ID A0A1I4SCG9_9BURK Unreviewed; 387 AA.
AC A0A1I4SCG9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Glutathione-independent formaldehyde dehydrogenase {ECO:0000313|EMBL:SFM62155.1};
GN ORFNames=SAMN05444747_10721 {ECO:0000313|EMBL:SFM62155.1};
OS Variovorax sp. OV329.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882825 {ECO:0000313|EMBL:SFM62155.1, ECO:0000313|Proteomes:UP000199688};
RN [1] {ECO:0000313|EMBL:SFM62155.1, ECO:0000313|Proteomes:UP000199688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV329 {ECO:0000313|EMBL:SFM62155.1,
RC ECO:0000313|Proteomes:UP000199688};
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; FOUG01000007; SFM62155.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4SCG9; -.
DR STRING; 1882825.SAMN05444747_10721; -.
DR OrthoDB; 9773078at2; -.
DR Proteomes; UP000199688; 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:UP000199688};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..151
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 197..284
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 387 AA; 41318 MW; 08DEC1F8F9DD5B7D CRC64;
MKALTYQGAK KVSVDTVPDP VLLADDDIVL RVTATAICGS DLHIYRGKIP AMKDGDILGH
EFMGVVEETG RAVSSLRKGD RVVVPFVIAC GQCFYCTKSL FAACEQTNDG RGAILNKKVS
TAGAGLFGYS HLYGGYAGGQ AEYVRVPKAD VGPIKIPDAL SDDQVLFLSD ILPTGYQAAV
NAQIEPGSSV AIFGAGPVGL MAALSARFLG AEKIFMVDHH PYRLRFAQQT YGVVPINFDE
DDDPAESILK ATQNHGVDAS IDAVGFEAKG SLLETTLAAL KLEGSSGKAL RQAMAATRRG
GIVSVPGVYA GFIHGFLFGD AFEKGLTFKM GQTHAQRFMP ELLGHIGEGK MKPEVIVSHR
MNLADAAKGY QIFNDKEDEC RKVILTP
//