ID A0A1M3BM44_9ACTN Unreviewed; 404 AA.
AC A0A1M3BM44;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Formaldehyde dehydrogenase, glutathione-independent {ECO:0000313|EMBL:OJU85386.1};
GN ORFNames=BGO11_07000 {ECO:0000313|EMBL:OJU85386.1};
OS Solirubrobacterales bacterium 70-9.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales.
OX NCBI_TaxID=1895833 {ECO:0000313|EMBL:OJU85386.1, ECO:0000313|Proteomes:UP000184118};
RN [1] {ECO:0000313|EMBL:OJU85386.1, ECO:0000313|Proteomes:UP000184118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-9 {ECO:0000313|EMBL:OJU85386.1};
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 -!- 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:OJU85386.1}.
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DR EMBL; MKSH01000037; OJU85386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3BM44; -.
DR Proteomes; UP000184118; 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; cd08282; PFDH_like; 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; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR014184; HCHO_DH_non_GSH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR02819; fdhA_non_GSH; 1.
DR PANTHER; PTHR42813:SF3; GLUTATHIONE-INDEPENDENT FORMALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 44..153
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 192..246
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|Pfam:PF01262"
SQ SEQUENCE 404 AA; 42344 MW; D6A28F5FA329333F CRC64;
MADNRGVAYM GTGKVEVQDI DYPAWEIKEG PGVPTESVGR ELPHGAIVKL VATNICGSDQ
HMVRGRTTAP EGLILGHEIT GEVVEVGPGV EFIEVGDLVS TPFNIACGRC RNCKERNTGV
CLNVNPAQPG GAYGYVDMGG WIGGQAEYVM VPYADWNLLK FPDKDQAMEK ILDLTMLSDI
FPTGYHGAVS AGVGTGSTVY VAGAGPVGLA AAHAAQLLGA AVVIVGDANE ERLEQARSFG
CETLNIDKGE IPDQIEGILG VPEVDCGVDA VGFEAKGHGP DAGEEPAVVL NALMDVTRAA
GRLGIPGLYV VEDPGAESDE AKEGSLALKL GAGWAKSLSF VTGQCPVMKY HRELMNAILN
DRCEIAKAVN ATVIRLDDAP EGYEDFDKGA AKKFVIDPHG LVAA
//