ID A0A1M3DCP2_9SPHN Unreviewed; 394 AA.
AC A0A1M3DCP2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glutathione-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:OJV32259.1};
GN ORFNames=BGO24_15890 {ECO:0000313|EMBL:OJV32259.1};
OS Sphingomonas sp. 67-36.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1895849 {ECO:0000313|EMBL:OJV32259.1, ECO:0000313|Proteomes:UP000183964};
RN [1] {ECO:0000313|EMBL:OJV32259.1, ECO:0000313|Proteomes:UP000183964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=67-36 {ECO:0000313|EMBL:OJV32259.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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:OJV32259.1}.
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DR EMBL; MKSU01000013; OJV32259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3DCP2; -.
DR STRING; 1895849.BGO24_15890; -.
DR Proteomes; UP000183964; 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 394 AA; 42769 MW; CEF2D89D6E705ADE CRC64;
MRALTWHGKH DVRIETVDDP EIINPRDAII KVTATAICGS DLHLYDGFIP TMQKGDILGH
EFMGEVVETG PASTLRKGER VVVPFTIACG NCYHCGKHQY SACDNGLPAD NQDIAQTLYG
QPMSGLFGYS HMTGGYSGGQ AEYVRVPFSD VGPIVIPDGV DDEEVLFLSD ILPTGWMAAE
NAGIEPGDIV AVWGCGPVGL FAVQSAFLMG ADRVIAIDHF PHRLELARKF GAETINFEES
KTYDALMEMT GGIGPDACID AVGLEAHGFF VDNVWDQIKA STFLGTDRAH SIRQAIIACR
KGGRVSMPAV YGGFIDKFPL GAFMEKGLTL KTGQTHVQHY MPGLLQAILD GKIDTTFLIS
HRLPLEEAPE GYRMFHDRQN EVTKVVLKPG LAAA
//
