ID   A0A2S0WUF9_9MICO        Unreviewed;       391 AA.
AC   A0A2S0WUF9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Glutathione-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:AWB94986.1};
GN   ORFNames=DCE93_04350 {ECO:0000313|EMBL:AWB94986.1};
OS   Agromyces badenianii.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agromyces.
OX   NCBI_TaxID=2080742 {ECO:0000313|EMBL:AWB94986.1, ECO:0000313|Proteomes:UP000244729};
RN   [1] {ECO:0000313|EMBL:AWB94986.1, ECO:0000313|Proteomes:UP000244729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30A {ECO:0000313|Proteomes:UP000244729};
RA   Li J.;
RL   Submitted (APR-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}.
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DR   EMBL; CP028913; AWB94986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S0WUF9; -.
DR   KEGG; agm:DCE93_04350; -.
DR   OrthoDB; 241504at2; -.
DR   Proteomes; UP000244729; Chromosome.
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   PANTHER; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 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:UP000244729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          26..139
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          189..255
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   391 AA;  41895 MW;  2695D57C391309CA CRC64;
     MRAVTWHSPR SVEVAEVPDP VPVEPTDAVV RVTSTAICGS DLHLYDVFGP FMHRGDILGH
     EAMGVVEAVG AAVRRVAVGD RVIVPFVIAC GACRMCARGL TTQCETTQNT EYGTGAMLYG
     YTELYGRVPG GQAEYLRVRL ADANATVVGR DLPDERYLFL TDVLPTAWQA MRYANVSPGD
     TLAVLGLGPI GQMVVRIAGH ENVRVIAVDP VAERRLMAER YGATTLDLDD AVLERIRELT
     QGRGADAVVD AVGLEAHGSP GAALAQNTVG ALPSAVAKPL MTKAGVDRLA ALHLAIEAVV
     RGGTVSVVGV YAGNLDPMPM MTIFDKQLTM RFGQANVQQW LPDLMPLAEA ESDPLGLEDF
     ATHRLPLARA PEMYEQFKQK TAGCIKVVLK P
//