ID A0A1G3JY50_9SPHN Unreviewed; 400 AA.
AC A0A1G3JY50;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glutathione-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:OHC98068.1};
GN ORFNames=A3H25_01570 {ECO:0000313|EMBL:OHC98068.1};
OS Sphingomonadales bacterium RIFCSPLOWO2_12_FULL_63_15.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX NCBI_TaxID=1802170 {ECO:0000313|EMBL:OHC98068.1, ECO:0000313|Proteomes:UP000176465};
RN [1] {ECO:0000313|EMBL:OHC98068.1, ECO:0000313|Proteomes:UP000176465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OHC98068.1}.
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DR EMBL; MIAK01000038; OHC98068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3JY50; -.
DR Proteomes; UP000176465; 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..150
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 197..265
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 400 AA; 43287 MW; 82E112969722154C CRC64;
MRALTWHGKH DVRVDTVDDP EILNPRDAII KITSTAICGS DLHLYDGYIP TMKAGDILGH
EFMGEVVETG PGSTLKKGQR VVVPFTIACG SCYHCGKHQY SACDNGNPAD NQDIGQEMYG
QPMSGLFGYS HLTGGYAGGQ AEYVRVPFSD VGPIVVPDGL TDEQVLFLSD ILPTGWQAAE
NADIEPGDTV AVWGCGPVGL FAVQSAFLMG AHRVIAIDHF PHRLELARRF GAETINFEES
KTYEALMEMT GGIGPDAVID AVGLEAHGFF VDNVVDQIKA SLFLGTDRIH SIRQAIHACR
KGGRVSMPAV YGGFVDKFPL GAFMEKGLTL KTGQTSVQHY MPALLNAIVE GQIDTTFLIS
HRMSLEDAPK GYKMFHDNQN EVTKIVLKPD FAPSSAIAAE
//
