ID A0A1A2MQU2_9MYCO Unreviewed; 390 AA.
AC A0A1A2MQU2;
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:OBH05296.1};
GN ORFNames=A5695_07630 {ECO:0000313|EMBL:OBH05296.1};
OS Mycobacterium sp. E1747.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834128 {ECO:0000313|EMBL:OBH05296.1, ECO:0000313|Proteomes:UP000092218};
RN [1] {ECO:0000313|Proteomes:UP000092218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1747 {ECO:0000313|Proteomes:UP000092218};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Sam S., Sreng N.,
RA Him V., Kerleguer A., Cheng S.;
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:OBH05296.1}.
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DR EMBL; LZJI01000207; OBH05296.1; -; Genomic_DNA.
DR RefSeq; WP_068087409.1; NZ_LZJI01000207.1.
DR AlphaFoldDB; A0A1A2MQU2; -.
DR STRING; 1834128.A5695_07630; -.
DR OrthoDB; 241504at2; -.
DR Proteomes; UP000092218; 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 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
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; 41973 MW; A0074400D4626335 CRC64;
MKATVWAGRN SVQVESVPDP KILNDRDAIV RITSTAICGS DLHLYDGYIP TVKHGDVLGH
EFMGEVVEVG RGVNNLAVGD RVVVPFPIAC GACSACQRDL YSLCENSNPN AGVAEKFMGH
SPAGLFGYSH MLGGFAGGQA EYARVPFADV GPLKIEDDLT DEQVLFLSDI LPTGYMGAEM
CGITPGDIVA VWGAGPVGLF AIMSAYLLGA SKVIVVDRVP YRLELAQKIG AVPVNFAETS
VLEELRDLTA GRGPDHCIDA AGMEARSGSA PVDAYDRVKQ AVRLETERPH AIREAAMSCR
NGGTLSIIGV YGGLMDKFPI GAVMNRSLTI KTGQCHVHRY MRPLLERIRN GDIDPTIVVS
HHLTLDQAPH GYEIFKNKED RCTKVILNPT
//
