ID   A0A495JN89_9ACTN        Unreviewed;       378 AA.
AC   A0A495JN89;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Glutathione-independent formaldehyde dehydrogenase {ECO:0000313|EMBL:RKR89834.1};
GN   ORFNames=BDK92_4193 {ECO:0000313|EMBL:RKR89834.1};
OS   Micromonospora pisi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=589240 {ECO:0000313|EMBL:RKR89834.1, ECO:0000313|Proteomes:UP000277671};
RN   [1] {ECO:0000313|EMBL:RKR89834.1, ECO:0000313|Proteomes:UP000277671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45175 {ECO:0000313|EMBL:RKR89834.1,
RC   ECO:0000313|Proteomes:UP000277671};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-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:RKR89834.1}.
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DR   EMBL; RBKT01000001; RKR89834.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495JN89; -.
DR   OrthoDB; 3399630at2; -.
DR   Proteomes; UP000277671; 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; cd08282; PFDH_like; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42813:SF3; GLUTATHIONE-INDEPENDENT FORMALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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; 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:UP000277671};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..374
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   378 AA;  40172 MW;  43A0C6D718216135 CRC64;
     MRAVVYHGAN NVTVENVEDP RIEDPNDVIL KITSTAICGS DLHMYEGRTK AQPGMVFGHE
     NMGIVTEVGP GVARVRKGDR VSIPFNVACG FCKNCFAGNT GFCLTVNPNF AGGAYGYAAM
     GPYRGGQAEY LRVPFADFNC LALPPGDELE DDFAMLADIF PTGYHGTALA DVRPGESVAV
     MGGGPVGLMA AYSAMLIGAA KVFVVDRVPG RLRLAESIGA IPIDFSKGDP VMQILDQTNG
     DGTDKGVDAV GYQAHGTGGE EQPALVLNSL VEIVRATGRI GVVGLYLPSD PGAPDEHSRH
     GELLFKAGKF FEKGQRMGTG QANVKAYNQQ LRDLIIAGRA KPGFVVSKRL SLEEAPDAYA
     RFDRREDGYS KVVLKPAA
//