ID   A0A1H0G4Z1_9ACTN        Unreviewed;       405 AA.
AC   A0A1H0G4Z1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Glutathione-independent formaldehyde dehydrogenase {ECO:0000313|EMBL:SDO01904.1};
GN   ORFNames=SAMN05428965_2434 {ECO:0000313|EMBL:SDO01904.1};
OS   Geodermatophilus sp. DSM 45219.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1881103 {ECO:0000313|EMBL:SDO01904.1, ECO:0000313|Proteomes:UP000198730};
RN   [1] {ECO:0000313|EMBL:SDO01904.1, ECO:0000313|Proteomes:UP000198730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45219 {ECO:0000313|EMBL:SDO01904.1,
RC   ECO:0000313|Proteomes:UP000198730};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNIQ01000003; SDO01904.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0G4Z1; -.
DR   STRING; 1881103.SAMN05428965_2434; -.
DR   OrthoDB; 241504at2; -.
DR   Proteomes; UP000198730; 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; IPR014184; HCHO_DH_non_GSH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR02819; fdhA_non_GSH; 1.
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   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   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          43..153
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          206..272
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   405 AA;  42443 MW;  3EEF50F599C250C5 CRC64;
     MAGNKAVMYM GPGKVEVADL DYPGLELKEG PGVNPANVGR KTPHGVILKT VSTNICGSDQ
     HMVRGRTTAP ERLVLGHEIT GEIIEKGSDV EFLQVGDIVS VPFNIACGRC RNCKEGKTGI
     CLNVNPDRPG SAYGYVDMGG WTGGQAEYVM VPYADWNCLK FPDRDQALAK IRDLTMLSDI
     FPTGYHGCVT AGVGTGSTVY IAGAGPVGLA AAASAQLLGA AVVIVGDLNA ERLAQARSFG
     CETVDVSQGD PKDQIAQILG EPEVDCGVDA VGFEARGHGK DAEREAPATV LNSLMDITRA
     GGALGIPGLY VTGDPGAADE AAKSGSLSIR LGLGWAKSHA FTTGQCPVMR YNRQLMMAIL
     HDRVQIAKAV NAEVIPLEDA PRGYAEFDQG AAKKYVLDPN GMIPA
//