; UP000240542; 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; cd06262; metallo-hydrolase-like_MBL-fold; 1.
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   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 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; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR017816; MycoS_dep_FDH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
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   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 2.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 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|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240542};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          12..359
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   DOMAIN          394..560
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   581 AA;  60898 MW;  9E58EA46795886BF CRC64;
     MPQEVSAVIA RERNAPVEVT TIVVPDPGPG EAVVAVQACG VCHTDLHYRE GGISDEYPFL
     LGHEAAGVVE SVGEGVTDVA PGDFVVLNWR AVCGTCRACA RGRPWYCFDT HNAAQKMTLL
     DGTELTPALG IGAFAEKTLV ASGQCTKVDP RADPAVAGLL GCGIMAGLGA AINTGGVSRG
     DSVAVIGCGG VGDAAIAGAA LAGAGRIIAV DIDDRKLQTA RRFGATHTVD SSGTDPVAAI
     RELTGGNGAD VVIEAVGRPE TYEQAFYARD LAGTVVLVGV PTPEMRIDLP LLDVFGRGGS
     LKSSWYGDCL PSRDFPMLID LYLQGRLDLA GFVTERIPLD GVEEAFARMH RGDVLRSVVV
     DAANRTATDP PVAGVESLVT SGVFALDGGE WEVDNNVWIV GDDRRAIVID PAHDHEAIAR
     ALGDRELMAI VCTHAHNDHV NAAAALADLS DAPVPIMLHP DDAVLWHQTY PDREPDGPLV
     HGEVLQVGEV ELKVLHTPGH APGAVCLYAP KLGVVFSGDT LFQGGPGATG RSYSDFPTII
     DSIREHLLPL SDDTVVYTGH GPATTIGAER PHLAEWIERG H
//