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Database: UniProt
Entry: A0A1A0U0N5_9MYCO
LinkDB: A0A1A0U0N5_9MYCO
Original site: A0A1A0U0N5_9MYCO 
ID   A0A1A0U0N5_9MYCO        Unreviewed;       390 AA.
AC   A0A1A0U0N5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Glutathione-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:OBB64592.1};
GN   ORFNames=A5758_20350 {ECO:0000313|EMBL:OBB64592.1};
OS   Mycobacterium sp. 852014-50255_SCH5639931.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834112 {ECO:0000313|EMBL:OBB64592.1, ECO:0000313|Proteomes:UP000092113};
RN   [1] {ECO:0000313|EMBL:OBB64592.1, ECO:0000313|Proteomes:UP000092113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=852014-50255_SCH5639931 {ECO:0000313|EMBL:OBB64592.1,
RC   ECO:0000313|Proteomes:UP000092113};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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:OBB64592.1}.
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DR   EMBL; LZSV01000032; OBB64592.1; -; Genomic_DNA.
DR   RefSeq; WP_067206165.1; NZ_LZSV01000032.1.
DR   AlphaFoldDB; A0A1A0U0N5; -.
DR   STRING; 1834112.A5758_20350; -.
DR   OrthoDB; 241504at2; -.
DR   Proteomes; UP000092113; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   TRANSMEM        189..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          26..148
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          196..264
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   390 AA;  41974 MW;  3593CECDB6C81526 CRC64;
     MKATVWAGRN SVQVESVPDP KILNDRDAIV RITSTAICGS DLHLYDGYIP TVKHGDVLGH
     EFMGEVVEVG KAVNNLAIGD RVVVPFPIAC GACSACRRDL YSLCENSNPN AGIAEKFMGH
     SPAGLFGYSH MLGGFAGGQA EYARVPFADV GPLKIEDDLT DEQVLFLSDI LPTGYMGAEM
     CNITPGDVVA VWGAGPVGLF AIMSAFLLGA SKVIAVDRVP YRLELAKQIG ATPVNFAETS
     VLEELRDITA GRGPDHCIDA VGMEARSGSA PVDAYDRVKQ AARLETERPH AIREAAMSCR
     NGGTLSIVGV YGGLMDKFPI GAVMNRSLTI KTGQCHVHRY MRPLLDRIRN GDIDPTIVVS
     HHLSLDQAPH GYEIFKNKED RCTKVILNPT
//
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