ID A0A2N0Z493_9BACI Unreviewed; 380 AA.
AC A0A2N0Z493;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Glutathione-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:PKG24335.1};
GN ORFNames=CWS01_06875 {ECO:0000313|EMBL:PKG24335.1};
OS Niallia nealsonii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=115979 {ECO:0000313|EMBL:PKG24335.1, ECO:0000313|Proteomes:UP000233375};
RN [1] {ECO:0000313|EMBL:PKG24335.1, ECO:0000313|Proteomes:UP000233375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-92 {ECO:0000313|EMBL:PKG24335.1,
RC ECO:0000313|Proteomes:UP000233375};
RX PubMed=12656168; DOI=10.1099/ijs.0.02311-0;
RA Venkateswaran K., Kempf M., Chen F., Satomi M., Nicholson W., Kern R.;
RT "Bacillus nealsonii sp. nov., isolated from a spacecraft-assembly facility,
RT whose spores are gamma-radiation resistant.";
RL Int. J. Syst. Evol. Microbiol. 53:165-172(2003).
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:PKG24335.1}.
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DR EMBL; PISE01000014; PKG24335.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0Z493; -.
DR OrthoDB; 9769198at2; -.
DR Proteomes; UP000233375; 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 Reference proteome {ECO:0000313|Proteomes:UP000233375};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..145
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 191..262
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 380 AA; 42373 MW; 55184F7DA9F2F789 CRC64;
MKAVTYQGAK EIQVKQVEDP ILQKKDDIIV RITSTAICGS DLHIYLGAIP AQKDYVIGHE
PMGIVEEVGP DVTKVKKGDR VVLPFNISCG HCYYCEHDME SQCDNANPNK EQADTGAYFG
FTERYGNYPG GQAELLRVPY GNFVPFVIPE SCEIEDEGLL FMSDVLPTAY WSVENSGVKE
GDTVVVLGCG PVGLMTQKFA WMKGAKRVIA VDNIPYRLNH AKKMNNVEII NFDQHEDTGL
YMKEITKGGA DVVIDCVGMD GKKTMMEKVE QKLKIQGGTL SAIQIGLNSI RKFGTMQLTG
VYGSTYNMFP LGNIFERNIT VKTGQAPVIH YMPMLFDKIA NKEFDPTEII THKVPLDQAS
EAYKMFYEHE DDVIKVILKP
//
