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Database: UniProt
Entry: A0A176QF58_9MICO
LinkDB: A0A176QF58_9MICO
Original site: A0A176QF58_9MICO 
ID   A0A176QF58_9MICO        Unreviewed;       393 AA.
AC   A0A176QF58;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Glutathione-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:OAB88298.1};
GN   ORFNames=AWH69_00305 {ECO:0000313|EMBL:OAB88298.1};
OS   Janibacter melonis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=262209 {ECO:0000313|EMBL:OAB88298.1, ECO:0000313|Proteomes:UP000076976};
RN   [1] {ECO:0000313|EMBL:OAB88298.1, ECO:0000313|Proteomes:UP000076976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD11-4 {ECO:0000313|EMBL:OAB88298.1,
RC   ECO:0000313|Proteomes:UP000076976};
RA   Nair G.R., Kaur G., Chander A.M., Mayilraj S.;
RT   "Janibacter melonis strain CD11_4 genome sequencing and assembly.";
RL   Submitted (JAN-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}.
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:OAB88298.1}.
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DR   EMBL; LQZG01000001; OAB88298.1; -; Genomic_DNA.
DR   RefSeq; WP_068269810.1; NZ_QSNP01000069.1.
DR   AlphaFoldDB; A0A176QF58; -.
DR   STRING; 262209.AWH69_00305; -.
DR   Proteomes; UP000076976; 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; cd08283; FDH_like_1; 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: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   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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076976};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..391
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   393 AA;  42206 MW;  FF576C8C860FDCE7 CRC64;
     MRALTWQGTR DVQVVDVPDP RIQEPTDAVI KVTSTAICGS DLHLYEPLGP FLAQGDVLGH
     ETMGVVEEVG AEVTHIKPGD RVVIPFNISC GHCWMCRRGY TAQCETTQVT SQDKGASLFG
     YTELYGSVPG GQAEYLRVPQ AHFGPIKVPD GVPDERFLYL SDILPTAWQG VEWAEVSEGD
     TLAVFGLGPV GLLATRIARH RGIRVIGVDN VPERLAAAQA YGVEVLSTDD VDDIPSAIKD
     MTDGRGADGT LDAVGMEAHG TPVLGAAVKG AGLLPDAIAK PLIKKAGVDR LAALYDSIRS
     VRRGGTVSVS GVYGGQSDPM PMMEMFDRGI ALRMGQCHVR RWVDDIVPVL TDDADVFGVE
     TLATHRLPLE DAPHGYDIFQ KKEDGCIKVV LKP
//
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